CA2595959A1 - Methods for treating renal cell carcinoma - Google Patents
Methods for treating renal cell carcinoma Download PDFInfo
- Publication number
- CA2595959A1 CA2595959A1 CA002595959A CA2595959A CA2595959A1 CA 2595959 A1 CA2595959 A1 CA 2595959A1 CA 002595959 A CA002595959 A CA 002595959A CA 2595959 A CA2595959 A CA 2595959A CA 2595959 A1 CA2595959 A1 CA 2595959A1
- Authority
- CA
- Canada
- Prior art keywords
- des
- weeks
- administering
- dose
- amino acid
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 98
- 208000006265 Renal cell carcinoma Diseases 0.000 title claims abstract description 31
- 108010002350 Interleukin-2 Proteins 0.000 claims abstract description 41
- 230000000694 effects Effects 0.000 claims abstract description 28
- 230000001771 impaired effect Effects 0.000 claims abstract description 27
- 230000004044 response Effects 0.000 claims description 61
- 238000011282 treatment Methods 0.000 claims description 61
- 102000000588 Interleukin-2 Human genes 0.000 claims description 38
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 claims description 32
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 30
- 206010028980 Neoplasm Diseases 0.000 claims description 29
- 230000036961 partial effect Effects 0.000 claims description 23
- 229920001223 polyethylene glycol Polymers 0.000 claims description 16
- 239000002202 Polyethylene glycol Substances 0.000 claims description 15
- 108700025316 aldesleukin Proteins 0.000 claims description 14
- 241000282414 Homo sapiens Species 0.000 claims description 12
- 239000003814 drug Substances 0.000 claims description 11
- 229920001583 poly(oxyethylated polyols) Polymers 0.000 claims description 10
- 206010061289 metastatic neoplasm Diseases 0.000 claims description 8
- 238000007920 subcutaneous administration Methods 0.000 claims description 8
- 150000002314 glycerols Polymers 0.000 claims description 5
- 238000007912 intraperitoneal administration Methods 0.000 claims description 5
- 238000001990 intravenous administration Methods 0.000 claims description 4
- 230000002685 pulmonary effect Effects 0.000 claims description 4
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Polymers OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 claims description 3
- 229960005310 aldesleukin Drugs 0.000 claims description 3
- 102000055277 human IL2 Human genes 0.000 claims description 3
- 238000001802 infusion Methods 0.000 claims description 3
- 230000001394 metastastic effect Effects 0.000 claims description 3
- 239000000829 suppository Substances 0.000 claims description 3
- 230000000699 topical effect Effects 0.000 claims description 3
- FBPFZTCFMRRESA-NQAPHZHOSA-N Sorbitol Polymers OCC(O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-NQAPHZHOSA-N 0.000 claims description 2
- 150000002303 glucose derivatives Polymers 0.000 claims description 2
- 150000002304 glucoses Polymers 0.000 claims description 2
- 125000002791 glucosyl group Polymers C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims description 2
- 238000007918 intramuscular administration Methods 0.000 claims description 2
- 238000004519 manufacturing process Methods 0.000 claims 1
- 238000002560 therapeutic procedure Methods 0.000 abstract description 29
- 206010050513 Metastatic renal cell carcinoma Diseases 0.000 abstract description 12
- 231100000419 toxicity Toxicity 0.000 abstract description 12
- 230000001988 toxicity Effects 0.000 abstract description 12
- 230000002411 adverse Effects 0.000 abstract description 10
- 230000002829 reductive effect Effects 0.000 abstract description 9
- 230000004614 tumor growth Effects 0.000 abstract description 5
- 238000011285 therapeutic regimen Methods 0.000 abstract description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 55
- 102000004196 processed proteins & peptides Human genes 0.000 description 52
- 229920001184 polypeptide Polymers 0.000 description 51
- 239000000203 mixture Substances 0.000 description 46
- 108090000623 proteins and genes Proteins 0.000 description 30
- 235000001014 amino acid Nutrition 0.000 description 29
- 201000010099 disease Diseases 0.000 description 29
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 29
- 235000018102 proteins Nutrition 0.000 description 26
- 102000004169 proteins and genes Human genes 0.000 description 26
- 229940024606 amino acid Drugs 0.000 description 24
- 230000003902 lesion Effects 0.000 description 24
- 239000002243 precursor Substances 0.000 description 24
- 230000004083 survival effect Effects 0.000 description 24
- 239000008194 pharmaceutical composition Substances 0.000 description 23
- 238000006467 substitution reaction Methods 0.000 description 23
- 150000001413 amino acids Chemical class 0.000 description 22
- 239000002253 acid Substances 0.000 description 21
- 238000013059 nephrectomy Methods 0.000 description 15
- 239000007788 liquid Substances 0.000 description 14
- 229940087463 proleukin Drugs 0.000 description 14
- 125000000539 amino acid group Chemical group 0.000 description 13
- 238000009472 formulation Methods 0.000 description 13
- 230000004071 biological effect Effects 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 150000003839 salts Chemical group 0.000 description 11
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 10
- 206010062237 Renal impairment Diseases 0.000 description 10
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 230000003907 kidney function Effects 0.000 description 10
- 231100000857 poor renal function Toxicity 0.000 description 10
- 230000000259 anti-tumor effect Effects 0.000 description 9
- 102000040430 polynucleotide Human genes 0.000 description 9
- 108091033319 polynucleotide Proteins 0.000 description 9
- 239000002157 polynucleotide Substances 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 8
- 230000007423 decrease Effects 0.000 description 8
- 229940079593 drug Drugs 0.000 description 8
- 230000009467 reduction Effects 0.000 description 8
- 235000004279 alanine Nutrition 0.000 description 7
- 201000011510 cancer Diseases 0.000 description 7
- 238000012217 deletion Methods 0.000 description 7
- 230000037430 deletion Effects 0.000 description 7
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 6
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 6
- 102220589633 RING finger protein 37_L40R_mutation Human genes 0.000 description 6
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- 229930182817 methionine Natural products 0.000 description 6
- 239000002773 nucleotide Substances 0.000 description 6
- 239000012071 phase Substances 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 239000004471 Glycine Substances 0.000 description 5
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 5
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 5
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 5
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 5
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 238000002512 chemotherapy Methods 0.000 description 5
- 229940109239 creatinine Drugs 0.000 description 5
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 5
- 230000034994 death Effects 0.000 description 5
- 231100000517 death Toxicity 0.000 description 5
- 229960000310 isoleucine Drugs 0.000 description 5
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 5
- 231100000417 nephrotoxicity Toxicity 0.000 description 5
- 125000003729 nucleotide group Chemical group 0.000 description 5
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 5
- 208000037821 progressive disease Diseases 0.000 description 5
- 239000003381 stabilizer Substances 0.000 description 5
- 238000003860 storage Methods 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 230000004797 therapeutic response Effects 0.000 description 5
- 239000004474 valine Substances 0.000 description 5
- 235000014393 valine Nutrition 0.000 description 5
- 239000004475 Arginine Substances 0.000 description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- 206010029155 Nephropathy toxic Diseases 0.000 description 4
- 206010037660 Pyrexia Diseases 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 4
- 235000009697 arginine Nutrition 0.000 description 4
- 238000003556 assay Methods 0.000 description 4
- 239000002585 base Substances 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 239000006172 buffering agent Substances 0.000 description 4
- 239000004067 bulking agent Substances 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 235000018417 cysteine Nutrition 0.000 description 4
- 230000002349 favourable effect Effects 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 235000018977 lysine Nutrition 0.000 description 4
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 4
- 230000007694 nephrotoxicity Effects 0.000 description 4
- 102000039446 nucleic acids Human genes 0.000 description 4
- 108020004707 nucleic acids Proteins 0.000 description 4
- 150000007523 nucleic acids Chemical class 0.000 description 4
- 235000000346 sugar Nutrition 0.000 description 4
- 238000013268 sustained release Methods 0.000 description 4
- 239000012730 sustained-release form Substances 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 102220497102 5-hydroxytryptamine receptor 3B_P65V_mutation Human genes 0.000 description 3
- 102220504866 Aladin_L40S_mutation Human genes 0.000 description 3
- 102220619065 Alpha-1,3-galactosyltransferase 2_R81E_mutation Human genes 0.000 description 3
- 102220465452 Angiogenin_K64Q_mutation Human genes 0.000 description 3
- 102220624991 Bcl-2-like protein 2_H79N_mutation Human genes 0.000 description 3
- 102220638992 Beta-enolase_H16D_mutation Human genes 0.000 description 3
- 102220638985 Beta-enolase_H16E_mutation Human genes 0.000 description 3
- 102220595179 Casein kinase II subunit alpha'-interacting protein_F78W_mutation Human genes 0.000 description 3
- 241001227713 Chiron Species 0.000 description 3
- 102220603939 Clathrin heavy chain 1_P65N_mutation Human genes 0.000 description 3
- 102220581530 DNA dC->dU-editing enzyme APOBEC-3G_E67A_mutation Human genes 0.000 description 3
- 108700004922 F42A Proteins 0.000 description 3
- 102220630762 Fibrinogen alpha chain_R38N_mutation Human genes 0.000 description 3
- 102220630764 Fibrinogen alpha chain_R38S_mutation Human genes 0.000 description 3
