ERKs, extracellular signal-regulated MAP-2 kinases

doi:10.1016/0955-0674(91)90124-H

Current Opinion in Cell Biology

Volume 3, Issue 6, December 1991, Pages 1025-1032

https://doi.org/10.1016/0955-0674(91)90124-H Get rights and content

Abstract

A family of protein kinases, known alternatively as microtubule-associated protein-2/myelin basic protein kinases or extracellular signal-regulated kinases, is activated by numerous hormones, growth factors and other extracellular stimuli. At least two members of this family function as intermediate kinases in protein phosphorylation cascades. Their mechanisms of activation may involve autophosphorylation, which occurs on both threonine and tyrosine residues.

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The mechanism is unclear but might be due to an up-regulatory response of embryonic growth factor receptors to their increased ligand levels in the abnormal medium containing PF. An important finding in our study was that the level of p-ERK, which is required to activate MAPKs in the EGFR and IGF-IR signal transduction pathways (20, 21, 42–44), was statistically significantly lower in embryos exposed to medium containing PF. The results suggest that although EGF, IGF-I, and their receptors increased in embryos, the postreceptor signal pathways might be impaired by PF.
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Peritoneal fluid was obtained from fertile women with no endometriosis (PF-NE) and infertile women with mild endometriosis (PF-E). In vitro fertilization was performed, and mouse two-cell stage embryos were cultured in human tubal fluid medium with or without PF.
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When oocytes and embryos were cultured in media with PF-E, the fertilization capability of oocytes and the development potential of embryos were decreased. The levels of embryonic EGF, IGF-I, and their receptors were increased. However, p-ERK of the postreceptor signal transduction pathway was down-regulated.
Endometriotic PF may attenuate oocyte and embryo development by impairing embryonic growth factor/receptor/signal transduction, resulting in endometriotic infertility.

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ERKs, extracellular signal-regulated MAP-2 kinases

Abstract

J Biol Chem

J Biol Chem

J Biol Chem

J Biol Chem

J Biol Chem

Cell

Science

J Biol Chem

Mol Cell Biol

J Biol Chem

J Biol Chem

Nature

J Biol Chem

J Immunol

J Biol Chem

Nature

Cell Regulation

EMBO J

Nucleic Acids Res

Biochim Biophys Acta

Insulin-Treated 3T3-L1 Adipocytes and Cell-Free Extracts Derived from Them Incorporate 32p into Ribosomal Protein S6

Growth Factor Receptor Tyrosine Kinases

Annu Rev Biochem

Tyrosine Phosphorylation and Tyrosine Kinase Activity of the trk Proto-Oncogene Product Induced by NGF

Nature

trkB En codes a Functional Receptor for Brain-Derived Neurotrophic Factor and Neurotrophin-3 but Not Nerve Growth Factor

Cell

A Xenopus Ribosomal Protein S6 Kinase has Two Apparent Kinase Domains that Each are Similar to Distinct Protein Kinases

Insulin-Stimulated MAP2 Kinase Phosphorylates and Activates Ribosomal Protein S6 Kinase II

Nature

Coordinate Regulation of pp90rsk and a Distinct Protein-Serine/Threonine Kinase Activity that Phosphorylates Recombinant pp90rsk In Vitro

Mol Cell Biol

Mitogen-Activated Swiss Mouse 3T3 RSK Kinases I and II are Related to pp44mpk from Sea Star Oocytes and Participate in the Regulation of pp90rsk Activity

Rapid Stimulation by Insulin of a Serine/Threonine Kinase in 3T3-L1 Adipocytes that Phosphorylates Microtubule-Associated Protein 2 In Vitro

Coordinate Regulation of pp90^rsk and a Distinct Protein-Serine/Threonine Kinase Activity that Phosphorylates Recombinant pp90^rsk In Vitro

Mitogen-Activated Swiss Mouse 3T3 RSK Kinases I and II are Related to pp44^mpk from Sea Star Oocytes and Participate in the Regulation of pp90^rsk Activity