EP1177290A2 - Laminine 5 recombinee - Google Patents

Laminine 5 recombinee

Info

Publication number
EP1177290A2
EP1177290A2 EP00928524A EP00928524A EP1177290A2 EP 1177290 A2 EP1177290 A2 EP 1177290A2 EP 00928524 A EP00928524 A EP 00928524A EP 00928524 A EP00928524 A EP 00928524A EP 1177290 A2 EP1177290 A2 EP 1177290A2
Authority
EP
European Patent Office
Prior art keywords
laminin
chain
recombinant
polypeptide
cells
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Withdrawn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
EP00928524A
Other languages
German (de)
English (en)
Inventor
Ariel Partners II Building BOUTAUD
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.)
Biostratum Inc
Original Assignee
Biostratum Inc
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 Biostratum Inc filed Critical Biostratum Inc
Publication of EP1177290A2 publication Critical patent/EP1177290A2/fr
Withdrawn legal-status Critical Current

Links

Classifications

    • 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
    • C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
    • A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
    • A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P17/00—Drugs for dermatological disorders
    • A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P21/00—Drugs for disorders of the muscular or neuromuscular system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P25/00—Drugs for disorders of the nervous system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P27/00—Drugs for disorders of the senses
    • A61P27/02—Ophthalmic agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
    • A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P9/00—Drugs for disorders of the cardiovascular system
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P9/00—Drugs for disorders of the cardiovascular system
    • A61P9/14—Vasoprotectives; Antihaemorrhoidals; Drugs for varicose therapy; Capillary stabilisers
    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N31/00—Investigating or analysing non-biological materials by the use of the chemical methods specified in the subgroup; Apparatus specially adapted for such methods
    • G01N31/22—Investigating or analysing non-biological materials by the use of the chemical methods specified in the subgroup; Apparatus specially adapted for such methods using chemical indicators
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide
    • C07K2319/01—Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/02—Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

