AU2003270509B2 - Analyzing nerve cell damage - Google Patents
Analyzing nerve cell damage Download PDFInfo
- Publication number
- AU2003270509B2 AU2003270509B2 AU2003270509A AU2003270509A AU2003270509B2 AU 2003270509 B2 AU2003270509 B2 AU 2003270509B2 AU 2003270509 A AU2003270509 A AU 2003270509A AU 2003270509 A AU2003270509 A AU 2003270509A AU 2003270509 B2 AU2003270509 B2 AU 2003270509B2
- Authority
- AU
- Australia
- Prior art keywords
- spectrin
- mixture
- biological sample
- subject
- sbdp145
- 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.)
- Ceased
Links
- 210000002569 neuron Anatomy 0.000 title claims description 41
- 208000037887 cell injury Diseases 0.000 title claims description 24
- 230000005779 cell damage Effects 0.000 title claims description 23
- 102000005890 Spectrin Human genes 0.000 claims description 58
- 108010019965 Spectrin Proteins 0.000 claims description 58
- 239000012472 biological sample Substances 0.000 claims description 53
- 239000003550 marker Substances 0.000 claims description 53
- 102000007590 Calpain Human genes 0.000 claims description 52
- 108010032088 Calpain Proteins 0.000 claims description 52
- 108090000397 Caspase 3 Proteins 0.000 claims description 50
- 102000003952 Caspase 3 Human genes 0.000 claims description 50
- 238000000034 method Methods 0.000 claims description 43
- 241000282414 Homo sapiens Species 0.000 claims description 22
- 239000000758 substrate Substances 0.000 claims description 21
- 239000000203 mixture Substances 0.000 claims description 20
- 108091005804 Peptidases Proteins 0.000 claims description 17
- 239000004365 Protease Substances 0.000 claims description 16
- 238000001514 detection method Methods 0.000 claims description 15
- 210000000653 nervous system Anatomy 0.000 claims description 11
- 230000006337 proteolytic cleavage Effects 0.000 claims description 11
- 230000015556 catabolic process Effects 0.000 claims description 9
- 238000004891 communication Methods 0.000 claims description 8
- 239000012530 fluid Substances 0.000 claims description 8
- 239000000126 substance Substances 0.000 claims description 8
- 208000028389 Nerve injury Diseases 0.000 claims description 6
- 238000004458 analytical method Methods 0.000 claims description 6
- 230000008764 nerve damage Effects 0.000 claims description 6
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
- 230000002797 proteolythic effect Effects 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 40
- 210000001175 cerebrospinal fluid Anatomy 0.000 description 31
- 239000003795 chemical substances by application Substances 0.000 description 30
- 235000018102 proteins Nutrition 0.000 description 25
- 102000004169 proteins and genes Human genes 0.000 description 25
- 108090000623 proteins and genes Proteins 0.000 description 25
- 239000000523 sample Substances 0.000 description 24
- 241001465754 Metazoa Species 0.000 description 17
- 208000027418 Wounds and injury Diseases 0.000 description 17
- 230000006378 damage Effects 0.000 description 17
- 208000014674 injury Diseases 0.000 description 17
- 239000012634 fragment Substances 0.000 description 16
- 238000001262 western blot Methods 0.000 description 16
- 102000035195 Peptidases Human genes 0.000 description 15
- 230000004913 activation Effects 0.000 description 13
- 235000019419 proteases Nutrition 0.000 description 13
- CHADEQDQBURGHL-UHFFFAOYSA-N (6'-acetyloxy-3-oxospiro[2-benzofuran-1,9'-xanthene]-3'-yl) acetate Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(OC(C)=O)C=C1OC1=CC(OC(=O)C)=CC=C21 CHADEQDQBURGHL-UHFFFAOYSA-N 0.000 description 12
- 241000700159 Rattus Species 0.000 description 12
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 12
- 239000002953 phosphate buffered saline Substances 0.000 description 12
- XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 12
- 206010008089 Cerebral artery occlusion Diseases 0.000 description 11
- 238000009825 accumulation Methods 0.000 description 11
- 238000003556 assay Methods 0.000 description 11
- 201000007309 middle cerebral artery infarction Diseases 0.000 description 11
- NWQUHAJRFNRIIU-DVGFTKJRSA-L 9p59ges78d Chemical compound [Na+].[Na+].C(/[C@@H]1O[C@]2(C)C[C@]3(C)O[C@]4(C)CC[C@H](O[C@H]4C[C@H]3O[C@H]2C[C@H]1O[C@H]1C2)[C@@H](O)[C@H](O)C[C@@H](C)[C@H](CC=C)C)=C/C[C@H]1O[C@@H]1[C@]2(C)O[C@@]2(C)CC[C@@]3(C)O[C@H]4C[C@@H](O)[C@](C)([C@H]5O[C@H]6C[C@H]7O[C@@]8(C)CC[C@H]9O[C@@]%10(C)[C@@H](O)[C@H]%11O[C@H]([C@H](O)C[C@]%11(C)O[C@@H]%10C[C@]9(C)O[C@@H]8C[C@]7(C)O[C@@H]6CC5)[C@H]5[C@@H](C[C@@H]6O[C@@H](C[C@H](O)C[C@@H](O)[C@H]7[C@@H](C[C@@H]8O[C@H]([C@H](O)[C@@H](O)[C@@H]8O7)[C@H]7[C@@H]([C@@H](O)[C@@H]8O[C@H]9C[C@H]%10O[C@H]%11[C@@H](O)[C@@H](OS([O-])(=O)=O)[C@H](C[C@H](O)[C@@H](O)[C@@H]%12[C@@H](C[C@H]%13O[C@@]%14(C)C[C@H]%15O[C@@]%16(C)C[C@@H](O)[C@H]%17O[C@H]([C@H](O)[C@H](O)[C@@H]%17O[C@@H]%16C[C@@H]%15O[C@@H]%14[C@@H](O)[C@@H]%13O%12)[C@H](C)[C@H](O)[C@H](C)CC[C@H](OS([O-])(=O)=O)[C@H](O)[C@H](C)C[C@@H](O)C(=C)C(\C)=C\CO)O)O[C@@H]%11C[C@@H]%10O[C@@H]9[C@@H](O)[C@H]8O7)O)O)[C@H](O)[C@@H](O)[C@@H]6O5)O)O[C@]4(C)C[C@@H]3O[C@@H]2C1 NWQUHAJRFNRIIU-DVGFTKJRSA-L 0.000 description 10
- 241000283984 Rodentia Species 0.000 description 10
- 210000004556 brain Anatomy 0.000 description 10
- 238000002474 experimental method Methods 0.000 description 10
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 9
- 238000003119 immunoblot Methods 0.000 description 9
- HKSZLNNOFSGOKW-UHFFFAOYSA-N ent-staurosporine Natural products C12=C3N4C5=CC=CC=C5C3=C3CNC(=O)C3=C2C2=CC=CC=C2N1C1CC(NC)C(OC)C4(C)O1 HKSZLNNOFSGOKW-UHFFFAOYSA-N 0.000 description 8
- 239000012528 membrane Substances 0.000 description 8
- HKSZLNNOFSGOKW-FYTWVXJKSA-N staurosporine Chemical compound C12=C3N4C5=CC=CC=C5C3=C3CNC(=O)C3=C2C2=CC=CC=C2N1[C@H]1C[C@@H](NC)[C@@H](OC)[C@]4(C)O1 HKSZLNNOFSGOKW-FYTWVXJKSA-N 0.000 description 8
- CGPUWJWCVCFERF-UHFFFAOYSA-N staurosporine Natural products C12=C3N4C5=CC=CC=C5C3=C3CNC(=O)C3=C2C2=CC=CC=C2N1C1CC(NC)C(OC)C4(OC)O1 CGPUWJWCVCFERF-UHFFFAOYSA-N 0.000 description 8
- 238000001356 surgical procedure Methods 0.000 description 8
- 210000001519 tissue Anatomy 0.000 description 8
- 239000007983 Tris buffer Substances 0.000 description 7
- 230000006907 apoptotic process Effects 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 238000011282 treatment Methods 0.000 description 7
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 7
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 6
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 6
- 210000000269 carotid artery external Anatomy 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- INAAIJLSXJJHOZ-UHFFFAOYSA-N pibenzimol Chemical compound C1CN(C)CCN1C1=CC=C(N=C(N2)C=3C=C4NC(=NC4=CC=3)C=3C=CC(O)=CC=3)C2=C1 INAAIJLSXJJHOZ-UHFFFAOYSA-N 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- 230000000472 traumatic effect Effects 0.000 description 6
- 108091023037 Aptamer Proteins 0.000 description 5
- 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 5
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 208000029028 brain injury Diseases 0.000 description 5
- 210000004004 carotid artery internal Anatomy 0.000 description 5
- 230000003833 cell viability Effects 0.000 description 5
- 238000003776 cleavage reaction Methods 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 239000000975 dye Substances 0.000 description 5
- 238000001378 electrochemiluminescence detection Methods 0.000 description 5
- 230000000925 erythroid effect Effects 0.000 description 5
- 238000001727 in vivo Methods 0.000 description 5
- 230000004044 response Effects 0.000 description 5
- 230000007017 scission Effects 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- 101100505161 Caenorhabditis elegans mel-32 gene Proteins 0.000 description 4
- 241000283707 Capra Species 0.000 description 4
- 238000002965 ELISA Methods 0.000 description 4
- 102100039289 Glial fibrillary acidic protein Human genes 0.000 description 4
- 101710193519 Glial fibrillary acidic protein Proteins 0.000 description 4
- 108090000192 Methionyl aminopeptidases Proteins 0.000 description 4
- 102100021118 Microtubule-associated protein 2 Human genes 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 230000001054 cortical effect Effects 0.000 description 4
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 4
- 238000001962 electrophoresis Methods 0.000 description 4
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 4
- 210000005046 glial fibrillary acidic protein Anatomy 0.000 description 4
- 230000003447 ipsilateral effect Effects 0.000 description 4
- 230000000302 ischemic effect Effects 0.000 description 4
- 230000017074 necrotic cell death Effects 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- 238000005406 washing Methods 0.000 description 4
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108010076667 Caspases Proteins 0.000 description 3
- 102000011727 Caspases Human genes 0.000 description 3
- 238000007400 DNA extraction Methods 0.000 description 3
- 239000012591 Dulbecco’s Phosphate Buffered Saline Substances 0.000 description 3
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 239000012981 Hank's balanced salt solution Substances 0.000 description 3
- 101001092197 Homo sapiens RNA binding protein fox-1 homolog 3 Proteins 0.000 description 3
- MQUQNUAYKLCRME-INIZCTEOSA-N N-tosyl-L-phenylalanyl chloromethyl ketone Chemical compound C1=CC(C)=CC=C1S(=O)(=O)N[C@H](C(=O)CCl)CC1=CC=CC=C1 MQUQNUAYKLCRME-INIZCTEOSA-N 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 239000004677 Nylon Substances 0.000 description 3
- 239000002033 PVDF binder Substances 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 229940123573 Protein synthesis inhibitor Drugs 0.000 description 3
- 102100035530 RNA binding protein fox-1 homolog 3 Human genes 0.000 description 3
- 208000006011 Stroke Diseases 0.000 description 3
- 208000030886 Traumatic Brain injury Diseases 0.000 description 3
- 238000000540 analysis of variance Methods 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 239000013060 biological fluid Substances 0.000 description 3
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical compound C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 3
- 210000001168 carotid artery common Anatomy 0.000 description 3
- 230000030833 cell death Effects 0.000 description 3
- 230000001413 cellular effect Effects 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
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 235000013861 fat-free Nutrition 0.000 description 3
- 108010006620 fodrin Proteins 0.000 description 3
- 239000011521 glass Substances 0.000 description 3
- 229960003132 halothane Drugs 0.000 description 3
- BCQZXOMGPXTTIC-UHFFFAOYSA-N halothane Chemical compound FC(F)(F)C(Cl)Br BCQZXOMGPXTTIC-UHFFFAOYSA-N 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 238000001114 immunoprecipitation Methods 0.000 description 3
- 239000012160 loading buffer Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 230000003961 neuronal insult Effects 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 210000004940 nucleus Anatomy 0.000 description 3
- 229920001778 nylon Polymers 0.000 description 3
- 230000007170 pathology Effects 0.000 description 3
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 3
- 210000002381 plasma Anatomy 0.000 description 3
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 238000000751 protein extraction Methods 0.000 description 3
- 239000000007 protein synthesis inhibitor Substances 0.000 description 3
- 238000011160 research Methods 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- OZFAFGSSMRRTDW-UHFFFAOYSA-N (2,4-dichlorophenyl) benzenesulfonate Chemical compound ClC1=CC(Cl)=CC=C1OS(=O)(=O)C1=CC=CC=C1 OZFAFGSSMRRTDW-UHFFFAOYSA-N 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
- SHXWCVYOXRDMCX-UHFFFAOYSA-N 3,4-methylenedioxymethamphetamine Chemical compound CNC(C)CC1=CC=C2OCOC2=C1 SHXWCVYOXRDMCX-UHFFFAOYSA-N 0.000 description 2
- 206010002091 Anaesthesia Diseases 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 102100021277 Beta-secretase 2 Human genes 0.000 description 2
- 101710150190 Beta-secretase 2 Proteins 0.000 description 2
- 208000022306 Cerebral injury Diseases 0.000 description 2
- 241000283073 Equus caballus Species 0.000 description 2
- 101000746373 Homo sapiens Granulocyte-macrophage colony-stimulating factor Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- PIWKPBJCKXDKJR-UHFFFAOYSA-N Isoflurane Chemical compound FC(F)OC(Cl)C(F)(F)F PIWKPBJCKXDKJR-UHFFFAOYSA-N 0.000 description 2
- 208000001738 Nervous System Trauma Diseases 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- 108091006629 SLC13A2 Proteins 0.000 description 2
- 230000037005 anaesthesia Effects 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 230000001640 apoptogenic effect Effects 0.000 description 2
- 210000001130 astrocyte Anatomy 0.000 description 2
- 238000001574 biopsy Methods 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 230000006931 brain damage Effects 0.000 description 2
- 231100000874 brain damage Toxicity 0.000 description 2
- 210000005013 brain tissue Anatomy 0.000 description 2
- 239000012159 carrier gas Substances 0.000 description 2
