The shed thyrotropin receptor is primarily a carboxyl terminal truncated form of the A subunit, not the entire A subunit

Molecular and Cellular Endocrinology

Volumn 150, Issue 1-2, 1999, Pages 113-119

  Tanaka, Kunihiko ^a   Chazenbalk, Gregorio D ^a   McLachlan, Sandra M ^a   Rapoport, Basil ^a  

^a CEDARS SINAI MEDICAL CENTER   (United States)

Author keywords

Proteolysis; Shedding; TSH receptor

Indexed keywords

CYSTEINE; POLYPEPTIDE; THYROTROPIN RECEPTOR;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DISULFIDE BOND; GENE OVEREXPRESSION; MOLECULAR INTERACTION; NONHUMAN; OVARY CELL; PRIORITY JOURNAL;

AMINO ACID SEQUENCE; ANIMALS; CHO CELLS; CRICETINAE; CULTURE MEDIA, SERUM-FREE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECEPTORS, THYROTROPIN; SIGNAL TRANSDUCTION;

EID: 0033602665     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(99)00018-0     Document Type: Article

References (14)

1. Chazenbalk G.D., Kakinuma A., Jaume J.C., McLachlan S.M., Rapoport B. Evidence for negative cooperativity among human thyrotropin receptors overexpressed in mammalian cells. Endocrinology. 137:1996;4586-4591.
2. Chazenbalk G.D., Tanaka K., Nagayama Y., Kakinuma A., Jaume J.C., McLachlan S.M., Rapoport B. Evidence that the thyrotropin receptor ectodomain contains not one, but two, cleavage sites. Endocrinology. 138:1996;2893-2899.
3. Couet J., de Bernard S., Loosfelt H., Saunier B., Milgrom E., Misrahi M. Cell surface protein disulfide-isomerase is involved in the shedding of human thyrotropin receptor ectodomain. Biochemistry. 35:1996;14800-14805.
4. Couet J., Sokhavut S., Jolivet A., Vu Hai M.-T., Milgrom E., Misrahi M. Shedding of human thyrotropin receptor ectodomain: involvement of a matrix metalloprotease. J. Biol. Chem. 271:1996;4545-4552.
5. Kakinuma A., Chazenbalk G.D., Tanaka K., Nagayama Y., McLachlan S.M., Rapoport B. 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. J. Biol. Chem. 272:1997;28296-28300.
6. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
7. Misrahi M., Ghinea N., Sar S., Saunier B., Jolivet A., Loosfelt H., Cerutti M., Devauchelle G., Milgrom E. Processing of the precursors of the human thyroid-stimulating hormone receptor in various eukaryotic cells (human thyrocytes, transfected L cells and baculovirus-infected insect cells). Eur. J. Biochem. 222:1994;711-719.
8. Misrahi M., Milgrom E. Cleavage and shedding of the TSH receptor. Eur. J. Endocrinol. 137:1997;599-602.
9. Nicholson L.B., Vlase H., Graves P., Nilsson M., Molne J., Huang G.C., Morgenthaler N.G., Davies T.F., McGregor A.M., Banga J.P. Monoclonal antibodies to the human thyrotropin receptor: epitope mapping and binding to the native receptor on the basolateral plasma membrane of thyroid follicular cells. J. Mol. Endocrinol. 16:1996;159-170.
10. Rapoport B., Chazenbalk G.D., Jaume J.C., McLachlan S.M. The thyrotropin (TSH) receptor: Interaction with TSH and autoantibodies. Endocr. Rev. 19:1998;673-716.
11. Rees Smith B., McLachlan S.M., Furmaniak J. Autoantibodies to the thyrotropin receptor. Endocr. Rev. 9:1988;106-121.
12. Russo D., Chazenbalk G.D., Nagayama Y., Wadsworth H.L., Seto P., Rapport B.A. New structural model for the thyrotropin (TSH) receptor as determined by covalent crosslinking of TSH to the recombinant receptor in intact cells: evidence for a single polypeptide chain. Mol. Endocrinol. 5:1991;1607-1612.
13. Seglen P.O., Bohley P. Autophagy and other vacuolar protein degradation mechanisms. Experientia. 48:1992;158-172.
14. Tanaka K., Chazenbalk G.D., McLachlan S.M., Rapoport B. Thyrotropin receptor cleavage at site 1 does not involve a specific amino acid motif but instead depends on the presence of the unique, 50 amino acid insertion. J. Biol. Chem. 273:1998;1959-1963.