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Major secretory protein of human decidualized endometrium in pregnancy is an insulin-like growth factor-binding protein

Major secretory protein of human decidualized endometrium in pregnancy is an insulin-like growth... ABSTRACTPregnancy-associated endometrial α1-globulin (α1-PEG) is quantitatively the major secretory protein product, synthesized and secreted in vitro, of the human decidualized endometrium during pregnancy. This protein has been purified from cytosolic extracts of this tissue and has now been characterized as a 32 kDa somatomedin/insulin-like growth factor (IGF)-binding protein. Immunoreactive α1-PEG isolated from amniotic fluid exhibited identical physiochemical properties and IGF-I-binding characteristics. In cytosolic extracts of pregnancy endometrium, in incubation medium of this tissue and in amniotic fluid, the 32 kDa protein represented the major α1-PEG immunoreactive protein and major IGF-I-binding component. Purified α1-PEG and incubation medium of pregnancy endometrium competed for IGF-I with placental membrane IGF receptors in vitro. The implications of the endometrial source of IGF-I-binding protein are dicussed with reference to the origin of the amniotic fluid and serum small Mr IGF-binding protein and to the suggested paracrine effect upon trophoblast proliferation.J. Endocr. (1988) 118, 317–328 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Endocrinology Bioscientifica

Major secretory protein of human decidualized endometrium in pregnancy is an insulin-like growth factor-binding protein

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Publisher
Bioscientifica
Copyright
Copyright © 1988 The Authors. All Rights Reserved.
ISSN
0022-0795
eISSN
1479-6805
DOI
10.1677/joe.0.1180317
Publisher site
See Article on Publisher Site

Abstract

ABSTRACTPregnancy-associated endometrial α1-globulin (α1-PEG) is quantitatively the major secretory protein product, synthesized and secreted in vitro, of the human decidualized endometrium during pregnancy. This protein has been purified from cytosolic extracts of this tissue and has now been characterized as a 32 kDa somatomedin/insulin-like growth factor (IGF)-binding protein. Immunoreactive α1-PEG isolated from amniotic fluid exhibited identical physiochemical properties and IGF-I-binding characteristics. In cytosolic extracts of pregnancy endometrium, in incubation medium of this tissue and in amniotic fluid, the 32 kDa protein represented the major α1-PEG immunoreactive protein and major IGF-I-binding component. Purified α1-PEG and incubation medium of pregnancy endometrium competed for IGF-I with placental membrane IGF receptors in vitro. The implications of the endometrial source of IGF-I-binding protein are dicussed with reference to the origin of the amniotic fluid and serum small Mr IGF-binding protein and to the suggested paracrine effect upon trophoblast proliferation.J. Endocr. (1988) 118, 317–328

Journal

Journal of Endocrinology – Bioscientifica

Published: Aug 1, 1988

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