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EP1446441A1 - Procede de traitement de materiaux d'origine biologique et produit a base de collagene et d'elastine - Google Patents

Procede de traitement de materiaux d'origine biologique et produit a base de collagene et d'elastine

Info

Publication number
EP1446441A1
EP1446441A1 EP02787383A EP02787383A EP1446441A1 EP 1446441 A1 EP1446441 A1 EP 1446441A1 EP 02787383 A EP02787383 A EP 02787383A EP 02787383 A EP02787383 A EP 02787383A EP 1446441 A1 EP1446441 A1 EP 1446441A1
Authority
EP
European Patent Office
Prior art keywords
collagen
materials
solution
elastin
accompanying substances
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.)
Withdrawn
Application number
EP02787383A
Other languages
German (de)
English (en)
Inventor
Leon Olde Damink
Ingo Heschel
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Matricel GmbH
Original Assignee
Matricel GmbH
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Matricel GmbH filed Critical Matricel GmbH
Publication of EP1446441A1 publication Critical patent/EP1446441A1/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L27/00—Materials for grafts or prostheses or for coating grafts or prostheses
    • A61L27/36—Materials for grafts or prostheses or for coating grafts or prostheses containing ingredients of undetermined constitution or reaction products thereof, e.g. transplant tissue, natural bone, extracellular matrix
    • A61L27/3683—Materials for grafts or prostheses or for coating grafts or prostheses containing ingredients of undetermined constitution or reaction products thereof, e.g. transplant tissue, natural bone, extracellular matrix subjected to a specific treatment prior to implantation, e.g. decellularising, demineralising, grinding, cellular disruption/non-collagenous protein removal, anti-calcification, crosslinking, supercritical fluid extraction, enzyme treatment
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L27/00—Materials for grafts or prostheses or for coating grafts or prostheses
    • A61L27/14—Macromolecular materials
    • A61L27/22—Polypeptides or derivatives thereof, e.g. degradation products
    • A61L27/24—Collagen
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L31/00—Materials for other surgical articles, e.g. stents, stent-grafts, shunts, surgical drapes, guide wires, materials for adhesion prevention, occluding devices, surgical gloves, tissue fixation devices
    • A61L31/005—Ingredients of undetermined constitution or reaction products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61L—METHODS OR APPARATUS FOR STERILISING MATERIALS OR OBJECTS IN GENERAL; DISINFECTION, STERILISATION OR DEODORISATION OF AIR; CHEMICAL ASPECTS OF BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES; MATERIALS FOR BANDAGES, DRESSINGS, ABSORBENT PADS OR SURGICAL ARTICLES
    • A61L31/00—Materials for other surgical articles, e.g. stents, stent-grafts, shunts, surgical drapes, guide wires, materials for adhesion prevention, occluding devices, surgical gloves, tissue fixation devices
    • A61L31/04—Macromolecular materials
    • A61L31/043—Proteins; Polypeptides; Degradation products thereof
    • A61L31/044—Collagen

Definitions

  • the invention relates to a method for treating materials of biological origin, such as membranes, skins, vessels, heart valves, tendons, and ligaments, in which hydrophobic accompanying substances are chemically removed, and an elastin product.
  • the invention relates to a processing method for collagen materials that can be used in a largely unchanged starting structure or that can be further processed into other structures.
  • collagen materials used in this invention is a simplified term for the materials of biological origin consisting in part of several structural proteins and supporting proteins.
  • elastin in particular may also be present in a considerable amount in some cases and may be desirable for certain applications
  • These collagen materials are obtained from animal membranes such as the intestine, fascia lata, pericardium, peritoneum, omentum or dura mater.
  • Other options are the processing of heart valves or blood vessels.
  • hides, ligaments such as ligamentum nuchae, ligamentum cruciatum and tendons such as Achilles tendons can be processed into collagen fibers which are either used directly or used to produce wound dressings, sponges, cell support structures and the like.
  • non-collagenic accompanying substances Before the collagen structures can be used in or on a patient's body, all cells and non-collagenic accompanying substances must first be removed in order to ensure a safe tissue reaction and to avoid immune reactions.
  • non-collagenous accompanying substances are non-structural proteins, proteoglycans, which consist of proteins and glycosaminoglycans, and lipids.
  • proteoglycans which consist of proteins and glycosaminoglycans
  • lipids A distinction can be made between lipids composed of fatty acids and steroid-like lipids. When removing these accompanying substances, it must be ensured that the collagen is carefully removed from the accompanying substances without the helical collagen structure being impaired.
  • the starting materials are mechanically degreased in a first process step and treated with strong alkali until the amide nitrogen is 0.35 mmol / g or less.
  • the materials are then treated with strong acid and possibly enzymes, which is intended to clean the collagen raw material from accompanying impurities.
  • WO 90/03811 describes a method in which pericardial membranes are degreased mechanically, treated with a basic solution and sodium chloride solution as well as a complexing agent and an acidic buffer system. Only in the last process step are the membranes degreased with acetone. According to WO 95/18638, membranes are cleaned by a sequence of alkaline solution wash, acid solution wash, water wash and subsequent drying and degreased in the last process step.
  • the middle step of removing cells and other accompanying substances takes place in an aqueous environment and it is very important in this process step that the aqueous phase penetrates into the collagen structures not only on a macroscopic but also on a microscopic and molecular level in order to ensure complete and guarantee deep cleaning of the collagen structures.
  • this is only insufficiently possible with the known methods.
  • the invention is based on the problem that there is a significant amount of lipids in the deeper collagen structures. These lipids are water-repellent and therefore prevent water from entering at the molecular level. Although in some of the known processes a part of the lipids is mechanically removed before the aqueous process steps are started, it can never be guaranteed that the mechanical removal of the lipids is sufficient to provide a good cleaning. There can even be an unfavorable case in which the lipids are inadvertently lubricated into the collagen structures during the mechanical removal. There is also the risk that excessive mechanical degreasing in some tissues will destroy the sensitive collagen structures
  • This procedure describes an effective method for removing lipids and hydrophobic substances from tissue structures.
  • the lipids can be removed completely without the lipids first having to be chemically changed.
  • aqueous cleaning can take place without the risk of parts the collagen structure is not accessible to aqueous solutions due to the remaining hydrophobic substances It is advantageous if the collagen materials are disinfected before the hydrophobic accompanying substances are removed.
  • hydrophobic accompanying substances are removed by washing with a water-miscible organic solvent, such as, for example, alcohols or acetone. This enables the lipids to be removed without chemical modification of the lipids. Mixtures of water-miscible solvents with each other or with water also lead to positive process results.
  • a water-miscible organic solvent such as, for example, alcohols or acetone.
  • surfactants Another possibility of removing hydrophobic accompanying substances is washing with surfactants.
  • biologically harmless anionic or cationic or non-ionic surfactants are preferably used.
  • surfactants are Triton X-100, tripolyphosphate or surfactants from the Tween® series, such as Tween® 20 (polyoxyethylene sorbitan monooleate).
  • Non-hydrophobic accompanying substances can be removed with a solution which removes hydrogen-bonded substances, in particular a urea solution.
  • non-hydrophobic accompanying substances can be removed with an aqueous solution of inorganic salts, in particular with a buffered sodium, potassium or calcium chloride solution, which preferably contains enzyme inhibitors.
  • non-hydrophobic accompanying substances are removed with an alkaline solution, such as, for example, sodium, potassium or calcium hydroxide solution.