- 102220571087 Growth arrest and DNA damage-inducible protein GADD45 gamma_L80E_mutation Human genes 0.000 description 3
- 101001127203 Homo sapiens 60S ribosomal protein L36a Proteins 0.000 description 3
- 208000001953 Hypotension Diseases 0.000 description 3
- 102220524218 Interferon regulatory factor 6_N88H_mutation Human genes 0.000 description 3
- 102220511586 Kappa-casein_D84R_mutation Human genes 0.000 description 3
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 3
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 3
- 102220617354 Leucine-rich repeat-containing protein 34_V91W_mutation Human genes 0.000 description 3
- 206010027476 Metastases Diseases 0.000 description 3
- 102220548801 Mitochondrial import inner membrane translocase subunit TIM16_L94A_mutation Human genes 0.000 description 3
- 102220570925 N-acetylgalactosamine-6-sulfatase_L36P_mutation Human genes 0.000 description 3
- 206010028813 Nausea Diseases 0.000 description 3
- 102220592496 Non-homologous end-joining factor 1_Q11A_mutation Human genes 0.000 description 3
- 102220546836 Nuclear pore complex protein Nup85_L19D_mutation Human genes 0.000 description 3
- 102220624881 PDZ and LIM domain protein 2_L80K_mutation Human genes 0.000 description 3
- 102220529451 Phorbol-12-myristate-13-acetate-induced protein 1_L36E_mutation Human genes 0.000 description 3
- 102220552473 Platelet-activating factor acetylhydrolase_K64D_mutation Human genes 0.000 description 3
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 3
- 102220550572 Proteasome maturation protein_L19E_mutation Human genes 0.000 description 3
- 102220471703 Proteasome subunit alpha type-7_K32A_mutation Human genes 0.000 description 3
- 102220511395 Proteasome subunit beta type-10_K35T_mutation Human genes 0.000 description 3
- 102220519967 Protein DEK_L66A_mutation Human genes 0.000 description 3
- 102220538345 Putative stereocilin-like protein_K35M_mutation Human genes 0.000 description 3
- 102220495631 Putative uncharacterized protein LOC645739_F42A_mutation Human genes 0.000 description 3
- 102220471503 Replication factor C subunit 4_R38D_mutation Human genes 0.000 description 3
- 102220547809 Serine/threonine-protein kinase B-raf_N88T_mutation Human genes 0.000 description 3
- 102220560185 Stromal cell-derived factor 1_K64R_mutation Human genes 0.000 description 3
- 102220559239 Voltage-dependent L-type calcium channel subunit alpha-1C_L36A_mutation Human genes 0.000 description 3
- 102220559240 Voltage-dependent L-type calcium channel subunit alpha-1C_P34S_mutation Human genes 0.000 description 3
- 206010047700 Vomiting Diseases 0.000 description 3
- 102220618307 YLP motif-containing protein 1_F42E_mutation Human genes 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 230000004075 alteration Effects 0.000 description 3
- 208000022531 anorexia Diseases 0.000 description 3
- 229940009098 aspartate Drugs 0.000 description 3
- 235000003704 aspartic acid Nutrition 0.000 description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 102220370481 c.101C>G Human genes 0.000 description 3
- 102220345545 c.103A>C Human genes 0.000 description 3
- 102220431680 c.124T>G Human genes 0.000 description 3
- 102220350876 c.190A>G Human genes 0.000 description 3
- 102220420188 c.193C>A Human genes 0.000 description 3
- 102220359607 c.194C>A Human genes 0.000 description 3
- 102220349468 c.194C>T Human genes 0.000 description 3
- 102220427208 c.233T>C Human genes 0.000 description 3
- 102220353454 c.262A>G Human genes 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000002591 computed tomography Methods 0.000 description 3
- 206010061428 decreased appetite Diseases 0.000 description 3
- 229960001484 edetic acid Drugs 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 230000027950 fever generation Effects 0.000 description 3
- 238000004108 freeze drying Methods 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 238000002595 magnetic resonance imaging Methods 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- PSGAAPLEWMOORI-PEINSRQWSA-N medroxyprogesterone acetate Chemical compound C([C@@]12C)CC(=O)C=C1[C@@H](C)C[C@@H]1[C@@H]2CC[C@]2(C)[C@@](OC(C)=O)(C(C)=O)CC[C@H]21 PSGAAPLEWMOORI-PEINSRQWSA-N 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 210000000822 natural killer cell Anatomy 0.000 description 3
- 230000008693 nausea Effects 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 239000000902 placebo Substances 0.000 description 3
- 229940068196 placebo Drugs 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 102220004796 rs104893939 Human genes 0.000 description 3
- 102220223852 rs1060502978 Human genes 0.000 description 3
- 102220234588 rs1114167484 Human genes 0.000 description 3
- 102220234204 rs1114167734 Human genes 0.000 description 3
- 102220110995 rs115116507 Human genes 0.000 description 3
- 102200081185 rs121909273 Human genes 0.000 description 3
- 102200042537 rs121909608 Human genes 0.000 description 3
- 102200115315 rs121918084 Human genes 0.000 description 3
- 102220322294 rs1554831400 Human genes 0.000 description 3
- 102220242995 rs1555187010 Human genes 0.000 description 3
- 102220266103 rs199901239 Human genes 0.000 description 3
- 102200136470 rs35114462 Human genes 0.000 description 3
- 102200158049 rs387906619 Human genes 0.000 description 3
- 102220039997 rs587778128 Human genes 0.000 description 3
- 102220056637 rs730880955 Human genes 0.000 description 3
- 102220058220 rs730881937 Human genes 0.000 description 3
- 102200080011 rs755832705 Human genes 0.000 description 3
- 102220097736 rs774586397 Human genes 0.000 description 3
- 102220062242 rs786201968 Human genes 0.000 description 3
- 102200076864 rs869312138 Human genes 0.000 description 3
- 102220098003 rs876661384 Human genes 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 230000002792 vascular Effects 0.000 description 3
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000030939 Bubalus bubalis Species 0.000 description 2
- 101100049641 Caenorhabditis elegans pfs-2 gene Proteins 0.000 description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 201000004624 Dermatitis Diseases 0.000 description 2
- 206010061818 Disease progression Diseases 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- 102220515709 Interferon regulatory factor 8_R81K_mutation Human genes 0.000 description 2
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 2
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 241000282567 Macaca fascicularis Species 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 101001043827 Mus musculus Interleukin-2 Proteins 0.000 description 2
- 241000699667 Mus spretus Species 0.000 description 2
- 208000000112 Myalgia Diseases 0.000 description 2
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 2
- 102220602029 Neutrophil elastase_R81P_mutation Human genes 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 241000283283 Orcinus orca Species 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 241000282516 Papio anubis Species 0.000 description 2
- 108010043958 Peptoids Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 229920000037 Polyproline Polymers 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 241000282898 Sus scrofa Species 0.000 description 2
- 102220500923 Telomerase reverse transcriptase_K35D_mutation Human genes 0.000 description 2
- 102220610852 Thialysine N-epsilon-acetyltransferase_L72G_mutation Human genes 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 235000009582 asparagine Nutrition 0.000 description 2
- 229960001230 asparagine Drugs 0.000 description 2
- 230000003190 augmentative effect Effects 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000012876 carrier material Substances 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 230000008034 disappearance Effects 0.000 description 2
- 230000005750 disease progression Effects 0.000 description 2
- 229940000406 drug candidate Drugs 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- -1 for example Chemical class 0.000 description 2
- 229930195712 glutamate Natural products 0.000 description 2
- 235000013922 glutamic acid Nutrition 0.000 description 2
- 239000004220 glutamic acid Substances 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 235000004554 glutamine Nutrition 0.000 description 2
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 2
- 229920001519 homopolymer Polymers 0.000 description 2
- 230000003054 hormonal effect Effects 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 230000036543 hypotension Effects 0.000 description 2
- 210000003810 lymphokine-activated killer cell Anatomy 0.000 description 2
- 239000008176 lyophilized powder Substances 0.000 description 2
- 230000007434 lytic lesion Effects 0.000 description 2
- 230000003211 malignant effect Effects 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 230000001613 neoplastic effect Effects 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 230000026731 phosphorylation Effects 0.000 description 2
- 238000006366 phosphorylation reaction Methods 0.000 description 2
- 108010026466 polyproline Proteins 0.000 description 2
- 238000010837 poor prognosis Methods 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 102220197507 rs1057519494 Human genes 0.000 description 2
- 102220223535 rs1060501767 Human genes 0.000 description 2
- 102220234844 rs1131690927 Human genes 0.000 description 2
- 102200000390 rs121917859 Human genes 0.000 description 2
- 102220295568 rs1554341697 Human genes 0.000 description 2
- 102220320766 rs1554448978 Human genes 0.000 description 2
- 102200066678 rs1554618767 Human genes 0.000 description 2
- 102220250393 rs553900705 Human genes 0.000 description 2
- 238000010845 search algorithm Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000001694 spray drying Methods 0.000 description 2
- 238000013517 stratification Methods 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 208000011580 syndromic disease Diseases 0.000 description 2
- 229940124597 therapeutic agent Drugs 0.000 description 2
- 238000011269 treatment regimen Methods 0.000 description 2
- 210000003171 tumor-infiltrating lymphocyte Anatomy 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- 230000009452 underexpressoin Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- YUXKOWPNKJSTPQ-AXWWPMSFSA-N (2s,3r)-2-amino-3-hydroxybutanoic acid;(2s)-2-amino-3-hydroxypropanoic acid Chemical compound OC[C@H](N)C(O)=O.C[C@@H](O)[C@H](N)C(O)=O YUXKOWPNKJSTPQ-AXWWPMSFSA-N 0.000 description 1
