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Title: Protein tyrosine phosphorylation during meiotic divisions of starfish oocytes

Abstract

We have used an antibody specific for phosphotyrosine to investigate protein phosphorylation on tyrosine during hormone-induced maturation of starfish oocytes. Analysis of immunoprecipitates from cortices of in vivo labeled Marthasterias glacialis oocytes revealed the presence of labeled phosphotyrosine-containing proteins only after hormone addition. Six major phosphoproteins of 195, 155, 100, 85, 45, and 35 kDa were detected. Total activity in immunoprecipitates increased until first polar body emission and was greatly reduced upon completion of meiosis but some proteins exhibited different kinetics. The labeling of the 155-kDa protein reached a maximum at germinal vesicle breakdown, while the 35-kDa appeared later and disappeared after polar body emission. Similar results were obtained with Asterias rubens oocytes. In vitro phosphorylation of cortices showed that tyrosine kinase activity is a major protein kinase activity in this fraction, the main endogenous substrate being a 68-kDa protein. The proteins phosphorylated on tyrosine in vitro were almost similar in extracts from oocytes treated or not with the hormone.

Authors:
; ;  [1]
  1. Univ. of Miami School of Medicine, FL (USA)
Publication Date:
OSTI Identifier:
7118079
Resource Type:
Journal Article
Journal Name:
Developmental Biology; (USA)
Additional Journal Information:
Journal Volume: 138:2; Journal ID: ISSN 0012-1606
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ANTIBODIES; SPECIFICITY; ECHINODERMS; OOGENESIS; PHOSPHOPROTEINS; PHOSPHORYLATION; PHOSPHOTRANSFERASES; ENZYME ACTIVITY; CELL DIVISION; MEMBRANE PROTEINS; MOLECULAR WEIGHT; OOCYTES; PHOSPHATES; PHOSPHORUS ISOTOPES; TRACER TECHNIQUES; TYROSINE; AMINO ACIDS; ANIMALS; AQUATIC ORGANISMS; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; ENZYMES; GAMETOGENESIS; GERM CELLS; HYDROXY ACIDS; INVERTEBRATES; ISOTOPE APPLICATIONS; ISOTOPES; ORGANIC ACIDS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PHOSPHORUS COMPOUNDS; PHOSPHORUS-GROUP TRANSFERASES; PROTEINS; TRANSFERASES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Peaucellier, G, Andersen, A C, and Kinsey, W H. Protein tyrosine phosphorylation during meiotic divisions of starfish oocytes. United States: N. p., 1990. Web. doi:10.1016/0012-1606(90)90205-W.
Peaucellier, G, Andersen, A C, & Kinsey, W H. Protein tyrosine phosphorylation during meiotic divisions of starfish oocytes. United States. https://doi.org/10.1016/0012-1606(90)90205-W
Peaucellier, G, Andersen, A C, and Kinsey, W H. 1990. "Protein tyrosine phosphorylation during meiotic divisions of starfish oocytes". United States. https://doi.org/10.1016/0012-1606(90)90205-W.
@article{osti_7118079,
title = {Protein tyrosine phosphorylation during meiotic divisions of starfish oocytes},
author = {Peaucellier, G and Andersen, A C and Kinsey, W H},
abstractNote = {We have used an antibody specific for phosphotyrosine to investigate protein phosphorylation on tyrosine during hormone-induced maturation of starfish oocytes. Analysis of immunoprecipitates from cortices of in vivo labeled Marthasterias glacialis oocytes revealed the presence of labeled phosphotyrosine-containing proteins only after hormone addition. Six major phosphoproteins of 195, 155, 100, 85, 45, and 35 kDa were detected. Total activity in immunoprecipitates increased until first polar body emission and was greatly reduced upon completion of meiosis but some proteins exhibited different kinetics. The labeling of the 155-kDa protein reached a maximum at germinal vesicle breakdown, while the 35-kDa appeared later and disappeared after polar body emission. Similar results were obtained with Asterias rubens oocytes. In vitro phosphorylation of cortices showed that tyrosine kinase activity is a major protein kinase activity in this fraction, the main endogenous substrate being a 68-kDa protein. The proteins phosphorylated on tyrosine in vitro were almost similar in extracts from oocytes treated or not with the hormone.},
doi = {10.1016/0012-1606(90)90205-W},
url = {https://www.osti.gov/biblio/7118079}, journal = {Developmental Biology; (USA)},
issn = {0012-1606},
number = ,
volume = 138:2,
place = {United States},
year = {Sun Apr 01 00:00:00 EST 1990},
month = {Sun Apr 01 00:00:00 EST 1990}
}