- 210000003169 central nervous system Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- -1 cerebrospinal fluid Substances 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 230000006835 compression Effects 0.000 description 2
- 238000007906 compression Methods 0.000 description 2
- 238000002591 computed tomography Methods 0.000 description 2
- 210000005257 cortical tissue Anatomy 0.000 description 2
- 238000007428 craniotomy Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000002224 dissection Methods 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 238000013467 fragmentation Methods 0.000 description 2
- 238000006062 fragmentation reaction Methods 0.000 description 2
- 230000002518 glial effect Effects 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 238000003384 imaging method Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 208000028867 ischemia Diseases 0.000 description 2
- 229960002725 isoflurane Drugs 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- YFCUZWYIPBUQBD-ZOWNYOTGSA-N n-[(3s)-7-amino-1-chloro-2-oxoheptan-3-yl]-4-methylbenzenesulfonamide;hydron;chloride Chemical compound Cl.CC1=CC=C(S(=O)(=O)N[C@@H](CCCCN)C(=O)CCl)C=C1 YFCUZWYIPBUQBD-ZOWNYOTGSA-N 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 230000001537 neural effect Effects 0.000 description 2
- 230000001722 neurochemical effect Effects 0.000 description 2
- 210000004498 neuroglial cell Anatomy 0.000 description 2
- 229940127255 pan-caspase inhibitor Drugs 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 210000001428 peripheral nervous system Anatomy 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920003023 plastic Polymers 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000013641 positive control Substances 0.000 description 2
- 230000010410 reperfusion Effects 0.000 description 2
- 238000011808 rodent model Methods 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- 239000011550 stock solution Substances 0.000 description 2
- 230000002459 sustained effect Effects 0.000 description 2
- 210000001103 thalamus Anatomy 0.000 description 2
- 230000009529 traumatic brain injury Effects 0.000 description 2
- 239000012224 working solution Substances 0.000 description 2
- OCJBOOLMMGQPQU-UHFFFAOYSA-N 1,4-dichlorobenzene Chemical compound ClC1=CC=C(Cl)C=C1 OCJBOOLMMGQPQU-UHFFFAOYSA-N 0.000 description 1
- PRDFBSVERLRRMY-UHFFFAOYSA-N 2'-(4-ethoxyphenyl)-5-(4-methylpiperazin-1-yl)-2,5'-bibenzimidazole Chemical compound C1=CC(OCC)=CC=C1C1=NC2=CC=C(C=3NC4=CC(=CC=C4N=3)N3CCN(C)CC3)C=C2N1 PRDFBSVERLRRMY-UHFFFAOYSA-N 0.000 description 1
- IHPYMWDTONKSCO-UHFFFAOYSA-N 2,2'-piperazine-1,4-diylbisethanesulfonic acid Chemical compound OS(=O)(=O)CCN1CCN(CCS(O)(=O)=O)CC1 IHPYMWDTONKSCO-UHFFFAOYSA-N 0.000 description 1
- 125000000022 2-aminoethyl group Chemical group [H]C([*])([H])C([H])([H])N([H])[H] 0.000 description 1
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 208000024827 Alzheimer disease Diseases 0.000 description 1
- 108010039627 Aprotinin Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-M Bicarbonate Chemical compound OC([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-M 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 201000006474 Brain Ischemia Diseases 0.000 description 1
- 208000003174 Brain Neoplasms Diseases 0.000 description 1
- 108091011896 CSF1 Proteins 0.000 description 1
- 229940121926 Calpain inhibitor Drugs 0.000 description 1
- 102000003900 Calpain-2 Human genes 0.000 description 1
- 108090000232 Calpain-2 Proteins 0.000 description 1
- 102100035037 Calpastatin Human genes 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 206010008111 Cerebral haemorrhage Diseases 0.000 description 1
- 206010008120 Cerebral ischaemia Diseases 0.000 description 1
- 206010008190 Cerebrovascular accident Diseases 0.000 description 1
- 206010008513 Child maltreatment syndrome Diseases 0.000 description 1
- 208000034656 Contusions Diseases 0.000 description 1
- 206010012289 Dementia Diseases 0.000 description 1
- 208000032131 Diabetic Neuropathies Diseases 0.000 description 1
- 238000009007 Diagnostic Kit Methods 0.000 description 1
- 102100021238 Dynamin-2 Human genes 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 102000053171 Glial Fibrillary Acidic Human genes 0.000 description 1
- 108700005000 Glial Fibrillary Acidic Proteins 0.000 description 1
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 208000010496 Heart Arrest Diseases 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 238000010867 Hoechst staining Methods 0.000 description 1
- 101000793880 Homo sapiens Caspase-3 Proteins 0.000 description 1
- 101000817607 Homo sapiens Dynamin-2 Proteins 0.000 description 1
- 208000023105 Huntington disease Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 206010022773 Intracranial pressure increased Diseases 0.000 description 1
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
- 102100028123 Macrophage colony-stimulating factor 1 Human genes 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 208000009857 Microaneurysm Diseases 0.000 description 1
- 102000009664 Microtubule-Associated Proteins Human genes 0.000 description 1
- 108010020004 Microtubule-Associated Proteins Proteins 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- KWYHDKDOAIKMQN-UHFFFAOYSA-N N,N,N',N'-tetramethylethylenediamine Chemical compound CN(C)CCN(C)C KWYHDKDOAIKMQN-UHFFFAOYSA-N 0.000 description 1
- RJWLAIMXRBDUMH-ULQDDVLXSA-N N-Acetylleucyl-leucyl-methioninal Chemical compound CSCC[C@@H](C=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(C)=O RJWLAIMXRBDUMH-ULQDDVLXSA-N 0.000 description 1
- 238000011887 Necropsy Methods 0.000 description 1
- 206010028851 Necrosis Diseases 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 239000007990 PIPES buffer Substances 0.000 description 1
- 241000609499 Palicourea Species 0.000 description 1
- 208000018737 Parkinson disease Diseases 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 102000029797 Prion Human genes 0.000 description 1
- 108091000054 Prion Proteins 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 206010039203 Road traffic accident Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 208000002108 Shaken Baby Syndrome Diseases 0.000 description 1
- 102100031874 Spectrin alpha chain, non-erythrocytic 1 Human genes 0.000 description 1
- 101710157175 Spectrin alpha chain, non-erythrocytic 1 Proteins 0.000 description 1
- 208000032851 Subarachnoid Hemorrhage Diseases 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 239000004809 Teflon Substances 0.000 description 1
- 229920006362 Teflon® Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 238000010162 Tukey test Methods 0.000 description 1
- 206010052428 Wound Diseases 0.000 description 1
- SXEHKFHPFVVDIR-UHFFFAOYSA-N [4-(4-hydrazinylphenyl)phenyl]hydrazine Chemical compound C1=CC(NN)=CC=C1C1=CC=C(NN)C=C1 SXEHKFHPFVVDIR-UHFFFAOYSA-N 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 210000002551 anterior cerebral artery Anatomy 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 229960004405 aprotinin Drugs 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- 230000007844 axonal damage Effects 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 238000007630 basic procedure Methods 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 238000009534 blood test Methods 0.000 description 1
- 230000036760 body temperature Effects 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 108010053420 calpain inhibitor 2 Proteins 0.000 description 1
- 108010079785 calpain inhibitors Proteins 0.000 description 1
- 108010044208 calpastatin Proteins 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 230000006727 cell loss Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000003855 cell nucleus Anatomy 0.000 description 1
- 206010008118 cerebral infarction Diseases 0.000 description 1
- 208000026106 cerebrovascular disease Diseases 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000009519 contusion Effects 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 239000003179 convulsant agent Substances 0.000 description 1
- 230000036757 core body temperature Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- KXGVEGMKQFWNSR-LLQZFEROSA-N deoxycholic acid Chemical compound C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(O)=O)C)[C@@]2(C)[C@@H](O)C1 KXGVEGMKQFWNSR-LLQZFEROSA-N 0.000 description 1
- 229960003964 deoxycholic acid Drugs 0.000 description 1
- KXGVEGMKQFWNSR-UHFFFAOYSA-N deoxycholic acid Natural products C1CC2CC(O)CCC2(C)C2C1C1CCC(C(CCC(O)=O)C)C1(C)C(O)C2 KXGVEGMKQFWNSR-UHFFFAOYSA-N 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 229940117389 dichlorobenzene Drugs 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- FOCAHLGSDWHSAH-UHFFFAOYSA-N difluoromethanethione Chemical compound FC(F)=S FOCAHLGSDWHSAH-UHFFFAOYSA-N 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 210000001951 dura mater Anatomy 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 206010015037 epilepsy Diseases 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 239000000834 fixative Substances 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 210000001320 hippocampus Anatomy 0.000 description 1
- 239000011539 homogenization buffer Substances 0.000 description 1
- 208000003906 hydrocephalus Diseases 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 239000003547 immunosorbent Substances 0.000 description 1
- 230000003116 impacting effect Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 210000004283 incisor Anatomy 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 208000037906 ischaemic injury Diseases 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 239000010410 layer Substances 0.000 description 1
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
- 108010052968 leupeptin Proteins 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000009593 lumbar puncture Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000006249 magnetic particle Substances 0.000 description 1
- 238000002595 magnetic resonance imaging Methods 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 238000002406 microsurgery Methods 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 230000000877 morphologic effect Effects 0.000 description 1
- 239000012120 mounting media Substances 0.000 description 1
- 210000000107 myocyte Anatomy 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 230000001338 necrotic effect Effects 0.000 description 1
- 210000000944 nerve tissue Anatomy 0.000 description 1
- 208000004296 neuralgia Diseases 0.000 description 1
- 208000015122 neurodegenerative disease Diseases 0.000 description 1
- 208000021722 neuropathic pain Diseases 0.000 description 1
- 201000001119 neuropathy Diseases 0.000 description 1
- 230000007823 neuropathy Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 201000003077 normal pressure hydrocephalus Diseases 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 108010091212 pepstatin Proteins 0.000 description 1
- 229950000964 pepstatin Drugs 0.000 description 1
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
- 239000000863 peptide conjugate Substances 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 208000033808 peripheral neuropathy Diseases 0.000 description 1
- 239000012466 permeate Substances 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 238000011458 pharmacological treatment Methods 0.000 description 1
- 229920000729 poly(L-lysine) polymer Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000011158 quantitative evaluation Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 208000037974 severe injury Diseases 0.000 description 1
- 230000009528 severe injury Effects 0.000 description 1
- 230000007781 signaling event Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 210000003625 skull Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- VVLFAAMTGMGYBS-UHFFFAOYSA-M sodium;4-[[4-(ethylamino)-3-methylphenyl]-(4-ethylimino-3-methylcyclohexa-2,5-dien-1-ylidene)methyl]-3-sulfobenzenesulfonate Chemical compound [Na+].C1=C(C)C(NCC)=CC=C1C(C=1C(=CC(=CC=1)S([O-])(=O)=O)S(O)(=O)=O)=C1C=C(C)C(=NCC)C=C1 VVLFAAMTGMGYBS-UHFFFAOYSA-M 0.000 description 1
- 210000004872 soft tissue Anatomy 0.000 description 1
- 238000012453 sprague-dawley rat model Methods 0.000 description 1
- 201000009032 substance abuse Diseases 0.000 description 1
- 231100000736 substance abuse Toxicity 0.000 description 1
- 208000011117 substance-related disease Diseases 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 210000001550 testis Anatomy 0.000 description 1
- BFKJFAAPBSQJPD-UHFFFAOYSA-N tetrafluoroethene Chemical compound FC(F)=C(F)F BFKJFAAPBSQJPD-UHFFFAOYSA-N 0.000 description 1
- 208000037816 tissue injury Diseases 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- 230000003144 traumatizing effect Effects 0.000 description 1
- 238000001665 trituration Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 238000010792 warming Methods 0.000 description 1
- 210000004885 white matter Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/573—Immunoassay; Biospecific binding assay; Materials therefor for enzymes or isoenzymes
