Journal article
Inhibition of ras-induced oocyte maturation by peptides from ras-p21 and GTPase activating protein (GAP) identified as being effector domains from molecular dynamics calculations
Journal of protein chemistry, v 21(5), pp 361-366
Jul 2002
PMID: 12206510
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
In the accompanying article, using molecular dynamics calculations, we found that the 66-77 and 122-138 domains in ras-p21 and the 821-827, 832-845, 917-924, 943-953, and 1003-1020 domains in GAP have different conformations in complexes of GAP with wild-type and oncogenic ras-p21. We have now synthesized peptides corresponding to each of these domains and coinjected them into oocytes with oncogenic p21, which induces oocyte maturation, or injected them into oocytes incubated with insulin that induces maturation by activating wild-type cellular ras-p21. We find that all of these peptides inhibit both agents but do not inhibit progesterone-induced maturation that occurs by a ras-independent pathway. The p21 66-77 and 122-138 peptides cause greater inhibition of oncogenic p21. On the other hand, the GAP 832-845 and 1003-1021 peptides inhibit insulin-induced maturation to a significantly greater extent. Since we have found that activated wild-type and oncogenic p21 activate downstream targets like raf differently, these GAP peptides may be useful probes for identifying elements unique to the wild-type ras-p21 pathway.
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Details
- Title
- Inhibition of ras-induced oocyte maturation by peptides from ras-p21 and GTPase activating protein (GAP) identified as being effector domains from molecular dynamics calculations
- Creators
- Fred K Friedman - National Cancer InstituteLyndon Chie - Long Island UniversityDenise Chung - Long Island UniversityRichard Robinson - Laboratory of Metabolism, National Cancer Institute, BethesdaPaul Brandt-Rauf - Royal College of PhysiciansZiro Yamaizumi - National Cancer Institute, Tokyo, JapanMatthew R Pincus - Department of Pathology and Laboratory Medicine, New York Harbor VA Medical Center, Brooklyn
- Publication Details
- Journal of protein chemistry, v 21(5), pp 361-366
- Grant note
- CA 42500 / NCI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- School of Biomedical Engineering, Science, and Health Systems; Drexel University
- Web of Science ID
- WOS:000177629500006
- Scopus ID
- 2-s2.0-0036638239
- Other Identifier
- 991019323770504721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology