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Title: Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium

Abstract

Insulin-stimulated sodium transport in the toad urinary bladder consists of two components, a brief element of rapid onset that is independent of protein synthesis, and a sustained increase, slower in onset, that is dependent upon RNA and protein synthesis. The mucosal epithelium of the toad bladder was labeled by lactoperoxidase-catalyzed radioiodination (125I) following 15 min and 3 h exposure to insulin. The membrane of ''mitochondria-rich'' and ''granular'' mucosal cells from these tissues were analyzed by electrophoresis in SDS-urea. Compared to untreated tissues, membranes of ''granular'' mucosal cells from tissues exposed to insulin for 15 min contained a band (Mr . 15,000) with significantly increased labeling. Bladders exposed to insulin for 3 h showed no consistent increase in labeling. These data suggest that there are differences in the conformation of apical membrane proteins during the two phases of hormone-induced sodium transport. The technique may also offer an opportunity to identify ''effector'' proteins mediating this and other insulin responses.

Authors:
; ; ;
Publication Date:
Research Org.:
Department of Physiology, Mount Sinai School of Medicine, New York
OSTI Identifier:
5551293
Resource Type:
Journal Article
Journal Name:
Endocrinology; (United States)
Additional Journal Information:
Journal Volume: 109:5
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BLADDER; PHYSIOLOGY; INSULIN; BIOLOGICAL EFFECTS; IODINE 125; TRACER TECHNIQUES; SODIUM; MEMBRANE TRANSPORT; BIOCHEMICAL REACTION KINETICS; BIOSYNTHESIS; EPITHELIUM; PEROXIDASES; RNA; TOADS; ALKALI METALS; AMPHIBIANS; ANIMAL TISSUES; ANIMALS; AQUATIC ORGANISMS; BETA DECAY RADIOISOTOPES; BODY; CARBOXYLIC ACIDS; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; ELEMENTS; ENZYMES; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; HORMONES; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; METALS; NUCLEI; NUCLEIC ACIDS; ODD-EVEN NUCLEI; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; ORGANS; OXIDOREDUCTASES; PEPTIDE HORMONES; PORPHYRINS; RADIOISOTOPES; REACTION KINETICS; SYNTHESIS; TISSUES; URINARY TRACT; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques; 551001 - Physiological Systems- Tracer Techniques

Citation Formats

Scott, W N, Slatin, S L, Cobb, M H, and Reich, I M. Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium. United States: N. p., 1981. Web. doi:10.1210/endo-109-5-1775.
Scott, W N, Slatin, S L, Cobb, M H, & Reich, I M. Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium. United States. https://doi.org/10.1210/endo-109-5-1775
Scott, W N, Slatin, S L, Cobb, M H, and Reich, I M. 1981. "Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium". United States. https://doi.org/10.1210/endo-109-5-1775.
@article{osti_5551293,
title = {Insulin-induced alterations in the lactoperoxidase-catalyzed radioiodination of membrane proteins of the toad bladder epithelium},
author = {Scott, W N and Slatin, S L and Cobb, M H and Reich, I M},
abstractNote = {Insulin-stimulated sodium transport in the toad urinary bladder consists of two components, a brief element of rapid onset that is independent of protein synthesis, and a sustained increase, slower in onset, that is dependent upon RNA and protein synthesis. The mucosal epithelium of the toad bladder was labeled by lactoperoxidase-catalyzed radioiodination (125I) following 15 min and 3 h exposure to insulin. The membrane of ''mitochondria-rich'' and ''granular'' mucosal cells from these tissues were analyzed by electrophoresis in SDS-urea. Compared to untreated tissues, membranes of ''granular'' mucosal cells from tissues exposed to insulin for 15 min contained a band (Mr . 15,000) with significantly increased labeling. Bladders exposed to insulin for 3 h showed no consistent increase in labeling. These data suggest that there are differences in the conformation of apical membrane proteins during the two phases of hormone-induced sodium transport. The technique may also offer an opportunity to identify ''effector'' proteins mediating this and other insulin responses.},
doi = {10.1210/endo-109-5-1775},
url = {https://www.osti.gov/biblio/5551293}, journal = {Endocrinology; (United States)},
number = ,
volume = 109:5,
place = {United States},
year = {Sun Nov 01 00:00:00 EST 1981},
month = {Sun Nov 01 00:00:00 EST 1981}
}