FR2955334A1 - Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux - Google Patents
Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux Download PDFInfo
- Publication number
- FR2955334A1 FR2955334A1 FR1150365A FR1150365A FR2955334A1 FR 2955334 A1 FR2955334 A1 FR 2955334A1 FR 1150365 A FR1150365 A FR 1150365A FR 1150365 A FR1150365 A FR 1150365A FR 2955334 A1 FR2955334 A1 FR 2955334A1
- Authority
- FR
- France
- Prior art keywords
- matrix
- collagen
- glycosaminoglycans
- type
- biomaterial according
- 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.)
- Granted
Links
- 239000011159 matrix material Substances 0.000 title claims abstract description 71
- 210000001612 chondrocyte Anatomy 0.000 title claims abstract description 26
- 229920002683 Glycosaminoglycan Polymers 0.000 title claims abstract description 23
- 102000000503 Collagen Type II Human genes 0.000 title claims abstract description 22
- 108010041390 Collagen Type II Proteins 0.000 title claims abstract description 22
- 238000000034 method Methods 0.000 title claims abstract description 15
- 241001465754 Metazoa Species 0.000 title claims abstract description 13
- 230000008569 process Effects 0.000 title claims abstract description 9
- 238000004108 freeze drying Methods 0.000 title claims abstract description 8
- 238000002156 mixing Methods 0.000 title claims abstract description 5
- 238000011124 ex vivo culture Methods 0.000 title claims abstract 3
- 210000000845 cartilage Anatomy 0.000 claims abstract description 22
- 239000012620 biological material Substances 0.000 claims abstract description 15
- 230000003902 lesion Effects 0.000 claims abstract description 15
- 238000010382 chemical cross-linking Methods 0.000 claims abstract description 7
- 238000005520 cutting process Methods 0.000 claims abstract description 7
- 238000005406 washing Methods 0.000 claims abstract description 4
- 230000008439 repair process Effects 0.000 claims description 15
- LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 claims description 10
- 241000283073 Equus caballus Species 0.000 claims description 7
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 claims description 7
- AVJBPWGFOQAPRH-FWMKGIEWSA-L dermatan sulfate Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@H](OS([O-])(=O)=O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](C([O-])=O)O1 AVJBPWGFOQAPRH-FWMKGIEWSA-L 0.000 claims description 7
- 210000001519 tissue Anatomy 0.000 claims description 6
- 239000000203 mixture Substances 0.000 claims description 5
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 claims description 2
- 241000271566 Aves Species 0.000 claims description 2
- 241000283690 Bos taurus Species 0.000 claims description 2
- 229920000045 Dermatan sulfate Polymers 0.000 claims description 2
- 229920000288 Keratan sulfate Polymers 0.000 claims description 2
- 210000001188 articular cartilage Anatomy 0.000 claims description 2
- 229940051593 dermatan sulfate Drugs 0.000 claims description 2
- 229920002674 hyaluronan Polymers 0.000 claims description 2
- 229960003160 hyaluronic acid Drugs 0.000 claims description 2
- KXCLCNHUUKTANI-RBIYJLQWSA-N keratan Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@H](COS(O)(=O)=O)O[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@H](O[C@@H](O[C@H]3[C@H]([C@@H](COS(O)(=O)=O)O[C@@H](O)[C@@H]3O)O)[C@H](NC(C)=O)[C@H]2O)COS(O)(=O)=O)O[C@H](COS(O)(=O)=O)[C@@H]1O KXCLCNHUUKTANI-RBIYJLQWSA-N 0.000 claims description 2
- 230000010534 mechanism of action Effects 0.000 abstract 1
- 102000008186 Collagen Human genes 0.000 description 16
- 108010035532 Collagen Proteins 0.000 description 16
- 229920001436 collagen Polymers 0.000 description 16
- 210000004027 cell Anatomy 0.000 description 14
- 238000002513 implantation Methods 0.000 description 8
- 238000004132 cross linking Methods 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 239000012528 membrane Substances 0.000 description 4
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 238000001574 biopsy Methods 0.000 description 3
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 3
- 230000003833 cell viability Effects 0.000 description 3
- 238000007710 freezing Methods 0.000 description 3
- 230000008014 freezing Effects 0.000 description 3
- 238000010899 nucleation Methods 0.000 description 3
- 230000001954 sterilising effect Effects 0.000 description 3
- 238000004659 sterilization and disinfection Methods 0.000 description 3
- 241000283086 Equidae Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 239000007987 MES buffer Substances 0.000 description 2
- 241000282887 Suidae Species 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- 239000007943 implant Substances 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- OARRHUQTFTUEOS-UHFFFAOYSA-N safranin Chemical compound [Cl-].C=12C=C(N)C(C)=CC2=NC2=CC(C)=C(N)C=C2[N+]=1C1=CC=CC=C1 OARRHUQTFTUEOS-UHFFFAOYSA-N 0.000 description 2
- 238000004626 scanning electron microscopy Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 230000035899 viability Effects 0.000 description 2
- HVCNXQOWACZAFN-UHFFFAOYSA-N 4-ethylmorpholine Chemical compound CCN1CCOCC1 HVCNXQOWACZAFN-UHFFFAOYSA-N 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-M Bisulfite Chemical compound OS([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-M 0.000 description 1
- 229920001287 Chondroitin sulfate Polymers 0.000 description 1
- 102000012422 Collagen Type I Human genes 0.000 description 1
- 108010022452 Collagen Type I Proteins 0.000 description 1
- 108020005199 Dehydrogenases Proteins 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- 201000009859 Osteochondrosis Diseases 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000029797 Prion Human genes 0.000 description 1
- 108091000054 Prion Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- AVJBPWGFOQAPRH-FWMKGIEWSA-N alpha-L-IdopA-(1->3)-beta-D-GalpNAc4S Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@H](OS(O)(=O)=O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](C(O)=O)O1 AVJBPWGFOQAPRH-FWMKGIEWSA-N 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 208000005881 bovine spongiform encephalopathy Diseases 0.000 description 1
- 230000022159 cartilage development Effects 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000002648 chondrogenic effect Effects 0.000 description 1
- 229940059329 chondroitin sulfate Drugs 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 239000000512 collagen gel Substances 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 230000032459 dedifferentiation Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 210000002744 extracellular matrix Anatomy 0.000 description 1
- 239000000834 fixative Substances 0.000 description 1
- 210000004276 hyalin Anatomy 0.000 description 1
- 210000003035 hyaline cartilage Anatomy 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000012606 in vitro cell culture Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 210000003127 knee Anatomy 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000007433 macroscopic evaluation Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000002906 microbiologic effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- VMGAPWLDMVPYIA-HIDZBRGKSA-N n'-amino-n-iminomethanimidamide Chemical compound N\N=C\N=N VMGAPWLDMVPYIA-HIDZBRGKSA-N 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000011164 ossification Effects 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 208000007656 osteochondritis dissecans Diseases 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- DHRLEVQXOMLTIM-UHFFFAOYSA-N phosphoric acid;trioxomolybdenum Chemical compound O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.O=[Mo](=O)=O.OP(O)(O)=O DHRLEVQXOMLTIM-UHFFFAOYSA-N 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 239000008213 purified water Substances 0.000 description 1
- BOLDJAUMGUJJKM-LSDHHAIUSA-N renifolin D Natural products CC(=C)[C@@H]1Cc2c(O)c(O)ccc2[C@H]1CC(=O)c3ccc(O)cc3O BOLDJAUMGUJJKM-LSDHHAIUSA-N 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 230000000472 traumatic effect Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/0068—General culture methods using substrates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/06—Animal cells or tissues; Human cells or tissues
- C12N5/0602—Vertebrate cells
- C12N5/0652—Cells of skeletal and connective tissues; Mesenchyme
- C12N5/0655—Chondrocytes; Cartilage
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2533/00—Supports or coatings for cell culture, characterised by material
- C12N2533/50—Proteins
- C12N2533/54—Collagen; Gelatin
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2533/00—Supports or coatings for cell culture, characterised by material
- C12N2533/70—Polysaccharides
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- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Organic Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Biotechnology (AREA)
- Rheumatology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Cell Biology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Materials For Medical Uses (AREA)
Abstract
Description
Claims (10)
- REVENDICATIONS1. Utilisation d'une matrice comportant du collagène de type Il et des glycosaminoglycanes, comme support de culture ex vivo de chondrocytes humains ou animaux, caractérisée en ce que ladite matrice a été obtenue par un procédé comprenant les étapes suivantes : (a) mélange du collagène de type II et des glycosaminoglycanes, (b) lyophilisation, (c) découpe de la matrice obtenue à l'étape (b) en au moins trois tranches, et élimination de la première tranche et de la dernière tranche, (d) réticulation chimique, et (e) lavage.
- 2. Biomatériau pour la réparation de lésions d'un tissu cartilagineux, constitué d'une matrice réticulée comportant du collagène de type II et des glycosaminoglycanes, caractérisé en ce que (i) la matrice est telle qu'obtenue par un procédé comprenant les étapes suivantes : (a) mélange du collagène de type II et des glycosaminoglycanes, (b) lyophilisation, (c) découpe de la matrice obtenue à l'étape (b) en au moins trois tranches, et élimination de la première tranche et de la dernière tranche, (d) réticulation chimique, et (e) lavage, et (ii) la matrice est colonisée par des chondrocytes sur l'ensemble de son épaisseur.
- 3. Utilisation selon la revendication 1 ou biomatériau selon la revendication 2, caractérisé(e) en ce que la matrice a été réticulée par une solution de N-hydroxysuccinimide (NHS) et d'éthyl-3 (3-diméthylaminopropyl) carbodiimide (EDC).
- 4. Utilisation ou biomatériau selon l'une quelconque des revendications 1 à 3, caractérisé(e) en ce qu'à l'étape (a), le mélange comporte 77 à 90% de collagène de type II et 10 à 23% de glycosaminoglycanes.
- 5. Utilisation ou biomatériau selon l'une quelconque des revendications 1 à 4, caractérisé(e) en ce que la matrice comporte 80 à 90% de collagène de type II et 10 à 20% de glycosaminoglycanes.
- 6. Utilisation ou biomatériau selon l'une quelconque des revendications 1 à 5, caractérisé(e) en ce que le glycosaminoglycane est l'acide chondroitine sulfurique, l'acide hyaluronique, le dermatan sulfate ou le keratan sulfate.
- 7. Utilisation ou biomatériau selon l'une quelconque des revendications 1 à 6, caractérisé(e) en ce que le collagène de type II est dérivé d'un cartilage naturel.
- 8. Utilisation ou biomatériau selon la revendication 7, caractérisé(e) en ce que le cartilage naturel est dérivé du cartilage articulaire porcin, bovin, équin ou aviaire.
- 9. Utilisation ou biomatériau selon l'une quelconque des revendications précédentes, caractérisé(e) en ce que la matrice présente une porosité comprise entre 50 et 150 tm.
- 10. Utilisation ou biomatériau selon l'une quelconque des revendications précédentes, caractérisé(e) en ce que la matrice présente une porosité ouverte sur toutes ses faces.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR1150365A FR2955334B1 (fr) | 2010-01-15 | 2011-01-17 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
FR1000152A FR2955333B1 (fr) | 2010-01-15 | 2010-01-15 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux; |
FR1150365A FR2955334B1 (fr) | 2010-01-15 | 2011-01-17 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux |
Publications (2)
Publication Number | Publication Date |
---|---|
FR2955334A1 true FR2955334A1 (fr) | 2011-07-22 |
FR2955334B1 FR2955334B1 (fr) | 2013-09-06 |
Family
ID=42340603
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FR1000152A Expired - Fee Related FR2955333B1 (fr) | 2010-01-15 | 2010-01-15 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux; |
FR1150365A Active FR2955334B1 (fr) | 2010-01-15 | 2011-01-17 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
FR1000152A Expired - Fee Related FR2955333B1 (fr) | 2010-01-15 | 2010-01-15 | Utilisation d'une matrice de collagene ii reticulee poreuse comme support a la culture de cellules et la regeneration d'un tissu cartilagineux; |
Country Status (1)
Country | Link |
---|---|
FR (2) | FR2955333B1 (fr) |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0296078A1 (fr) * | 1987-06-15 | 1988-12-21 | Centre National De La Recherche Scientifique (Cnrs) | Nouveaux biomatériaux à base de mélanges de collagène, de chitosan et de glycosaminoglycanes, leur procédé de préparation ainsi que leurs applications en médecine humaine |
WO1999019005A1 (fr) * | 1997-10-10 | 1999-04-22 | Ed Geistlich Söhne Ag Für Chemische Industrie | Membrane utilisee dans la regeneration tissulaire |
EP1254670A1 (fr) * | 2001-05-03 | 2002-11-06 | Stichting Katholieke Universiteit | Matrices de collagène II pour la régéneration de cartilage |
-
2010
- 2010-01-15 FR FR1000152A patent/FR2955333B1/fr not_active Expired - Fee Related
-
2011
- 2011-01-17 FR FR1150365A patent/FR2955334B1/fr active Active
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP0296078A1 (fr) * | 1987-06-15 | 1988-12-21 | Centre National De La Recherche Scientifique (Cnrs) | Nouveaux biomatériaux à base de mélanges de collagène, de chitosan et de glycosaminoglycanes, leur procédé de préparation ainsi que leurs applications en médecine humaine |
WO1999019005A1 (fr) * | 1997-10-10 | 1999-04-22 | Ed Geistlich Söhne Ag Für Chemische Industrie | Membrane utilisee dans la regeneration tissulaire |
EP1254670A1 (fr) * | 2001-05-03 | 2002-11-06 | Stichting Katholieke Universiteit | Matrices de collagène II pour la régéneration de cartilage |
Non-Patent Citations (6)
Title |
---|
CHAJRA H ET AL: "Collagen-based biomaterials and cartilage engineering. Application to osteochondral defects", BIO-MEDICAL MATERIALS AND ENGINEERING, IOS PRESS, AMSTERDAM, NL, vol. 18, no. Suppl. 1, 1 January 2008 (2008-01-01), pages S33 - S45, XP009108989, ISSN: 0959-2989 * |
HUI CAO ET AL: "EDC/NHS-crosslinked type II collagen-chondroitin sulfate scaffold: characterization and in vitro evaluation", JOURNAL OF MATERIALS SCIENCE: MATERIALS IN MEDICINE, KLUWER ACADEMIC PUBLISHERS, BO, vol. 19, no. 2, 6 December 2007 (2007-12-06), pages 567 - 575, XP019575683, ISSN: 1573-4838 * |
KO C -S ET AL: "Type II collagen-chondroitin sulfate-hyaluronan scaffold cross-linked by genipin for cartilage tissue engineering", JOURNAL OF BIOSCIENCE AND BIOENGINEERING 2009 ELSEVIER NLD LNKD- DOI:10.1016/J.JBIOSC.2008.09.020, vol. 107, no. 2, February 2009 (2009-02-01), pages 177 - 182, XP002593846, ISSN: 1389-1723 * |
LIEN S -M ET AL: "Effect of pore size on ECM secretion and cell growth in gelatin scaffold for articular cartilage tissue engineering", ACTA BIOMATERIALIA 200902 GB LNKD- DOI:10.1016/J.ACTBIO.2008.09.020, vol. 5, no. 2, February 2009 (2009-02-01), pages 670 - 679, XP002593848, ISSN: 1742-7061 * |
PIEPER J S ET AL: "Crosslinked type II collagen matrices: preparation, characterization, and potential for cartilage engineering", BIOMATERIALS, ELSEVIER SCIENCE PUBLISHERS BV., BARKING, GB LNKD- DOI:10.1016/S0142-9612(02)00067-4, vol. 23, no. 15, 1 August 2002 (2002-08-01), pages 3183 - 3192, XP004354888, ISSN: 0142-9612 * |
VICKERS SCOTT M ET AL: "Effects of cross-linking type II collagen-GAG scaffolds on chondrogenesis in vitro: dynamic pore reduction promotes cartilage formation.", TISSUE ENGINEERING MAY 2006 LNKD- PUBMED:16771647, vol. 12, no. 5, May 2006 (2006-05-01), pages 1345 - 1355, XP002593847, ISSN: 1076-3279 * |
Also Published As
Publication number | Publication date |
---|---|
FR2955333B1 (fr) | 2014-03-21 |
FR2955334B1 (fr) | 2013-09-06 |
FR2955333A1 (fr) | 2011-07-22 |
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