Definitions

  • Laminins are a family of heterotrimeric glycoproteins that reside primarily in the basal lamina. They function via binding interactions with neighboring cell receptors, and are important signaling molecules that can strongly influence cellular function. Laminins are important in both maintaining cell/tissue phenotype as well as promoting cell growth and differentiation in tissue repair and development.
  • the long arm of the cross is composed of the C-terminal parts of the tliree chains, which together form a coiled coil structure. (Wewer and Engvall, 1996) The long arm ends with the globular G domain. The coiled-coil domain ofthe long arm is crucial for assembly of the three chains of laminin. (Yurchenco et al, Proc. Natl. Acad. Sci. 94:10189-10194 (1997)). Disulfide bonds bridge and stabilize all three chains in the most proximal region of the long arm and join the ⁇ and ⁇ chains in the most distal region of the long arm.
  • pancreatic beta islet cells Proliferation of pancreatic beta islet cells (Todorov et al., Transplant. Proc. 1998 Mar; 30(2): 455; Quaranta and Jones, U.S. Patent No. 5,510,263; Halberstadt et al, U.S. Patent No. 5,681,587; Halberstadt et al., U.S. Patent No. 5,672,361), and T cells (Vivinus- Nebot et al., J. Cell Biol. 1999 Feb 8; 144(3):563-574)
  • conservative polynucleotide variants may be generated to improve or alter the characteristics of the expressed laminin chain polypeptides.
  • one or more amino acids can be deleted from the N-terminus or C-terminus of the secreted protein.
  • Ample evidence demonstrates that variants often retain a biological activity similar to that of the naturally occurring protein.
  • Gayleet al., J. Biol. Chem 268:22105- 22111 (1993) Furthermore, even if deleting one or more amino acids from the N-terminus or C-terminus of a polypeptide results in modification or loss of one or more biological functions, other biological activities may still be retained.
  • the "substantially similar" polypeptides of the present invention also include (i) substitutions with one or more of the non-conserved amino acid residues, where the substituted amino acid residues may or may not be one encoded by the genetic code, or (ii) substitution with one or more of amino acid residues having a substituent group; (iii) fusion of the mature polypeptide with another compound, such as a compound to increase the stability and/or solubility of the polypeptide (for example, polyethylene glycol); and/or (iv) fusion of the polypeptide with additional amino acids, such as an IgG Fc fusion region peptide, or leader or secretory sequence, or a sequence facilitating purification.
  • substitutions with one or more of the non-conserved amino acid residues where the substituted amino acid residues may or may not be one encoded by the genetic code, or (ii) substitution with one or more of amino acid residues having a substituent group
  • fusion of the mature polypeptide with another compound
  • Transfection of expression vectors into the host cells can be accomplished via any technique known in the art, including but not limited to standard bacterial transformation, calcium phosphate co-precipitation, electroporation, or liposome mediated-, DEAE dextran mediated-, polycationic mediated-, or viral mediated transfection.
  • Media from cells transfected with a single laminin chain are initially analyzed on Western blots using chain-specific anti-laminin-5 antibodies.
  • the expression of single laminin chains following transfection is generally intracellular.
  • Clones showing reactivity against individual transfected chain(s) are verified by any appropriate method, such as PCR, reverse transcription-PCR, or nucleic acid hybridization, to confirm incorporation of the transfected gene.
  • analysis of genomic DNA preparations from such clones is done by PCR using laminin chain-specific primer pairs.
  • no epitope tag is fused to any of the r-laminin 5 chains, and the r-laminin 5 is purified by standard techniques, including but not limited to affinity chromatography using laminin 5 specific antibodies or other laminin 5 binding molecules.
  • Suitable solutions for use in accordance with the invention are sterile, are not harmful for the proposed application, and may be subjected to conventional pharmaceutical operations such as sterilization and/or may contain conventional adjuvants, such as preservatives, stabilizers, wetting agents, emulsifiers, buffers etc.
  • conventional adjuvants such as preservatives, stabilizers, wetting agents, emulsifiers, buffers etc.
  • the pharmaceutical compositions of the present invention may be in the form of toothcreams, toothpastes, liquid dentifrices, tooth-powders chewing-gum, tablets and the like.
  • the pharmaceutical compositions of the invention can also contain flavoring, coloring agents, sweeteners, preservatives, surface active agents, and the like.
  • the present invention provides a method of treating Type I diabetes in a patient in need thereof comprising contacting pancreatic beta islet cells with an amount effective of r-laminin 5 to provide an efficient adhesion substrate for the cells, leading to increased proliferation of insulin-producing pancreatic beta islet cells, and administering the cells to a patient in need thereof.
  • Type I diabetes insulin-dependent
  • the pancreas has lost its ability to secrete insulin due to an autoimmune disorder in which the insulin-secreting beta cells, found within the islet cells of the pancreas, are destroyed.
  • insulin injections can compensate for beta cell destruction, blood sugar levels can still fluctuate dramatically.
  • the impaired ability to take up glucose from the blood results in side reactions in which toxic products accumulate, leading to complications including blindness, kidney disease, nerve damage, and, ultimately, coma and death.

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • General Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Pharmacology & Pharmacy (AREA)
  • General Chemical & Material Sciences (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Animal Behavior & Ethology (AREA)
  • Diabetes (AREA)
  • Neurology (AREA)
  • Dermatology (AREA)
  • Cardiology (AREA)
  • Molecular Biology (AREA)
  • Heart & Thoracic Surgery (AREA)
  • Biophysics (AREA)
  • Biochemistry (AREA)
  • Genetics & Genomics (AREA)
  • Orthopedic Medicine & Surgery (AREA)
  • Neurosurgery (AREA)
  • Ophthalmology & Optometry (AREA)
  • Biomedical Technology (AREA)
  • Toxicology (AREA)
  • Zoology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Obesity (AREA)
  • Hematology (AREA)
  • Endocrinology (AREA)
  • Emergency Medicine (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Vascular Medicine (AREA)
  • Physical Education & Sports Medicine (AREA)
  • Physics & Mathematics (AREA)
  • Analytical Chemistry (AREA)

Abstract

L'invention concerne la laminine 5 recombinée, des procédés de fabrication de la laminine 5, des cellules exprimant la laminine 5 recombinée ainsi que des techniques d'utilisation de la laminine 5 recombinée pour accélérer la cicatrisation et pour favoriser la fixation et la migration des cellules.
EP00928524A 1999-04-30 2000-04-28 Laminine 5 recombinee Withdrawn EP1177290A2 (fr)

Applications Claiming Priority (7)

Application Number Priority Date Filing Date Title
US13172099P 1999-04-30 1999-04-30
US131720P 1999-04-30
US14973899P 1999-08-21 1999-08-21
US149738P 1999-08-21
US15594599P 1999-09-24 1999-09-24
US155945P 1999-09-24
PCT/US2000/011459 WO2000066731A2 (fr) 1999-04-30 2000-04-28 Laminine 5 recombinee

Publications (1)

Publication Number Publication Date
EP1177290A2 true EP1177290A2 (fr) 2002-02-06

Family

ID=27384196

Family Applications (1)

Application Number Title Priority Date Filing Date
EP00928524A Withdrawn EP1177290A2 (fr) 1999-04-30 2000-04-28 Laminine 5 recombinee

Country Status (4)

Country Link
EP (1) EP1177290A2 (fr)
JP (1) JP2002542824A (fr)
AU (1) AU4675300A (fr)
WO (1) WO2000066731A2 (fr)

Families Citing this family (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2002050111A2 (fr) 2000-12-21 2002-06-27 Biostratum, Inc. Laminine 10 isolee
JP4798560B2 (ja) * 2003-06-04 2011-10-19 よこはまティーエルオー株式会社 ラミニン５ｂ
JP4566603B2 (ja) * 2004-03-31 2010-10-20 財団法人かずさディー・エヌ・エー研究所 細胞付着ポリペプチド
FR2873698B1 (fr) 2004-07-29 2006-10-20 D Anjou Sa Lab Nouveau peptide et composition pharmaceutique le contenant
WO2006091675A2 (fr) * 2005-02-23 2006-08-31 Surmodics, Inc. Articles medicaux implantables a revetement de laminine et methodes d'utilisation
FR2943062B1 (fr) * 2009-03-13 2011-04-08 Symatese Nouveau peptide promoteur de l'adhesion et de la migration cellulaire
CN105814195A (zh) 2013-11-27 2016-07-27 京都府公立大学法人 层粘连蛋白应用于角膜内皮细胞培养
US11918630B2 (en) 2014-10-31 2024-03-05 Kyoto Prefectural Public University Corporation Treatment of retina and nerve using laminin
CN113559246A (zh) 2014-10-31 2021-10-29 京都府公立大学法人 使用层粘连蛋白的新的角膜的治疗
JP6792852B2 (ja) * 2016-06-07 2020-12-02 国立大学法人 岡山大学 角化歯肉誘導剤
US11655451B2 (en) * 2017-05-05 2023-05-23 National University Of Singapore Methods for culturing human keratinocytes
FR3127219A1 (fr) 2021-09-20 2023-03-24 Laboratoires D'anjou Nouveaux peptides et compositions pharmaceutiques et cosmetiques les contenants

Family Cites Families (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
ES8802441A1 (es) * 1985-06-03 1988-06-16 Meloy Lab Procedimiento para preparar laminina humana
WO1994005316A1 (fr) * 1992-08-28 1994-03-17 The State Of Oregon Acting By And Through The State Board Of Higher Education On Behalf Of Oregon Health Sciences University Produits et procedes destines a ameliorer l'adhesion du keratinocyte sur le derme
US5422264A (en) * 1993-11-12 1995-06-06 Desmos, Inc. Soluble factor stimulation of attachment and hemidesmosome assembly in epithelial cells
US5610031A (en) * 1993-10-27 1997-03-11 The General Hospital Corporation B1k chain of laminin and methods of use
US5660982A (en) * 1994-10-04 1997-08-26 Tryggvason; Karl Laminin chains: diagnostic uses
US5681587A (en) * 1995-10-06 1997-10-28 Desmos, Inc. Growth of adult pancreatic islet cells
EP0889743A1 (fr) * 1996-03-29 1999-01-13 Desmos, Inc. Fixation de cellules sur des dispositifs trans-epitheliaux recouverts de laminine 5
JP2000513220A (ja) * 1996-06-05 2000-10-10 ザ ジェネラル ホスピタル コーポレイション ラミニン―５及び基底膜構造の形成
US5760179A (en) * 1996-06-10 1998-06-02 Desmos, Inc. Purification of soluble laminin 5
CA2265923A1 (fr) * 1996-09-13 1998-03-19 Sagami Chemical Research Center Proteines humaines comportant des sequences de signaux secretoires et adn codant ces proteines

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See references of WO0066731A2 *

Also Published As

Publication number Publication date
WO2000066731A2 (fr) 2000-11-09
JP2002542824A (ja) 2002-12-17
AU4675300A (en) 2000-11-17
WO2000066731A3 (fr) 2001-06-28

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