- PXFBZOLANLWPMH-UHFFFAOYSA-N 16-Epiaffinine Natural products C1C(C2=CC=CC=C2N2)=C2C(=O)CC2C(=CC)CN(C)C1C2CO PXFBZOLANLWPMH-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 101100060192 Anopheles gambiae ser4 gene Proteins 0.000 description 1
- 241001133287 Artocarpus hirsutus Species 0.000 description 1
- 241001422755 Atys Species 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 206010061728 Bone lesion Diseases 0.000 description 1
- 206010006002 Bone pain Diseases 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 201000005488 Capillary Leak Syndrome Diseases 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 241000282691 Cercocebus Species 0.000 description 1
- 241000282556 Cercocebus atys Species 0.000 description 1
- 241000282985 Cervus Species 0.000 description 1
- 241000283026 Cervus elaphus Species 0.000 description 1
- 206010011224 Cough Diseases 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 241000484025 Cuniculus Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 description 1
- 208000000059 Dyspnea Diseases 0.000 description 1
- 206010013975 Dyspnoeas Diseases 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 101001002658 Equus caballus Interleukin-2 Proteins 0.000 description 1
- 206010015150 Erythema Diseases 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 102220597417 Fizzy-related protein homolog_R81L_mutation Human genes 0.000 description 1
- 241000699694 Gerbillinae Species 0.000 description 1
- 102220485773 Glycophorin-A_L94I_mutation Human genes 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 241000282620 Hylobates sp. Species 0.000 description 1
- 208000037147 Hypercalcaemia Diseases 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 206010061218 Inflammation Diseases 0.000 description 1
- 206010022095 Injection Site reaction Diseases 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 206010025323 Lymphomas Diseases 0.000 description 1
- 241000282553 Macaca Species 0.000 description 1
- 241000282560 Macaca mulatta Species 0.000 description 1
- 241000699696 Meriones Species 0.000 description 1
- 206010027480 Metastatic malignant melanoma Diseases 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241001024304 Mino Species 0.000 description 1
- 241000283128 Mirounga angustirostris Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101000931108 Mus musculus DNA (cytosine-5)-methyltransferase 1 Proteins 0.000 description 1
- ONYFNWIHJBLQKE-ZETCQYMHSA-N N(6)-acetimidoyl-L-lysine Chemical compound CC(=N)NCCCC[C@H](N)C(O)=O ONYFNWIHJBLQKE-ZETCQYMHSA-N 0.000 description 1
- 108010049175 N-substituted Glycines Proteins 0.000 description 1
- 206010061309 Neoplasm progression Diseases 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 206010030113 Oedema Diseases 0.000 description 1
- 240000008881 Oenanthe javanica Species 0.000 description 1
- 101001043815 Ovis aries Interleukin-2 Proteins 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- MUPFEKGTMRGPLJ-RMMQSMQOSA-N Raffinose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 MUPFEKGTMRGPLJ-RMMQSMQOSA-N 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 101001043830 Rattus norvegicus Interleukin-2 Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 241000282696 Saimiri sciureus Species 0.000 description 1
- 208000032023 Signs and Symptoms Diseases 0.000 description 1
- 208000013738 Sleep Initiation and Maintenance disease Diseases 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- UQZIYBXSHAGNOE-USOSMYMVSA-N Stachyose Natural products O(C[C@H]1[C@@H](O)[C@H](O)[C@H](O)[C@@H](O[C@@]2(CO)[C@H](O)[C@@H](O)[C@@H](CO)O2)O1)[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@H](CO[C@@H]2[C@@H](O)[C@@H](O)[C@@H](O)[C@H](CO)O2)O1 UQZIYBXSHAGNOE-USOSMYMVSA-N 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-N Succinic acid Natural products OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 1
- 101001043834 Sus scrofa Interleukin-2 Proteins 0.000 description 1
- 208000031932 Systemic capillary leak syndrome Diseases 0.000 description 1
- 230000006052 T cell proliferation Effects 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- ATJFFYVFTNAWJD-UHFFFAOYSA-N Tin Chemical compound [Sn] ATJFFYVFTNAWJD-UHFFFAOYSA-N 0.000 description 1
- HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
- MUPFEKGTMRGPLJ-UHFFFAOYSA-N UNPD196149 Natural products OC1C(O)C(CO)OC1(CO)OC1C(O)C(O)C(O)C(COC2C(C(O)C(O)C(CO)O2)O)O1 MUPFEKGTMRGPLJ-UHFFFAOYSA-N 0.000 description 1
- 102220559056 Voltage-dependent L-type calcium channel subunit alpha-1C_L36I_mutation Human genes 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 150000008043 acidic salts Chemical class 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 238000007605 air drying Methods 0.000 description 1
- 150000001447 alkali salts Chemical class 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-L aspartate group Chemical group N[C@@H](CC(=O)[O-])C(=O)[O-] CKLJMWTZIZZHCS-REOHCLBHSA-L 0.000 description 1
