WO1998056810A2 - Proteine humaine lus-i, sa production et son utilisation - Google Patents
Proteine humaine lus-i, sa production et son utilisation Download PDFInfo
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- WO1998056810A2 WO1998056810A2 PCT/EP1998/003460 EP9803460W WO9856810A2 WO 1998056810 A2 WO1998056810 A2 WO 1998056810A2 EP 9803460 W EP9803460 W EP 9803460W WO 9856810 A2 WO9856810 A2 WO 9856810A2
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- Prior art date
Links
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- CAAULPUQFIIOTL-UHFFFAOYSA-N methyl dihydrogen phosphate Chemical class COP(O)(O)=O CAAULPUQFIIOTL-UHFFFAOYSA-N 0.000 description 1
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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
- C07K14/46—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
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4702—Regulators; Modulating activity
- C07K14/4703—Inhibitors; Suppressors
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2217/00—Genetically modified animals
- A01K2217/05—Animals comprising random inserted nucleic acids (transgenic)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Definitions
- This disulfide pattern was obtained by proteolytic cleavage with various endoproteases and sequencing of the fragments obtained.
- the corresponding fragments were sequenced by a combination of electrospray mass spectroscopy and Edman protein sequencing. Both human hemofiltrate and urine-derived LUS-I had identical chromatographic properties, molecular weights, and disulfide patterns.
- a further embodiment of the invention is represented by pharmaceutical compositions which contain the peptides according to the invention in a pharmaceutical dosage form.
- the preferred amount of the peptides according to the invention to be administered is between 1 ⁇ g and 1 g per dose unit when 1 to 5 doses of the drug are administered per day.
- nucleic acids which code for the peptides according to the invention can derive nucleic acids which code for the peptides according to the invention from the sequence of the peptides according to the invention using the genetic code. For expression in recombinant organisms, those codons are chosen which correspond to the codon usage of the transformed organism.
- Antisense nucleotides i.e. Nucleotides which bind to the nucleic acid sequences according to the invention under stringent conditions have, in particular, those sequences which can bind to parts of the mRNA in the target system.
- the person skilled in the art can determine the sequence of the mRNA from the peptide sequence using known methods.
- Antibodies that bind to the peptides according to the invention can be obtained in a simple manner by immunizing animals become.
- the peptides are optionally injected into the animals together with other auxiliary substances at intervals of several weeks, and then antibodies are isolated from the blood.
- Preferred animals for this are rabbits and mice.
- Known methods can be used to obtain immortal cells from the antibody-producing mouse cells, which allow the production of monoclonal antibodies.
- the transgenic mammals according to the invention with gene efficiency LUS-1 are obtained by methods known to the person skilled in the art. In general, the homologous recombination between DNA sequences is used. The vectors required for this can be constructed in a simple manner if the gene sequence is known. If the mRNA sequence is known, the gene can be found, for example, likewise by means of a polymerase chain reaction, and the amplified gene fragment can be elucidated by means of sequencing.
- the proteins, nucleic acids and antisense nucleotides, antibodies and inhibitors according to the invention are suitable for the production of diagnostic agents.
- the antibodies in particular enable the expression of the protein according to the invention to be determined in tissue or body fluids, for example by means of an immunoassay such as the known ELISA.
- an immunoassay such as the known ELISA.
- the nucleic acids according to the invention it can be analyzed - by means of amplification reactions such as polymerase chain reactions - whether there are gene diseases which can then be treated with the help of the medicaments according to the invention.
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
L'invention concerne une protéine présentant la séquence d'acides aminés de SEQ ID N° 1: NH2-Leu-Lys-Cys-Tyr-Thr- Cys-Lys-Glu-Pro-Met- Thr-Ser-Ala-Ser-Cys-Arg- Thr-Ile-Thr-Arg- Cys-Lys-Pro-Glu-Asp-Thr- Ala-Cys-Met-Thr-Thr-Leu- Val-Thr-Val-Glu-Ala-Glu- Tyr-Pro-Phe- Asn-Gln-Ser-Pro- Val-Val-Thr-Arg- Ser-Cys-Ser-Ser- Ser-Cys-Val-Ala-Thr- Asp-Pro-Asp-Ser- Ile-Gly-Ala-Ala- His-Leu-Ile-Phe- Cys-Cys-Phe-Arg- Asp-Leu-Cys-Asn- Ser-Glu-Leu-COOH (LUS-I). Elle concerne également ses dérivés cycliques, glycosylés, phosphorylés, acétylés, amidés et/ou contenant des liaisons de chaînes latérales, ainsi que des fragments présentant l'activité biologique de LUS-I.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU85366/98A AU8536698A (en) | 1997-06-09 | 1998-06-09 | Lus-1 human protein, its production and use |
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE19724301 | 1997-06-09 | ||
| DE19724301.0 | 1997-06-09 | ||
| DE1997149073 DE19749073C1 (de) | 1997-11-06 | 1997-11-06 | Humanes ANUP (humanes Anti-Neoplastisches-Urin-Peptid), seine Herstellung und Verwendung |
| DE19749073.5 | 1997-11-06 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| WO1998056810A2 true WO1998056810A2 (fr) | 1998-12-17 |
| WO1998056810A3 WO1998056810A3 (fr) | 1999-03-11 |
Family
ID=26037290
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/EP1998/003460 WO1998056810A2 (fr) | 1997-06-09 | 1998-06-09 | Proteine humaine lus-i, sa production et son utilisation |
Country Status (2)
| Country | Link |
|---|---|
| AU (1) | AU8536698A (fr) |
| WO (1) | WO1998056810A2 (fr) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004091646A3 (fr) * | 2003-04-16 | 2004-12-16 | Univ Lausanne | Compositions de slurp-1 et leurs methodes d'utilisation |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5298604A (en) * | 1992-07-27 | 1994-03-29 | Sloane Nathan H | Parital primary amino acid sequence of the antineoplastic protein (ANUP); a cytokine present in granulocytes |
| IT1257184B (it) * | 1992-12-22 | 1996-01-10 | Applied Research Systems | Preparato ad attivita' antinfiammatoria, anticoagulante e antitumorale |
-
1998
- 1998-06-09 AU AU85366/98A patent/AU8536698A/en not_active Abandoned
- 1998-06-09 WO PCT/EP1998/003460 patent/WO1998056810A2/fr active Application Filing
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004091646A3 (fr) * | 2003-04-16 | 2004-12-16 | Univ Lausanne | Compositions de slurp-1 et leurs methodes d'utilisation |
| JP2006523678A (ja) * | 2003-04-16 | 2006-10-19 | アプライド リサーチ システムズ エーアールエス ホールディング ナームロゼ フェンノートシャップ | Ｓｌｕｒｐ−１組成物及びその使用方法 |
| US7135454B2 (en) | 2003-04-16 | 2006-11-14 | Applied Research Systems Ars Holding N.V. | Use of SLURP-1 compositions for treating schizophrenia |
| AU2004229237B2 (en) * | 2003-04-16 | 2009-06-04 | Merck Serono Sa | Use of SLURP-1 for treating diseases related to acetylcholine receptors dysfunction |
| US7691808B2 (en) | 2003-04-16 | 2010-04-06 | Merck Serono Sa | Use of Slurp-1 for treating diseases related to acetylcholine receptor dysfunction |
| NO337494B1 (no) * | 2003-04-16 | 2016-04-25 | Merck Serono Sa | Sammensetninger som omfatter en effektiv mengde Slurp-1 for anvendelse i behandling av nevrologiske forstyrrelser og hudsykdommer |
Also Published As
| Publication number | Publication date |
|---|---|
| WO1998056810A3 (fr) | 1999-03-11 |
| AU8536698A (en) | 1998-12-30 |
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