EP1177290A2 - Rekombinantes laminin 5 - Google Patents
Rekombinantes laminin 5Info
- 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- Withdrawn
Links
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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
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- 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
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- 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)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Diabetes (AREA)
- Heart & Thoracic Surgery (AREA)
- Dermatology (AREA)
- Cardiology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Neurology (AREA)
- Biomedical Technology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Obesity (AREA)
- Neurosurgery (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Hematology (AREA)
- Endocrinology (AREA)
- Genetics & Genomics (AREA)
- Emergency Medicine (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Vascular Medicine (AREA)
- Ophthalmology & Optometry (AREA)
- Physical Education & Sports Medicine (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
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 (en) | 1999-04-30 | 2000-04-28 | Recombinant laminin 5 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| EP1177290A2 true EP1177290A2 (de) | 2002-02-06 |
Family
ID=27384196
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP00928524A Withdrawn EP1177290A2 (de) | 1999-04-30 | 2000-04-28 | Rekombinantes laminin 5 |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP1177290A2 (de) |
| JP (1) | JP2002542824A (de) |
| AU (1) | AU4675300A (de) |
| WO (1) | WO2000066731A2 (de) |
Families Citing this family (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2002050111A2 (en) | 2000-12-21 | 2002-06-27 | Biostratum, Inc. | Isolated laminin 10 |
| WO2004108927A1 (ja) * | 2003-06-04 | 2004-12-16 | Yokohama Tlo Company, Ltd. | 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 |
| JP2008531125A (ja) * | 2005-02-23 | 2008-08-14 | サーモディクス，インコーポレイティド | ラミニンコーティングを有する移植可能な医療装置、及び使用方法 |
| FR2943062B1 (fr) * | 2009-03-13 | 2011-04-08 | Symatese | Nouveau peptide promoteur de l'adhesion et de la migration cellulaire |
| US11624053B2 (en) | 2013-11-27 | 2023-04-11 | Kyoto Prefectural Public University Corporation | Application of laminin to corneal endothelial cell culture |
| JP6925805B2 (ja) * | 2014-10-31 | 2021-08-25 | 京都府公立大学法人 | ラミニンによる角膜の新規治療 |
| JP6770435B2 (ja) | 2014-10-31 | 2020-10-14 | 京都府公立大学法人 | ラミニンによる網膜および神経の新規治療 |
| 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)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES8802441A1 (es) * | 1985-06-03 | 1988-06-16 | Meloy Lab | Procedimiento para preparar laminina humana |
| WO1994005316A1 (en) * | 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 | Products and methods for improving keratinocyte adhesion to the dermis |
| 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 |
| WO1997036621A1 (en) * | 1996-03-29 | 1997-10-09 | Desmos, Inc. | Cellular attachment to laminin 5-coated trans-epithelial appliances |
| AU3300297A (en) * | 1996-06-05 | 1998-01-07 | General Hospital Corporation, The | Laminin-5 and the formation of basement membrane structure |
| US5760179A (en) * | 1996-06-10 | 1998-06-02 | Desmos, Inc. | Purification of soluble laminin 5 |
| AU4220797A (en) * | 1996-09-13 | 1998-04-02 | Protegene Inc. | Human proteins having secretory signal sequences and DNAs encoding these prot eins |
-
2000
- 2000-04-28 AU AU46753/00A patent/AU4675300A/en not_active Abandoned
- 2000-04-28 JP JP2000615755A patent/JP2002542824A/ja active Pending
- 2000-04-28 WO PCT/US2000/011459 patent/WO2000066731A2/en not_active Application Discontinuation
- 2000-04-28 EP EP00928524A patent/EP1177290A2/de not_active Withdrawn
Non-Patent Citations (1)
| Title |
|---|
| See references of WO0066731A2 * |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2000066731A3 (en) | 2001-06-28 |
| WO2000066731A2 (en) | 2000-11-09 |
| JP2002542824A (ja) | 2002-12-17 |
| AU4675300A (en) | 2000-11-17 |
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