- 230000003416 augmentation Effects 0.000 description 1
- 239000003124 biologic agent Substances 0.000 description 1
- 238000004820 blood count Methods 0.000 description 1
- 230000036765 blood level Effects 0.000 description 1
- KDYFGRWQOYBRFD-NUQCWPJISA-N butanedioic acid Chemical compound O[14C](=O)CC[14C](O)=O KDYFGRWQOYBRFD-NUQCWPJISA-N 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- CCGSUNCLSOWKJO-UHFFFAOYSA-N cimetidine Chemical group N#CNC(=N/C)\NCCSCC1=NC=N[C]1C CCGSUNCLSOWKJO-UHFFFAOYSA-N 0.000 description 1
- 229960001380 cimetidine Drugs 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 229940127089 cytotoxic agent Drugs 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000011026 diafiltration Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000003467 diminishing effect Effects 0.000 description 1
- 235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 231100000321 erythema Toxicity 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000012458 free base Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000014509 gene expression Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000024924 glomerular filtration Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000003630 glycyl group Chemical class [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 231100001156 grade 3 toxicity Toxicity 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000019622 heart disease Diseases 0.000 description 1
- 231100000171 higher toxicity Toxicity 0.000 description 1
- 230000002962 histologic effect Effects 0.000 description 1
- 238000001794 hormone therapy Methods 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000000148 hypercalcaemia Effects 0.000 description 1
- 208000030915 hypercalcemia disease Diseases 0.000 description 1
- 230000009610 hypersensitivity Effects 0.000 description 1
- 125000001841 imino group Chemical group [H]N=* 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000001976 improved effect Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000008595 infiltration Effects 0.000 description 1
- 238000001764 infiltration Methods 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 206010022437 insomnia Diseases 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 238000013332 literature search Methods 0.000 description 1
- 238000007477 logistic regression Methods 0.000 description 1
- 210000003141 lower extremity Anatomy 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229960004616 medroxyprogesterone Drugs 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 208000021039 metastatic melanoma Diseases 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000003589 nefrotoxic effect Effects 0.000 description 1
- 210000005170 neoplastic cell Anatomy 0.000 description 1
- 231100000381 nephrotoxic Toxicity 0.000 description 1
- 230000000926 neurological effect Effects 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229940068968 polysorbate 80 Drugs 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000000770 proinflammatory effect Effects 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 238000007409 radiographic assessment Methods 0.000 description 1
- 238000001959 radiotherapy Methods 0.000 description 1
- MUPFEKGTMRGPLJ-ZQSKZDJDSA-N raffinose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O2)O)O1 MUPFEKGTMRGPLJ-ZQSKZDJDSA-N 0.000 description 1
- 238000002271 resection Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 102200100726 rs61752874 Human genes 0.000 description 1
- 102220097967 rs876660873 Human genes 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000012883 sequential measurement Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 206010040882 skin lesion Diseases 0.000 description 1
- 231100000444 skin lesion Toxicity 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- UQZIYBXSHAGNOE-XNSRJBNMSA-N stachyose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO[C@@H]2[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO[C@@H]3[C@@H]([C@@H](O)[C@@H](O)[C@@H](CO)O3)O)O2)O)O1 UQZIYBXSHAGNOE-XNSRJBNMSA-N 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 238000001356 surgical procedure Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 238000009121 systemic therapy Methods 0.000 description 1
- 229950001699 teceleukin Drugs 0.000 description 1
- 238000003325 tomography Methods 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000005751 tumor progression Effects 0.000 description 1
- 229960003048 vinblastine Drugs 0.000 description 1
- JXLYSJRDGCGARV-XQKSVPLYSA-N vincaleukoblastine Chemical compound C([C@@H](C[C@]1(C(=O)OC)C=2C(=CC3=C([C@]45[C@H]([C@@]([C@H](OC(C)=O)[C@]6(CC)C=CCN([C@H]56)CC4)(O)C(=O)OC)N3C)C=2)OC)C[C@@](C2)(O)CC)N2CCC2=C1NC1=CC=CC=C21 JXLYSJRDGCGARV-XQKSVPLYSA-N 0.000 description 1
- 230000008673 vomiting Effects 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A61K38/20—Interleukins [IL]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A61K38/20—Interleukins [IL]
- A61K38/2013—IL-2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/56—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule
- A61K47/59—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes
- A61K47/60—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an organic macromolecular compound, e.g. an oligomeric, polymeric or dendrimeric molecule obtained otherwise than by reactions only involving carbon-to-carbon unsaturated bonds, e.g. polyureas or polyurethanes the organic macromolecular compound being a polyoxyalkylene oligomer, polymer or dendrimer, e.g. PEG, PPG, PEO or polyglycerol
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/04—Antineoplastic agents specific for metastasis
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Public Health (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Epidemiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Organic Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Urology & Nephrology (AREA)
- Oncology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US64749605P | 2005-01-27 | 2005-01-27 | |
| US60/647,496 | 2005-01-27 | ||
| PCT/US2006/003116 WO2006081510A2 (en) | 2005-01-27 | 2006-01-27 | Methods for treating renal cell carcinoma |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2595959A1 true CA2595959A1 (en) | 2006-08-03 |
Family
ID=36741121
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002595959A Abandoned CA2595959A1 (en) | 2005-01-27 | 2006-01-27 | Methods for treating renal cell carcinoma |
Country Status (13)
| Country | Link |
|---|---|
| US (2) | US20070014765A1 (https=) |
| EP (1) | EP1846020B1 (https=) |
| JP (2) | JP2008528621A (https=) |
| KR (1) | KR20070102576A (https=) |
| CN (1) | CN101132809A (https=) |
| AU (1) | AU2006207987B2 (https=) |
| BR (1) | BRPI0606774A2 (https=) |
| CA (1) | CA2595959A1 (https=) |
| ES (1) | ES2432141T3 (https=) |
| IL (1) | IL184865A (https=) |
| MX (1) | MX2007009012A (https=) |
| RU (1) | RU2404795C2 (https=) |
| WO (1) | WO2006081510A2 (https=) |
Families Citing this family (38)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2370399A4 (en) * | 2008-12-11 | 2013-05-22 | Agency Science Tech & Res | GLUCOSE-PEG CONJUGATES TO REDUCE GLUCOSE TRANSPORT INTO A CELL |
| US20150299255A1 (en) * | 2010-11-01 | 2015-10-22 | Susavion Biosciences, Inc. | Compositions and methods for modulating innate and adaptive immune systems |
| US9428567B2 (en) | 2010-12-22 | 2016-08-30 | The Board Of Trustees Of The Leland Stanford Junior University | Antagonists of interleukin-2 receptor |
| KR102220006B1 (ko) * | 2011-03-11 | 2021-02-24 | 아시스땅스 퍼블리끄-오삐또 드 빠리 | 자가면역 - 관련 또는 염증성 장애를 치료하기 위한 저용량 ｉｌ２ 의 용도 |
| ES2811624T3 (es) * | 2011-03-11 | 2021-03-12 | Hopitaux Paris Assist Publique | Régimen de dosificación de IL-2 para tratar lupus eritematoso sistémico |
| CN105722860A (zh) | 2013-09-24 | 2016-06-29 | 梅迪塞纳医疗股份有限公司 | 白介素-2融合蛋白及其应用 |
| WO2015164815A1 (en) | 2014-04-24 | 2015-10-29 | The Board Of Trustees Of The Leland Stanford Junior University | Superagonists, partial agonists and antagonists of interleukin-2 |
| WO2016025385A1 (en) | 2014-08-11 | 2016-02-18 | Delinia, Inc. | Modified il-2 variants that selectively activate regulatory t cells for the treatment of autoimmune diseases |
| US10350260B2 (en) * | 2015-04-27 | 2019-07-16 | Susavion Biosciences, Inc. | Compositions and methods for treating cancer and persistent viral infections |
| EP3288576A4 (en) * | 2015-04-27 | 2019-01-16 | Susavion Biosciences, Inc. | COMPOSITIONS AND METHODS FOR THE TREATMENT OF CANCER AND PERSISTENT VIRUS INFECTIONS |
| US20170204154A1 (en) | 2016-01-20 | 2017-07-20 | Delinia, Inc. | Molecules that selectively activate regulatory t cells for the treatment of autoimmune diseases |
| US11077172B2 (en) | 2016-11-08 | 2021-08-03 | Delinia, Inc. | IL-2 variants for the treatment of psoriasis |
| CU24483B1 (es) * | 2016-11-15 | 2020-04-02 | Ct Inmunologia Molecular | Método para incrementar los niveles de secreción de la interleucina-2 |
| BR112019018915A2 (pt) | 2017-03-15 | 2020-04-14 | Pandion Therapeutics Inc | imunotolerância direcionada |
| BR112019024556A2 (pt) | 2017-05-24 | 2020-06-23 | Novartis Ag | Proteínas enxertadas com citocina de anticorpo e métodos para uso no tratamento de câncer |
| JP2020521452A (ja) | 2017-05-24 | 2020-07-27 | パンディオン・セラピューティクス・インコーポレイテッド | 標的化免疫寛容 |
| AU2018287317B2 (en) | 2017-06-19 | 2024-06-20 | Medicenna Therapeutics Inc. | Uses and methods for IL-2 superagonists, agonists, and fusions thereof |
| AU2018300069C1 (en) | 2017-07-11 | 2025-11-20 | Synthorx, Inc. | Incorporation of unnatural nucleotides and methods thereof |
| WO2019028419A1 (en) | 2017-08-03 | 2019-02-07 | Synthorx, Inc. | CYTOKINE CONJUGATES FOR THE TREATMENT OF PROLIFERATIVE AND INFECTIOUS DISEASES |
| US20200299349A1 (en) | 2017-11-21 | 2020-09-24 | The Board Of Trustees Of The Leland Stanford Junior University | Partial agonists of interleukin-2 |
| US10946068B2 (en) | 2017-12-06 | 2021-03-16 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| USRE50550E1 (en) | 2017-12-06 | 2025-08-26 | Pandion Operations, Inc. | IL-2 muteins and uses thereof |
| US10174091B1 (en) | 2017-12-06 | 2019-01-08 | Pandion Therapeutics, Inc. | IL-2 muteins |
| EP3737692A4 (en) | 2018-01-09 | 2021-09-29 | Elstar Therapeutics, Inc. | CALRETICULIN AND MODIFIED T-LYMPHOCYTES BINDING CONSTRUCTIONS FOR THE TREATMENT OF DISEASES |