  • non-hydrophobic accompanying substances are removed with an acidic solution, such as, for example, hydrochloric acid, sulfuric acid or acetic acid.
  • the materials of biological origin are made up into cleaned membranes, heart valves or vessels or are further processed into collagen solutions, collagen fibers, collagen fiber braids, collagen fiber tissues or KoUagen sponges.
  • Packaging is understood to mean, for example, cutting, expanding or chemically crosslinking the treated materials.
  • nativity of the materials of biological origin is set to a value below 95%, in many applications, such as in particular for cartilage regeneration, better cell culture results are shown than with membranes whose nativity is significantly higher.
  • the method according to the invention makes it possible to colonize the treated collagen materials with cells because of the high reproducibility. For example, collagen materials treated in this way have been populated with various skin cells, nerve cells and in particular cartilage cells. The materials of biological origin treated in this way and also the further processed and assembled materials can be used for controlled tissue regeneration.
  • the problem on which the invention is based is also solved with a collagen-elastin product from insoluble collagen, the product having insoluble elastin.
  • the tendency to calcification of such collagen-elastin products in vivo is significantly reduced.
  • the addition of insoluble elastin can increase the elasticity and improve the strength of the product. If the elastin is already contained in the biological starting material, the advantage of working up the material according to the invention arises almost automatically.
  • the elastin is processed in such a way that at least 20% elastin fibers have the originally existing fibrillin structure.
  • the elastin fibers with the originally existing fibrillin structure can be detected microscopically or histologically.
  • the invented The advantage of the addition of elastin according to the invention becomes less and less with further processing and is practically completely lost when admixing soluble elastin.
  • pericardial membranes 10 kg are inactivated and disinfected for one hour in 50 liters of 1.0 N sodium hydroxide solution.
  • the lye bath temperature is 20 ° C.
  • a hydrochloric acid solution is added for neutralization (pH between 6.0 and 8.0).
  • the membranes are washed 3 times with water to remove neutralization residues. Then the membranes are degreased in three stages, each with 50 liters of acetone.
  • the membranes are washed 3 times with water.
  • the membranes are cleaned with sodium hydroxide solution 0.05 N - 0.1 N for about 1 to 21 days.
  • the pH of the lye is between 12 and 14 during this time.
  • a hydrochloric acid solution is added for neutralization.
  • the membranes are washed 3 times with water.
  • the membranes are dewatered with acetone and then air dried.
  • the dried product consists of a collagen fiber braid in which the natural fiber arrangement is still present.
  • the membranes can be used as support and implant material for surgical operations, as a membrane for controlled tissue regeneration or as a carrier for cell cultures. If necessary, the Strength and the rate of degradation of the membranes can be specifically optimized by chemical crosslinking. Conventional crosslinking methods with glutaraldehyde, hexamethylene diisocyanate, carbodiimide or polyepoxide can be used for this.
  • peritoneum membranes 10 kg are inactivated and disinfected in 50 liters of 1.0 N sodium hydroxide solution for one hour.
  • the bath temperature should be 20 ° C.
  • Sodium chloride can be added to suppress excessive swelling.
  • a hydrochloric acid solution is added for neutralization, so that a pH between 6.0 and 8.0 is reached.
  • the peritoneum membranes are washed 3 times with water.
  • the membranes are degreased with 3 x 50 liters of acetone.
  • the membranes are washed 3 times with water.
  • the membranes are washed with buffered sodium chloride solutions that contain enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleimide (NEM).
  • enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleimide (NEM).
  • the membranes are washed 3 times with water to remove salt residues.
  • the membranes are washed with a 4 M urea solution.
  • the membranes are washed 3 times with water to remove residual urea.
  • the membranes are cleaned with sodium hydroxide solution 0.05 N - 0.1 N for about 1 to 21 days.
  • the pH of the lye is between 12 and 14 during this time.
  • a hydrochloric acid solution is added for neutralization.
  • the membranes are washed 3 times with water.
  • the membranes are dewatered with 3 x 50 liters of acetone for about 30 to 60 minutes and then dried.
  • the dried product consists of a collagen elastin fiber braid in which the natural fiber arrangement is still present.
  • the elastin fibers still contain the naturally existing fibrillin structures.
  • the membranes can be used as support and implant material for surgical operations, as a membrane for controlled tissue regeneration or as a carrier for cell cultures. If necessary, the strength and rate of degradation of the membranes can be specifically optimized by chemical crosslinking. Conventional crosslinking methods with glutaraldehyde, hexamethylene diisocyanate, carbodiimide or polyepoxide can be used for this.
  • the tendons are crushed to optimize the degreasing process.
  • the tendons are degreased with 3 x 50 liters of acetone.
  • the tendons are washed 3 times with water to remove acetone residues.
  • the tendons are washed with buffered sodium chloride solutions containing enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleimide (NEM).
  • enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleimide (NEM).
  • the tendons are washed 3 times with water.
  • the tendons are treated with a 4 M urea solution.
  • the tendons are washed 3 times with water to remove residual urea.
  • the tendons are about 0.05 N - 0.1 N (0.2% - 0.4%) with caustic soda solution Cleaned for 1 to 21 days.
  • the pH of the lye is between 12 and 14 during this time.
  • a hydrochloric acid solution is added for neutralization.
  • the tendons are washed 3 times with water.
  • the tendons are cleaned with a hydrochloric acid solution 0.05 N - 1.0 N for about 1 hour to 7 days.
  • the pH of the solution is between 0 and 3 during this time.
  • a lye is added for neutralization.
  • the tendons are washed 3 times with water.
  • the tendons are dried with acetone or by freeze-drying.
  • cleaned collagen fibers are produced, which are used for the production of fiber fabrics, fiber braids, sponges or as a coating material for e.g. B. synthetic vascular prostheses can be used.
  • the strength and degradation rate of these products can be specifically optimized by chemical crosslinking.
  • Common cross-linking methods with glutaraldehyde, hexamethylene diisocyanate, carbodiimide or polyepoxide can be used for this.
  • neck straps e.g. Ligamentum Nuchea
  • the bath temperature should be 20 ° C.
  • the neck bands are crushed to optimize the degreasing process.
  • the neck straps are degreased with 3 x 50 liters of acetone.
  • the neck bands are washed 3 times with water to remove the acetone.
  • the neck straps are washed with buffered sodium chloride solutions containing enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleinimide (NEM).
  • enzyme inhibitors such as ethylenediaminetetraacetic acid (EDTA) or N-ethylmaleinimide (NEM).
  • EDTA ethylenediaminetetraacetic acid
  • NEM N-ethylmaleinimide
  • Ethylendiamine tetraacetic acid (EDTA) or N-ethylmaleimide (NEM) contain.
  • the neck straps are washed 3 times with water.
  • the neck straps are washed with 4 M urea solution.
  • the neck bands are washed with 3 x 50 liters of water for about 30 to 60 minutes to remove residual urea.
  • the neck straps are cleaned with caustic soda solution 0.05 N - 0.1 N (0.2% - 0.4%) for about 1 to 21 days.
  • the pH of the lye is between 12 and 14 during this time.
  • a hydrochloric acid solution is added for neutralization (pH between 6.0 and 8.0).
  • the neck straps are washed 3 times with water.
  • the neck bands are cleaned with a hydrochloric acid solution 0.05 N - 1.0 N for about 1 hour to 7 days.
  • the pH of the solution is between 0 and 3 during this time.
  • a lye is added for neutralization.
  • the neck straps are washed 3 times with water.
  • the neck tape fibers are dried by dewatering with acetone or by freeze-drying.
  • an optimal mixture of cleaned Contain elastin fibers and purified collagen fibers By working up the neck band, an optimal mixture of cleaned Contain elastin fibers and purified collagen fibers.
  • the elastin fibers still contain the naturally existing fibrillin structures.
  • This mixture can be used for the production of fiber fabrics, fiber braids, sponges or as a coating material for synthetic vascular prostheses.
  • this mixture can also be used after the addition of collagen fibers from Example 3 for the production of fiber fabrics, fiber braids, sponges or as a coating material for synthetic vascular prostheses.
  • the neck tape fibers can be used to make fiber fabrics, braids or sponges. If necessary, the strength and rate of degradation of the products can be optimized by chemical crosslinking as described above.
  • the mass fraction of the lipids is typically still between 15% and 20% even after the cleaning step with an acid has been completed.
  • the mass fraction of the lipids is typically less than 0.5%, so that optimal accessibility of the collagen membranes is guaranteed for the subsequent aqueous cleaning processes.
  • Ash value 0.1 - 0.2% (w / w)
  • Lipid content ⁇ 0.5% (w / w)
  • nativity of the membranes was determined according to the method developed by Bank, which is described in detail in: Bank R.A. et al: A simplified measurement of degraded collagen in tissues: Application in healthy, fibrillated and osteoarthritic cartilage, Matrix Biology 16, 233-243 (1997).
  • the purity of collagen structures can be directly related to the remaining amounts of glucosamine and galactosamine in the material. These two substances are characteristic marker molecules for the presence of glucosaminoglycans, that is to say of non-collagen molecules which are to be removed in the course of the cleaning process.
  • glucosamine and galactosamine contents of freshly obtained collagen membranes from the slaughterhouse are compared to the values of commercially available collagen membranes that were not chemically degreased before the aqueous cleaning steps and collagen membranes produced according to the invention.
  • the glucosamine and galactosamine contents were determined by an amino acid analysis following acid hydrolysis of the starting material. terials determined with 6 M hydrochloric acid, the contents being expressed as the number of molecules per 1000 molecules (n / lOOOn).
  • the cultivability of commercial and collagen membranes produced according to the invention with biological cells was investigated using the example of colonization with chondrocytes.
  • the following table shows the results of the cell numbers and cell vitality following a three-day cell cultivation. All membranes were populated with an identical number of starting cells, the cells being taken from the same cell suspension and then cultivated under the same conditions.

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Veterinary Medicine (AREA)
  • Chemical & Material Sciences (AREA)
  • Public Health (AREA)
  • General Health & Medical Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • Epidemiology (AREA)
  • Oral & Maxillofacial Surgery (AREA)
  • Heart & Thoracic Surgery (AREA)
  • Dermatology (AREA)
  • Transplantation (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Vascular Medicine (AREA)
  • Surgery (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biophysics (AREA)
  • Engineering & Computer Science (AREA)
  • Biomedical Technology (AREA)
  • Botany (AREA)
  • Materials For Medical Uses (AREA)

Abstract

Afin de parvenir à un traitement reproductible de matériaux d'origine biologique, tels que par exemple des membranes, des peaux, des vaisseaux, des valvules du coeur, des tendons et des ligaments, et notamment des matériaux collagène, des substances associées hydrophobes sont d'abord éliminées par voie chimique, sans que ces substances associées ne soient modifiées par voie chimique. Des substances associées non hydrophobes sont ensuite éliminées. Les matériaux ainsi traités sont façonnés pour donner lieu à des membranes, des valvules du coeur ou des vaisseaux ou bien sont soumis à d'autres traitements pour former des solutions, des fibres, des structures fibreuses, des tissus fibreux ou des éponges et sont également éventuellement peuplés de cellules et/ou utilisés pour régénérer des tissus de manière commandée.
EP02787383A 2001-11-22 2002-11-21 Procede de traitement de materiaux d'origine biologique et produit a base de collagene et d'elastine Withdrawn EP1446441A1 (fr)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DE10157182A DE10157182A1 (de) 2001-11-22 2001-11-22 Verfahren zur Behandlung von Materialien biologischen Ursprungs und Elastin-Produkt
DE10157182 2001-11-22
PCT/DE2002/004278 WO2003046055A1 (fr) 2001-11-22 2002-11-21 Procede de traitement de materiaux d'origine biologique et produit a base de collagene et d'elastine

Publications (1)

Publication Number Publication Date
EP1446441A1 true EP1446441A1 (fr) 2004-08-18

Family

ID=7706500

Family Applications (1)

Application Number Title Priority Date Filing Date
EP02787383A Withdrawn EP1446441A1 (fr) 2001-11-22 2002-11-21 Procede de traitement de materiaux d'origine biologique et produit a base de collagene et d'elastine

Country Status (5)

Country Link
US (1) US20040265785A1 (fr)
EP (1) EP1446441A1 (fr)
AU (1) AU2002351688A1 (fr)
DE (2) DE10157182A1 (fr)
WO (1) WO2003046055A1 (fr)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2009017646A2 (fr) * 2007-07-27 2009-02-05 Humacyte, Inc. Compositions et procédés pour une augmentation de tissu mou
EP2412795B1 (fr) * 2009-03-27 2016-12-28 Maruha Nichiro Corporation Matériau réticulé à base d'élastine et de collagène, et son utilisation
EP3034103A1 (fr) 2014-12-15 2016-06-22 Geistlich Pharma AG Éponge de Collagène
CN104874012B (zh) * 2015-05-05 2017-05-31 四川大学 蓬松型皮胶原止血材料及其制备方法
US20190298883A1 (en) * 2018-03-30 2019-10-03 Case Western Reserve University Insoluble native collagen fibers and their use in cell aggregates and tissue constructs
CN115697428A (zh) * 2020-04-03 2023-02-03 生命细胞公司 含有原弹性蛋白的脂肪组织基质

Family Cites Families (19)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE2854490C2 (de) * 1978-12-16 1981-04-09 B. Braun Melsungen Ag, 3508 Melsungen Knochenersatzmaterial mit verbesserter biologischer Stabilität auf Basis von Kollagen
US4985270A (en) * 1988-01-26 1991-01-15 The Nutrasweet Company Cream substitute ingredient and food products
EP0331786B1 (fr) * 1988-03-11 1994-08-03 CHEMOKOL G.b.R. Ing.-Büro für Kollagenprodukte Procédé pour la préparation de membranes de collagène pour hémostase, traitement de blessures, et implants
DE3835237C1 (fr) * 1988-10-15 1989-12-28 B. Braun Melsungen Ag, 3508 Melsungen, De
AT398276B (de) * 1989-05-31 1994-11-25 Sorin Biomedica Spa Verfahren zur präparierung von biologischem implantationsmaterial
FR2649982B1 (fr) * 1989-07-20 1991-09-27 Inst Nat Sante Rech Med Membrane biologique artificielle
FR2654625B1 (fr) * 1989-11-22 1992-02-21 Transphyto Sa Procede de fabrication d'un materiau pour osteoplastie a partir d'un tissu osseux naturel et materiau obtenu par ce procede.
IT1251701B (it) * 1991-10-16 1995-05-19 Angra Srl Soluzione di collagene marino con elastina e relativo metodo di estrazione.
US5676698A (en) * 1993-09-07 1997-10-14 Datascope Investment Corp. Soft tissue implant
DE4332211A1 (de) * 1993-09-22 1995-03-23 Oscar Sergio Baldomero Verfahren zur Langzeitkonservierung von Geweben und Organen
US5441491A (en) * 1994-02-04 1995-08-15 Verschoor; Jacob Method and composition for treating biopsy wounds
GB9402348D0 (en) * 1994-02-08 1994-03-30 Chapman Thomas B Method of manufacture of d limonene skin emulsion
ATE181745T1 (de) * 1994-08-16 1999-07-15 Frische Gmbh Verfahren zur gewinnung von nicht wasserlöslichen, nativen produkten aus nativen stoffgemengen mit hilfe der zentrifugalkraft
DE19541555C2 (de) * 1995-11-08 1997-09-11 Henkel Kgaa Verfahren zur Herstellung wasserunlöslicher, vernetzerfreier Kollagenschwämme
US6024735A (en) * 1996-03-20 2000-02-15 Lifenet Research Foundation Process and composition for cleaning soft tissue grafts optionally attached to bone and soft tissue and bone grafts produced thereby
DE19834087C1 (de) * 1998-07-29 2000-03-30 Mirzaie Sedaposhteh Massoud Wäßrige Konservierungslösung und Verfahren zur Aufbewahrung tierischen Gewebes
MXPA02000937A (es) * 1999-07-28 2002-07-30 Regeneration Tech Inc Implantes de tejidos con antigenicidad reducida (tar).
FR2798294B1 (fr) * 1999-09-10 2001-10-12 Ost Dev Procede de fabrication d'un materiau de prothese osseuse par traitement d'un tissu osseux naturel
WO2002076285A2 (fr) * 2001-03-23 2002-10-03 Histogenics Corporation Composition et methodes de production de tissus biologiques et de constructions tissulaires

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO03046055A1 *

Also Published As

Publication number Publication date
US20040265785A1 (en) 2004-12-30
DE10157182A1 (de) 2003-06-05
WO2003046055A1 (fr) 2003-06-05
AU2002351688A1 (en) 2003-06-10
DE10295506D2 (de) 2004-10-07

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