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WO1998020125A1 - Proteines secretees et polynucleotides qui les codent - Google Patents

Proteines secretees et polynucleotides qui les codent Download PDF

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Publication number
WO1998020125A1
WO1998020125A1 PCT/US1997/014649 US9714649W WO9820125A1 WO 1998020125 A1 WO1998020125 A1 WO 1998020125A1 US 9714649 W US9714649 W US 9714649W WO 9820125 A1 WO9820125 A1 WO 9820125A1
Authority
WO
WIPO (PCT)
Prior art keywords
protein
polynucleotide
amino acid
composition
seq
Prior art date
Application number
PCT/US1997/014649
Other languages
English (en)
Inventor
Kenneth Jacobs
John M. Mccoy
Edward R. Lavallie
Lisa A. Racie
David Merberg
Maurice Treacy
Vikki Spaulding
Original Assignee
Genetics Institute, 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 Genetics Institute, Inc. filed Critical Genetics Institute, Inc.
Priority to EP97938459A priority Critical patent/EP0950102A1/fr
Priority to AU40776/97A priority patent/AU4077697A/en
Priority to CA002275535A priority patent/CA2275535A1/fr
Publication of WO1998020125A1 publication Critical patent/WO1998020125A1/fr

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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

Definitions

  • the present invention provides novel polynucleotides and proteins encoded by such polynucleotides, along with therapeutic, diagnostic and research utilities for these polynucleotides and proteins.
  • the invention also encompasses allelic variants of the disclosed polynucleotides or proteins; that is, naturally-occurring alternative forms of the isolated polynucleotide which also encode proteins which are identical, homologous or related to that encoded by the polynucleotides.
  • RP- HPLC reverse-phase high performance liquid chromatography
  • hydrophobic RP-HPLC media e.g., silica gel having pendant methyl or other aliphatic groups
  • Some or all of the foregoing purification steps, in various combinations, can also be employed to provide a substantially homogeneous isolated recombinant protein.
  • the protein thus purified is substantially free of other mammalian proteins and is defined in accordance with the present invention as an "isolated protein.”
  • the proteins provided herein also include proteins characterized by amino acid sequences similar to those of purified proteins but into which modification are naturally provided or deliberately engineered.
  • modifications in the peptide or DNA sequences can be made by those skilled in the art using known techniques.
  • Modifications of interest in the protein sequences may include the alteration, substitution, replacement, insertion or deletion of a selected amino acid residue in the coding sequence.
  • one or more of the cysteine residues may be deleted or replaced with another amino acid to alter the conformation of the molecule.
  • Techniques for such alteration, substitution, replacement, insertion or deletion are well known to those skilled in the art (see, e.g., U.S. Patent No.
  • the polynucleotide encodes a protein which binds or potentially binds to another protein (such as, for example, in a receptor-ligand interaction)
  • the polynucleotide can also be used in interaction trap assays (such as, for example, that described in Gyuris et al., Cell 75:791-803 (1993)) to identify polynucleotides encoding the other protein with which binding occurs or to identify inhibitors of the binding interaction.
  • Assays for proliferation and differentiation of hematopoietic and lymphopoietic cells include, without limitation, those described in: Measurement of Human and Murine Interleukin
  • a protein of the present invention may also exhibit immune stimulating or immune suppressing activity, including without limitation the activities for which assays are described herein.
  • a protein may be useful in the treatment of various immune deficiencies and disorders (including severe combined immunodeficiency (SOD)), e.g., in regulating (up or down) growth and proliferation of T and/or B lymphocytes, as well as effecting the cytolytic activity of NK cells and other cell populations.
