Claims
- 1. An isolated polynucleotide selected from the group consisting of:a) a polynucleotide which encodes a polypeptide comprising the uninterrupted sequence SEQ ID NO: 2, and b) the complementary strand of a polynucleotide as defined in a).
- 2. The polynucleotide of claim 1, comprising nucleotides 37-564 of SEQ ID NO: 1 or the complementary strand of nucleotides 37-564 of SEQ ID NO: 1.
- 3. The polynucleotide of claim 1 comprising the sequence SEQ ID NO: 1 or the complementary strand of SEQ ID NO:1.
- 4. An antisense polynucleotide comprising a polynucleotide of claim 1, part b, wherein said antisense polynucleotide inhibits the expression of Grb2 and Grb3-3.
- 5. An antisense polynucleotide comprising all or part of the polynucleotide of claim 1, part b, wherein said antisense polynucleotide specifically inhibits the expression of Grb3-3.
- 6. A vector comprising a polynucleotide according to claim 1.
- 7. A vector according to claim 6, wherein said vector is a viral vector.
- 8. A vector according to claim 7, selected from the group consisting of adenoviruses, retroviruses, adeno-associated viruses, herpes virus, cytomegalovirus and vaccinia virus.
- 9. A vector according to claim 8, wherein the virus is defective for replication.
- 10. A composition comprising a vector according to claim 6 in a pharmaceutically acceptable carrier.
- 11. A composition comprising a polynucleotide according to claim 1 complexed with DEAE-dextran, nuclear proteins or lipids, or incorporated into liposomes.
- 12. An isolated polypeptide having the sequence SEQ ID NO: 2.
- 13. A composition comprising a polypeptide according to claim 12 in a pharmaceutically acceptable carrier.
- 14. An antisense polynucleotide according to claim 5, and comprisingwherein the polynucleotide comprises the complementary strand of the sequence joining the N-terminal SH3 domain and the residual SH2 domain of Grb3-3.
- 15. An antisense RNA comprising a sequence complementary to all or part of a polynucleotide of claim 1, part a, wherein said antisense RNA specifically inhibits the expression of Grb3-3.
- 16. An antisense RNA according to claim 15, and comprising the sequence joining the N-terminal SH3 domain and the residual SH2 domain of Grb3-3.
- 17. An antisense RNA comprising a polynucleotide of claim 1, part b, wherein said antisense RNA inhibits the expression of Grb2 and Grb3-3.
- 18. A process for expressing Grb3-3 in a host cell, comprising introducing the vector according to claim 6 into the host cell.
- 19. A process for expressing Grb3-3 in a host cell, comprising introducing the vector according to claim 7 into the host cell.
- 20. A process for expressing Grb3-3 in a host cell, comprising introducing the vector according to claim 8 into the host cell.
- 21. A process for expressing Grb3-3 in a host cell, comprising introducing the vector according to claim 9 into the host cell.
- 22. The process according to claim 18, wherein the host cell is a prokaryotic cell.
- 23. The process according to claim 22, wherein the prokaryotic cell is E. coli.
- 24. The process according to claim 18, wherein the host cell is a eukaryotic cell.
- 25. A process for preparing a Grb3-3 polypeptide, comprising transforming a host cell with a vector according to claim 6, culturing the host cell under conditions permitting expression of the Grb3-3 polypeptide, and recovering the Grb3-3 polypeptide.
- 26. A process for preparing a Grb3-3 polypeptide, comprising transforming a host cell with a vector according to claim 7, culturing the host cell under conditions permitting expression of the Grb3-3 polypeptide, and recovering the Grb3-3 polypeptide.
- 27. A process for preparing a Grb3-3 polypeptide, comprising transforming a host cell with a vector according to claim 8, culturing the host cell under conditions permitting expression of the Grb3-3 polypeptide, and recovering the Grb3-3 polypeptide.
- 28. A process for preparing a Grb3-3 polypeptide, comprising transforming a host cell with a vector according to claim 9, culturing the host cell under conditions permitting expression of the Grb3-3 polypeptide, and recovering the Grb3-3 polypeptide.
- 29. The process according to claim 25, wherein the host cell is a prokaryotic cell.
- 30. The process according to claim 29, wherein the prokaryotic cell is E. coli.
- 31. An antisense RNA according to claim 15, wherein the polynucleotide comprises the complementary strand of the sequence joining the N-terminal SH3 domain and the residual SH2 domain of Grb3-3.
Priority Claims (1)
Number |
Date |
Country |
Kind |
93 10971 |
Sep 1993 |
FR |
|
Parent Case Info
This application is a reissue application of U.S. application Ser. No. 08/612,857, filed Mar. 13, 1996, which is a §371 national stage filing of PCT/FR94/00542, filed May 9, 1994.
Government Interests
This application is a reissue application of U.S. application Ser. No. 08/612,857, filed Mar. 13, 1996, which is a §371 national stage filing of PCT/FR94/00542, filed May 9, 1994.
PCT Information
Filing Document |
Filing Date |
Country |
Kind |
PCT/FR94/00542 |
|
WO |
00 |
Publishing Document |
Publishing Date |
Country |
Kind |
WO95/07981 |
3/23/1995 |
WO |
A |
US Referenced Citations (1)
Number |
Name |
Date |
Kind |
5434064 |
Schlessinger et al. |
Jul 1995 |
A |
Foreign Referenced Citations (1)
Number |
Date |
Country |
WO 9407913 |
Apr 1994 |
WO |
Non-Patent Literature Citations (5)
Entry |
Lowenstein et al., “The SH2 and SH3 Domain-containing Protein GRB2 Links Receptor Tyrosine Kinases to Ras Signaling,” Cell., vol. 70, pp. 431-442 (1992). |
Matuoka et al., “Cloning of ASH, a Ubiquitous Protein Composed of One Src Homology Region (SH) 2 and Two SH3 Domains, From Human and Rat cDNA Libraries,” Proc. Nat'l. Acad. Sci., USA, vol. 89, pp. 9015-9019 (1992). |
Rey et al., “A Role for Grb2 in Apoptosis?” Cell Death and Diff., vol. 2, pp. 105-111 (1995). |
Suen et al., “Molecular Cloning of the Mouse Grb2 Gene: Differential Interaction of the Grb2 Adaptor Protein with Epidermal Growth Factor and Nerve Growth Factor Receptors,” Mol. Cell. Biol., vol. 13, pp. 5500-5512 (1993). |
Watanabe et al., “Splicing Isoforms of Rat Ash/Grb2. Isolation and Characterization of the cDNA and genomic DNA Clones and Implications for the Physiological Roles of the Isoforms,” J. Biol. Chem., vol. 270, pp. 13733-13739 (1995). |
Divisions (1)
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Number |
Date |
Country |
Parent |
08/612857 |
Mar 1996 |
US |
Child |
09/641640 |
|
US |
Reissues (1)
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Number |
Date |
Country |
Parent |
08/612857 |
Mar 1996 |
US |
Child |
09/641640 |
|
US |