Journal
JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
Volume 85, Issue 11, Pages 3996-3999Publisher
ENDOCRINE SOC
DOI: 10.1210/jc.85.11.3996
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T(4)-binding globulin (TBG), the principal thyroid hormone-binding protein of serum, is a member of the serine protease inhibitor (serpin) superfamily. We report a characteristic serpin cleavage product of TBG in sepsis sera. At 49-50 kDa, the TBG remnant is 4-5 kDa smaller than the intact protein and is the same molecular mass as a TBG cleavage product produced by incubation with polymorphonuclear elastase. Incubation with polymorphonuclear leukocytes also produces the 49- to 50-kDa remnant, and this proteolysis is stimulated by zymosan activation. Polymorphonuclear cell cleavage of TBG increases the ratio of free/bound T(4). As previously described, in vitro cleavage of TBG by elastase also increases free/bound T(4). These findings are consistent with the hypothesis that serine proteases present at inflammatory sites cleave TBG, releasing its hormonal ligands.
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