The shed thyrotropin receptor is primarily a carboxyl terminal truncated form of the A subunit, not the entire A subunit
Author:
Publisher
Elsevier BV
Subject
Endocrinology,Molecular Biology,Biochemistry
Reference14 articles.
1. Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells;Chazenbalk;Endocrinology,1996
2. Evidence that the thyrotropin receptor ectodomain contains not one, but two, cleavage sites;Chazenbalk;Endocrinology,1996
3. Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain;Couet;Biochemistry,1996
4. Shedding of human thyrotropin receptor ectodomain: involvement of a matrix metalloprotease;Couet;J. Biol. Chem.,1996
5. An N-linked glycosylation motif from the non-cleaving luteinizing hormone receptor substituted for the homologous region (Gly-367 to Glu-369) of the thyrotropin receptor prevents cleavage at its second, downstream site;Kakinuma;J. Biol. Chem.,1997
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