Molecular cloning of two types of GAP complementary DNA from human placenta
- PMID: 3201259
- DOI: 10.1126/science.3201259
Molecular cloning of two types of GAP complementary DNA from human placenta
Abstract
The ras p21 GTPase-activating protein (GAP) was purified from human placental tissue. Internal amino acid sequence was obtained from this 120,000-dalton protein and, by means of this sequence, two types of complementary DNA clones were isolated and characterized. One type encoded GAP with a predicted molecular mass of 116,000 daltons and 96% identity with bovine GAP. The messenger RNA of this GAP was detected in human lung, brain, liver, leukocytes, and placenta. The second type appeared to be generated by a differential splicing mechanism and encoded a novel form of GAP with a predicted molecular mass of 100,400 daltons. This protein lacks the hydrophobic amino terminus characteristic of the larger species, but retains GAP activity. The messenger RNA of this type was abundantly expressed in placenta and in several human cell lines, but not in adult tissues.
Similar articles
-
Molecular cloning of a cDNA coding for neurofibromatosis type 1 protein isoform lacking the domain related to ras GTPase-activating protein.Biochem Biophys Res Commun. 1992 Sep 16;187(2):984-90. doi: 10.1016/0006-291x(92)91294-z. Biochem Biophys Res Commun. 1992. PMID: 1339276
-
Chromosome localization and cDNA sequence of murine and human genes for ras p21 GTPase activating protein (GAP).Somat Cell Mol Genet. 1989 Nov;15(6):579-90. doi: 10.1007/BF01534919. Somat Cell Mol Genet. 1989. PMID: 2574500
-
Expression of the placenta-specific, 100 kDa ras GTPase activating protein in several human cancer cell lines and normal human tissues.Mol Cell Biochem. 1997 Oct;175(1-2):195-204. doi: 10.1023/a:1006871516961. Mol Cell Biochem. 1997. PMID: 9350052
-
Purification, characterization, and western blot analysis of human GTPase-activating protein from native and recombinant sources.J Biol Chem. 1990 Dec 15;265(35):21922-8. J Biol Chem. 1990. PMID: 2123878
-
Characterization of the C. elegans gap-2 gene encoding a novel Ras-GTPase activating protein and its possible role in larval development.Genes Cells. 1998 Mar;3(3):189-202. doi: 10.1046/j.1365-2443.1998.00179.x. Genes Cells. 1998. PMID: 9619631
Cited by
-
Two species of human CRK cDNA encode proteins with distinct biological activities.Mol Cell Biol. 1992 Aug;12(8):3482-9. doi: 10.1128/mcb.12.8.3482-3489.1992. Mol Cell Biol. 1992. PMID: 1630456 Free PMC article.
-
Mutants of H-ras that interfere with RAS effector function in Saccharomyces cerevisiae.EMBO J. 1989 Oct;8(10):3039-44. doi: 10.1002/j.1460-2075.1989.tb08454.x. EMBO J. 1989. PMID: 2684634 Free PMC article.
-
Coxsackievirus B3 replication is reduced by inhibition of the extracellular signal-regulated kinase (ERK) signaling pathway.J Virol. 2002 Apr;76(7):3365-73. doi: 10.1128/jvi.76.7.3365-3373.2002. J Virol. 2002. PMID: 11884562 Free PMC article.
-
β3 integrin-EGF receptor cross-talk activates p190RhoGAP in mouse mammary gland epithelial cells.Mol Biol Cell. 2011 Nov;22(22):4288-301. doi: 10.1091/mbc.E10-08-0700. Epub 2011 Sep 21. Mol Biol Cell. 2011. PMID: 21937717 Free PMC article.
-
Differential antagonism of Ras biological activity by catalytic and Src homology domains of Ras GTPase activation protein.Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4887-91. doi: 10.1073/pnas.90.11.4887. Proc Natl Acad Sci U S A. 1993. PMID: 8506332 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous