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

The TSH receptor (TSHR) sheds its A subunit, particularly when cells are cultured in serum-poor medium. This shed A subunit is reported to be smaller than the cell-associated receptor because of the loss of glycan without change in its polypeptide core. Contrary to previous deductions, we now find that the 'small' shed A subunit has lost a glycan moiety because of the proteolytic clipping of a small C-terminal fragment containing an Asn-linked glycan. Moreover, this lost peptide fragment contains cysteine residues likely involved in A subunit linkage to the membrane-associated B subunit. Progressive lowering of the serum concentration in culture medium accentuates the process. Therefore, 'small' A subunit shedding does not appear related to a physiological mechanism involving disulfide bond reduction. On the other hand, we detected, for the first time, shedding of a lesser amount of normal-sized, in addition to small, A subunits, especially by cells cultured in standard serum concentrations.