  • SOD severe combined immunodeficiency
  • These immune deficiencies may be genetic or be caused by viral (e.g., HIV) as well as bacterial or fungal infections, or may result from autoimmune disorders.
  • Examples of appropriate systems which can be used include allogeneic cardiac grafts in rats and xenogeneic pancreatic islet cell grafts in mice, both of which have been used to examine the immunosuppressive effects of CTLA4Ig fusion proteins in vivo as described in Lenschow et al, Science 257:789-792 (1992) and Turka et al, Proc. Natl. Acad. Sci USA, 89: 1 1 102- 11105 (1992).
  • murine models of GVHD see Paul ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 846-847) can be used to determine the effect of blocking B lymphocyte antigen function in vivo on the development of that disease.
  • the efficacy of blocking reagents in preventing or alleviating autoimmune disorders can be determined using a number of well- characterized animal models of human autoimmune diseases. Examples include murine experimental autoimmune encephalitis, systemic lupus erythmatosis in MRL/lpr/lpr mice or NZB hybrid mice, murine autoimmune collagen arthritis, diabetes mellitus in NOD mice and BB rats, and murine experimental myasthenia gravis (see Paul ed., Fundamental Immunology, Raven Press, New York, 1989, pp. 840-856).
  • tumor cells obtained from a patient can be transfected ex vivo with an expression vector directing the expression of a peptide having B7-2-like activity alone, or in conjunction with a peptide having B7-l-like activity and/or B7-3-like activity.
  • the transfected tumor cells are returned to the patient to result in expression of the peptides on the surface of the transfected cell.
  • gene therapy techniques can be used to target a tumor cell for transfection in vivo.
  • lymphocyte survival/apoptosis (which will identify, among others, proteins that prevent apoptosis after superantigen induction and proteins that regulate lymphocyte homeostasis) include, without limitation, those described in: Darzynkiewicz et al., Cytometry 13:795-808, 1992; Gorczyca et al., Leukemia 7:659-670, 1993; Gorczyca et al., Cancer Research 53: 1945-1951, 1993; Itoh et al., Cell 66:233-243, 1991 ; Zacharchuk, Journal .of Immunology 145:4037-4045, 1990; Zamai et al., Cytometry 14:891-897, 1993; Gorczyca et al., International Journal of Oncology 1 :639-648, 1992.
  • Assays for embryonic stem cell differentiation include, without limitation, those described in : Johansson et al. Cellular Biology 15:141-151 , 1995 ; Keller et al. , Molecular and Cellular Biology 13:473-486, 1993; McClanahan et al., Blood 81 :2903-2915, 1993.
  • a protein of the present invention may have chemotactic or chemokinetic activity (e.g., act as a chemokine) for mammalian cells, including, for example, monocytes, fibroblasts, neutrophils, T-cells, mast cells, eosinophils, epithelial and/or endothelial cells.
  • Chemotactic and chemokinetic proteins can be used to mobilize or attract a desired cell population to a desired site of action.
  • Chemotactic or chemokinetic proteins provide particular advantages in treatment of wounds and other trauma to tissues, as well as in treatment of localized infections. For example, attraction of lymphocytes, monocytes or neutrophils to tumors or sites of infection may result in improved immune responses against the tumor or infecting agent.
  • protein of the present invention When a therapeutically effective amount of protein of the present invention is administered orally, protein of the present invention will be in the form of a tablet, capsule, powder, solution or elixir.
  • the pharmaceutical composition of the invention may additionally contain a solid carrier such as a gelatin or an adjuvant.
  • the tablet, capsule, and powder contain from about 5 to 95% protein of the present invention, and preferably from about 25 to 90% protein of the present invention.
  • a liquid carrier such as water, petroleum, oils of animal or plant origin such as peanut oil, mineral oil, soybean oil, or sesame oil, or synthetic oils may be added.
  • MOLECULE TYPE cDNA
  • SEQUENCE DESCRIPTION SEQ ID NO : 1 :

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  • 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)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

L'invention concerne de nouveaux polynucléotides et les protéines qu'ils codent.
PCT/US1997/014649 1996-11-06 1997-08-20 Proteines secretees et polynucleotides qui les codent WO1998020125A1 (fr)

Priority Applications (3)

Application Number Priority Date Filing Date Title
EP97938459A EP0950102A1 (fr) 1996-11-06 1997-08-20 Proteines secretees et polynucleotides qui les codent
AU40776/97A AU4077697A (en) 1996-11-06 1997-08-20 Secreted proteins and polynucleotides encoding them
CA002275535A CA2275535A1 (fr) 1996-11-06 1997-08-20 Proteines secretees et polynucleotides qui les codent

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US74369096A 1996-11-06 1996-11-06
US08/743,690 1996-11-06

Publications (1)

Publication Number Publication Date
WO1998020125A1 true WO1998020125A1 (fr) 1998-05-14

Family

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Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/US1997/014649 WO1998020125A1 (fr) 1996-11-06 1997-08-20 Proteines secretees et polynucleotides qui les codent

Country Status (4)

Country Link
EP (1) EP0950102A1 (fr)
AU (1) AU4077697A (fr)
CA (1) CA2275535A1 (fr)
WO (1) WO1998020125A1 (fr)

Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990005780A1 (fr) * 1988-11-18 1990-05-31 State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education, Acting For And On Behalf Of The Oregon Health Sciences University Recepteurs de dopamine et genes
WO1990014432A1 (fr) * 1989-05-23 1990-11-29 Genetics Institute, Inc. Une cytokine humaine, l'interleukine 9
EP0510691A1 (fr) * 1991-04-26 1992-10-28 Osaka Bioscience Institute ADN codant un antigène de surface cellulaire humaine
WO1994007916A1 (fr) * 1992-10-07 1994-04-14 Merck & Co., Inc. Recepteur d'hormone steroide humain neri
WO1996017925A1 (fr) * 1994-12-06 1996-06-13 Immunex Corporation Cytokine designee par lerk-7
US5536637A (en) * 1993-04-07 1996-07-16 Genetics Institute, Inc. Method of screening for cDNA encoding novel secreted mammalian proteins in yeast
WO1997007198A2 (fr) * 1995-08-11 1997-02-27 Genetics Institute, Inc. Sequences d'adn et proteines secretees codees par celles-ci
WO1997025427A1 (fr) * 1996-01-12 1997-07-17 Genetics Institute, Inc. Beta-chemokine, h1305 (mpc-2)

Patent Citations (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990005780A1 (fr) * 1988-11-18 1990-05-31 State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education, Acting For And On Behalf Of The Oregon Health Sciences University Recepteurs de dopamine et genes
WO1990014432A1 (fr) * 1989-05-23 1990-11-29 Genetics Institute, Inc. Une cytokine humaine, l'interleukine 9
EP0510691A1 (fr) * 1991-04-26 1992-10-28 Osaka Bioscience Institute ADN codant un antigène de surface cellulaire humaine
WO1994007916A1 (fr) * 1992-10-07 1994-04-14 Merck & Co., Inc. Recepteur d'hormone steroide humain neri
US5536637A (en) * 1993-04-07 1996-07-16 Genetics Institute, Inc. Method of screening for cDNA encoding novel secreted mammalian proteins in yeast
WO1996017925A1 (fr) * 1994-12-06 1996-06-13 Immunex Corporation Cytokine designee par lerk-7
WO1997007198A2 (fr) * 1995-08-11 1997-02-27 Genetics Institute, Inc. Sequences d'adn et proteines secretees codees par celles-ci
WO1997025427A1 (fr) * 1996-01-12 1997-07-17 Genetics Institute, Inc. Beta-chemokine, h1305 (mpc-2)

Non-Patent Citations (6)

* Cited by examiner, † Cited by third party
Title
ADAMS M D ET AL: "3,400 NEW EXPRESSED SEQUENCE TAGS IDENTIFY DIVERSITY OF TRANSCRIPTS IN HUMAN BRAIN", NATURE GENETICS, vol. 4, no. 3, pages 256 - 267, XP000611495 *
JACOBS K ET AL: "A novel method for isolating eukaryotic cDNA clones encoding secreted proteins.", KEYSTONE SYMPOSIUM ON DENDRITIC CELLS: ANTIGEN PRESENTING CELLS OF T AND B LYMPHOCYTES, TAOS, NEW MEXICO, USA, MARCH 10-16, 1995. JOURNAL OF CELLULAR BIOCHEMISTRY SUPPLEMENT 0 (21A). 1995. 19. ISSN: 0733-1959, XP002027246 *
L. HILLIER ET AL.: "y178e09.r1 Homo sapiens cDNA clone 44074 5'", EMBL SEQUENCE DATABASE, 23 June 1995 (1995-06-23), HEIDELBERG, BRD, XP002049827 *
R.J. KAUFMAN ET AL.: "Effect of von Willebrand factor coexpression on the synthesis and secretion of factor VIII in chinese hamster ovary cells", MOL. CELL. BIOL., vol. 9, no. 3, March 1989 (1989-03-01), ASM WASHINGTON, DC,US, pages 1233 - 1242, XP002041592 *
R.J. KAUFMAN ET AL.: "Improved vectors for stable expression of foreign genes in mammalian cells by use of the untranslated leader sequence from EMC virus", NUCLEIC ACIDS RESEARCH, vol. 19, no. 16, 1991, IRL PRESS LIMITED,OXFORD,ENGLAND, pages 4485 - 4490, XP002041594 *
R.J. KAUFMAN ET AL.: "The phosphorylation state of eucaryotic initiation factor 2 alters translation efficiency of specific mRNAs", MOL. CELL. BIOL., vol. 9, no. 3, March 1989 (1989-03-01), ASM WASHINGTON, DC,US, pages 946 - 958, XP002041593 *

Also Published As

Publication number Publication date
AU4077697A (en) 1998-05-29
CA2275535A1 (fr) 1998-05-14
EP0950102A1 (fr) 1999-10-20

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