Health & Environmental Research Online (HERO)


Print Feedback Export to File
9211051 
Journal Article 
Thyrotropin-induced plasma membrane protein modifications in porcine thyroid cells 
Giraud, A; Couraud, F; Lissitzky, S; , 
1977 
1 
Molecular and Cellular Endocrinology
ISSN: 0303-7207
EISSN: 1872-8057 
ELSEVIER IRELAND LTD 
CLARE 
297-312 
English 
885286 
WOS:A1977DM25200002 
Highly purified plasma membranes were obtained from isolated porcine thyroid cells maintained in conditions of culture in the presence of thyrotropin (stimulated cells) or in their absence (non-stimulated cells). Analyses of both types of membranes by high-resolution sodium dodecylsulfate-polyacrylamide slab gel electrophoresis showed reproducible quantitative differences in protein bands of apparent molecular weight 38,000, 36,000 and inconstantly 96,000. Phosphorylation of membranes by [gamma-32P]ATP was 2-3 times higher in membranes from thyrotropin-stimulated than in membranes from non-stimulated cells. About 20 32P-labeled bands were detected by slab gel electrophoresis in denaturing conditions, among which the catalytic subunit of Na+, K+ ATPase was characterized. In addition, plasma membranes from thyrotropin-stimulated cells contained a firmly bound [14C]glucosamine-containing glycoprotein probably related to an aggregation-promoting factor. 125I-labeled thyroglobulin and components of unknown nature were associated with plasma membranes from thyrotropin-stimulated cells. Whether they participate in the structure and function(s) of the plasma membrane or represent contaminants of the preparation is not clear at the present time.