| US12152073B2 (en) | 2018-03-14 | 2024-11-26 | Marengo Therapeutics, Inc. | Multifunctional molecules that bind to calreticulin and uses thereof |
| EP3818083A2 (en) | 2018-07-03 | 2021-05-12 | Elstar Therapeutics, Inc. | Anti-tcr antibody molecules and uses thereof |
| ES3059360T3 (en) | 2018-11-08 | 2026-03-19 | Synthorx Inc | Interleukin 10 conjugates and uses thereof |
| KR20260039812A (ko) | 2019-02-06 | 2026-03-20 | 신톡스, 인크. | Il-2 콘쥬게이트 및 이의 사용 방법 |
| JP7710373B2 (ja) | 2019-02-21 | 2025-07-18 | マレンゴ・セラピューティクス，インコーポレーテッド | Ｔ細胞関連のがん細胞に結合する多機能性分子およびその使用 |
| AU2020224681A1 (en) | 2019-02-21 | 2021-09-16 | Marengo Therapeutics, Inc. | Antibody molecules that bind to NKp30 and uses thereof |
| WO2020236875A1 (en) | 2019-05-20 | 2020-11-26 | Pandion Therapeutics, Inc. | Madcam targeted immunotolerance |
| CN114555632A (zh) | 2019-08-23 | 2022-05-27 | 新索思股份有限公司 | Il-15缀合物及其用途 |
| MX2022002740A (es) | 2019-09-10 | 2022-03-25 | Synthorx Inc | Conjugados de il-2 y metodos de uso para tratar enfermedades autoinmunes. |
| BR112022012112A2 (pt) | 2019-12-20 | 2022-09-06 | Regeneron Pharma | Agonistas de il2 e métodos de uso dos mesmos |
| CN116234829A (zh) | 2020-01-03 | 2023-06-06 | 马伦戈治疗公司 | 抗tcr抗体分子及其用途 |
| US11633488B2 (en) | 2020-01-10 | 2023-04-25 | Bright Peak Therapeutics Ag | Modified IL-2 polypeptides and uses thereof |
| US11981715B2 (en) | 2020-02-21 | 2024-05-14 | Pandion Operations, Inc. | Tissue targeted immunotolerance with a CD39 effector |
| TW202317623A (zh) | 2021-06-14 | 2023-05-01 | 美商再生元醫藥公司 | 基於il2之治療劑及其使用方法 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4752585A (en) * | 1985-12-17 | 1988-06-21 | Cetus Corporation | Oxidation-resistant muteins |
| US4766106A (en) | 1985-06-26 | 1988-08-23 | Cetus Corporation | Solubilization of proteins for pharmaceutical compositions using polymer conjugation |
| US4931543A (en) | 1987-05-11 | 1990-06-05 | Cetus Corporation | Process for recovering microbially produced interleukin-2 |
| US5830452A (en) * | 1990-11-20 | 1998-11-03 | Chiron Corporation | Method for enhancing the anti-tumor therapeutic index of interleukin-2 |
| RU2174409C2 (ru) * | 1995-11-30 | 2001-10-10 | Борд оф Риджентс, ЗЭ Юниверсити оф Тексас Систем | Способы и композиции для диагностики и лечения рака |
| US7632496B2 (en) * | 2002-07-01 | 2009-12-15 | Wilex Ag | Co-administration of cG250 and IL-2 or IFN-α for treating cancer such as renal cell carcinomas |
-
2006
- 2006-01-27 AU AU2006207987A patent/AU2006207987B2/en not_active Ceased
- 2006-01-27 JP JP2007553304A patent/JP2008528621A/ja active Pending
- 2006-01-27 WO PCT/US2006/003116 patent/WO2006081510A2/en not_active Ceased
- 2006-01-27 CA CA002595959A patent/CA2595959A1/en not_active Abandoned
- 2006-01-27 RU RU2007132125/14A patent/RU2404795C2/ru not_active IP Right Cessation
- 2006-01-27 EP EP06719806.9A patent/EP1846020B1/en not_active Expired - Lifetime
- 2006-01-27 MX MX2007009012A patent/MX2007009012A/es active IP Right Grant
- 2006-01-27 BR BRPI0606774-3A patent/BRPI0606774A2/pt not_active Application Discontinuation
- 2006-01-27 CN CNA2006800067217A patent/CN101132809A/zh active Pending
- 2006-01-27 KR KR1020077019556A patent/KR20070102576A/ko not_active Ceased
- 2006-01-27 ES ES06719806T patent/ES2432141T3/es not_active Expired - Lifetime
- 2006-01-27 US US11/342,243 patent/US20070014765A1/en not_active Abandoned
-
2007
- 2007-07-26 IL IL184865A patent/IL184865A/en active IP Right Grant
-
2009
- 2009-07-28 US US12/460,991 patent/US8012465B2/en not_active Expired - Fee Related
-
2011
- 2011-12-06 JP JP2011266809A patent/JP2012046552A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| JP2008528621A (ja) | 2008-07-31 |
| MX2007009012A (es) | 2007-09-14 |
| WO2006081510A2 (en) | 2006-08-03 |
| AU2006207987B2 (en) | 2011-09-15 |
| EP1846020A2 (en) | 2007-10-24 |
| RU2007132125A (ru) | 2009-03-10 |
| US20100316595A1 (en) | 2010-12-16 |
| BRPI0606774A2 (pt) | 2009-07-14 |
| WO2006081510A3 (en) | 2007-01-18 |
| IL184865A (en) | 2011-04-28 |
| IL184865A0 (en) | 2007-12-03 |
| JP2012046552A (ja) | 2012-03-08 |
| RU2404795C2 (ru) | 2010-11-27 |
| AU2006207987A1 (en) | 2006-08-03 |
| ES2432141T3 (es) | 2013-11-29 |
| CN101132809A (zh) | 2008-02-27 |
| EP1846020B1 (en) | 2013-08-21 |
| US20070014765A1 (en) | 2007-01-18 |
| US8012465B2 (en) | 2011-09-06 |
| KR20070102576A (ko) | 2007-10-18 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8012465B2 (en) | Methods for treating renal cell carcinoma | |
| JP6718494B2 (ja) | 癌を処置するためのペグ化ｉｌ−１０の使用 | |
| JP2023099731A (ja) | ＩＬ－２Ｒβ選択的作動薬と長時間作用型ＩＬ－１５作動薬との併用 | |
| KR20070108402A (ko) | 화학요법제와 ｉｌ-2 및 선택적으로 항-ｃｄ20 항체의조합물을 사용하여 임파종을 치료하는 방법 | |
| CN114746104A (zh) | 治疗由化疗或放疗引起的中性粒细胞减少症的方法 | |
| US20060039892A1 (en) | Methods of healing wounds by administering human IL-18 | |
| KR20250004790A (ko) | 항-her2 항체를 함유하는 피하 투여용 약학 조성물 | |
| JP2000109434A (ja) | 細胞増殖抑制方法および細胞増殖抑制剤 | |
| HK1172248A (en) | Use of pegylated il-10 to treat cancer | |
| HK1201182B (en) | Pegylated il-10 for use in treating lymphoma |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued |
Effective date: 20131205 |