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6893—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids related to diseases not provided for elsewhere
- G01N33/6896—Neurological disorders, e.g. Alzheimer's disease
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Molecular Biology (AREA)
- Organic Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Hematology (AREA)
- Medicinal Chemistry (AREA)
- Urology & Nephrology (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biotechnology (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Cell Biology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Food Science & Technology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US40992002P | 2002-09-11 | 2002-09-11 | |
| US60/409,920 | 2002-09-11 | ||
| PCT/US2003/028406 WO2004025298A1 (en) | 2002-09-11 | 2003-09-11 | Analyzing nerve cell damage |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| AU2003270509A1 AU2003270509A1 (en) | 2004-04-30 |
| AU2003270509A2 AU2003270509A2 (en) | 2004-04-30 |
| AU2003270509B2 true AU2003270509B2 (en) | 2009-03-26 |
Family
ID=31994033
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2003270509A Ceased AU2003270509B2 (en) | 2002-09-11 | 2003-09-11 | Analyzing nerve cell damage |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US7291710B2 (enExample) |
| EP (3) | EP2211176A3 (enExample) |
| JP (1) | JP2005538380A (enExample) |
| AU (1) | AU2003270509B2 (enExample) |
| CA (1) | CA2498614C (enExample) |
| WO (1) | WO2004025298A1 (enExample) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8492107B2 (en) | 2004-04-15 | 2013-07-23 | University Of Florida Research Foundation, Inc. | Neural proteins as biomarkers for nervous system injury and other neural disorders |
| EP1747282B1 (en) * | 2004-04-15 | 2011-06-08 | University of Florida Research Foundation, Inc. | Map-2 proteolytic breakdown products as diagnostic biomarkers for neural injury |
| AU2005238446B2 (en) * | 2004-04-15 | 2009-07-30 | Banyan Biomarkers Inc. | Neural proteins as biomarkers for nervous system injury and other neural disorders |
| US8048638B2 (en) * | 2005-04-01 | 2011-11-01 | University Of Florida Research Foundation, Inc. | Biomarkers of liver injury |
| WO2006107846A2 (en) * | 2005-04-01 | 2006-10-12 | University Of Florida Research Foundation, Inc. | Biomakers of liver injury |
| EP1840574A1 (en) | 2006-03-30 | 2007-10-03 | Institut Pasteur | Use of the alpha chain of brain spectrin and fragments thereof, for diagnosing cerebral diseases |
| JP2011511301A (ja) * | 2008-02-04 | 2011-04-07 | バンヤン・バイオマーカーズ・インコーポレイテッド | 脳損傷を診断または治療するための方法 |
| US20140342381A1 (en) * | 2008-08-11 | 2014-11-20 | Banyan Biomarkers, Inc. | Devices and methods for biomarker detection process and assay of neurological condition |
| JP5781436B2 (ja) * | 2008-08-11 | 2015-09-24 | バンヤン・バイオマーカーズ・インコーポレーテッド | 神経学的状態のバイオマーカー検出方法およびアッセイ |
| EP3355059A3 (en) | 2009-06-19 | 2018-09-26 | Banyan Biomarkers, Inc. | Biomarker assay of neurological condition |
| CA2774173A1 (en) | 2009-09-14 | 2011-03-17 | Banyan Biomarkers, Inc. | Micro-rna, autoantibody and protein markers for diagnosis of neuronal injury |
| US9682132B2 (en) | 2010-01-26 | 2017-06-20 | Banyan Biomarkers, Inc | Compositions and methods relating to argininosucccinate synthetase |
| US20130029362A1 (en) * | 2010-04-01 | 2013-01-31 | Andreas Jeromin | Markers and assays for detection of neurotoxicity |
| CA2939692C (en) | 2013-03-15 | 2022-10-18 | The Trustees Of The University Of Pennsylvania | Blood biomarkers that predict persistent cognitive dysfunction after concussion |
| WO2015066211A1 (en) * | 2013-10-29 | 2015-05-07 | Banyan Biomarkers, Inc. | Uch-l1 isoforms, assays and devices for detection of a neurological condition |
| CN110366558A (zh) | 2016-10-28 | 2019-10-22 | 班扬生物标记公司 | 针对泛素c末端水解酶l1(uch-l1)和胶质纤维酸性蛋白(gfap)的抗体及相关方法 |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5116606A (en) * | 1989-03-09 | 1992-05-26 | Alt John P | Skin treatment method and solution |
| WO1995026506A1 (en) * | 1994-03-25 | 1995-10-05 | Cephalon, Inc. | Methods for detecting calpain activation and indentifying calpain inhibitors |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5118606A (en) * | 1988-09-02 | 1992-06-02 | The Regents Of The University Of California | Methods for detecting cellular pathology by assaying spectrin and spectrin breakdown products |
| US5270163A (en) | 1990-06-11 | 1993-12-14 | University Research Corporation | Methods for identifying nucleic acid ligands |
| US6011020A (en) | 1990-06-11 | 2000-01-04 | Nexstar Pharmaceuticals, Inc. | Nucleic acid ligand complexes |
| US5683867A (en) | 1990-06-11 | 1997-11-04 | Nexstar Pharmaceuticals, Inc. | Systematic evolution of ligands by exponential enrichment: blended SELEX |
| US5707796A (en) | 1990-06-11 | 1998-01-13 | Nexstar Pharmaceuticals, Inc. | Method for selecting nucleic acids on the basis of structure |
| US5660985A (en) | 1990-06-11 | 1997-08-26 | Nexstar Pharmaceuticals, Inc. | High affinity nucleic acid ligands containing modified nucleotides |
| US5567588A (en) | 1990-06-11 | 1996-10-22 | University Research Corporation | Systematic evolution of ligands by exponential enrichment: Solution SELEX |
| ATE318832T1 (de) | 1990-06-11 | 2006-03-15 | Gilead Sciences Inc | Verfahren zur vervendung von nukleinsäureliganden |
| US5496938A (en) | 1990-06-11 | 1996-03-05 | Nexstar Pharmaceuticals, Inc. | Nucleic acid ligands to HIV-RT and HIV-1 rev |
| US5637459A (en) | 1990-06-11 | 1997-06-10 | Nexstar Pharmaceuticals, Inc. | Systematic evolution of ligands by exponential enrichment: chimeric selex |
-
2003
- 2003-09-11 EP EP09014717A patent/EP2211176A3/en not_active Ceased
- 2003-09-11 JP JP2004536454A patent/JP2005538380A/ja active Pending
- 2003-09-11 EP EP10185059.2A patent/EP2348317B1/en not_active Expired - Lifetime
- 2003-09-11 CA CA2498614A patent/CA2498614C/en not_active Expired - Lifetime
- 2003-09-11 US US10/660,069 patent/US7291710B2/en not_active Expired - Lifetime
- 2003-09-11 AU AU2003270509A patent/AU2003270509B2/en not_active Ceased
- 2003-09-11 EP EP03752207A patent/EP1546717A4/en not_active Ceased
- 2003-09-11 WO PCT/US2003/028406 patent/WO2004025298A1/en not_active Ceased
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5116606A (en) * | 1989-03-09 | 1992-05-26 | Alt John P | Skin treatment method and solution |
| WO1995026506A1 (en) * | 1994-03-25 | 1995-10-05 | Cephalon, Inc. | Methods for detecting calpain activation and indentifying calpain inhibitors |
Non-Patent Citations (1)
| Title |
|---|
| PIKE, B. R. et al, Journal of Neurochemistry, 2001, 78, 1297-1306 * |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2348317A2 (en) | 2011-07-27 |
| WO2004025298A1 (en) | 2004-03-25 |
| EP1546717A1 (en) | 2005-06-29 |
| AU2003270509A1 (en) | 2004-04-30 |
| CA2498614C (en) | 2013-04-16 |
| EP1546717A4 (en) | 2007-01-17 |
| US7291710B2 (en) | 2007-11-06 |
| EP2348317A3 (en) | 2011-09-07 |
| CA2498614A1 (en) | 2004-03-25 |
| AU2003270509A2 (en) | 2004-04-30 |
| EP2348317B1 (en) | 2014-12-03 |
| JP2005538380A (ja) | 2005-12-15 |
| US20070003982A1 (en) | 2007-01-04 |
| EP2211176A3 (en) | 2010-12-08 |
| EP2211176A2 (en) | 2010-07-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2003270509B2 (en) | Analyzing nerve cell damage | |
| US20210011028A1 (en) | Biomarker detection process and assay of neurological condition | |
| Rohn et al. | Correlation between caspase activation and neurofibrillary tangle formation in Alzheimer’s disease | |
| US20120202231A1 (en) | Synergistic biomarker assay of neurological condition using s-100b | |
| AU633312B2 (en) | Diagnostic method for alzheimer's disease: examination of non-neural tissue | |
| US20110082203A1 (en) | Process to diagnose or treat brain injury | |
| US20170307640A1 (en) | Methods, kits and devices for detecting bii-spectrin, and breakdown products thereof, as biomarkers for the diagnosis of neural injury | |
| US5871712A (en) | Methods for detecting calpain activation and identifying calpain inhibitors | |
| DE69720433T2 (de) | Verfahren zum nachweis von prionkrankheit | |
| JP4933159B2 (ja) | アルツハイマー病の診断方法 | |
| JPWO2000057189A1 (ja) | メグシンタンパク質の検出方法およびその用途 | |
| US20070184485A1 (en) | Method of diagnosing diseases relating to endometriosis | |
| US20240264177A1 (en) | Biomarker detection process and assay of neurological condition | |
| JPWO2006093138A1 (ja) | アポトーシスに陥る傾向を判定する方法及びその利用 | |
| JP2005049343A (ja) | 子宮内膜症関連疾患の診断方法 | |
| CA2013396A1 (en) | Diagnostic method for alzheimer's disease: examination of non-neural tissue |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| DA3 | Amendments made section 104 |
Free format text: THE NATURE OF THE AMENDMENT IS AS SHOWN IN THE STATEMENT(S) FILED 17 OCT 2007 |
|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |