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Thyroxine-Binding Globulin Cleavage in Cord Blood

Departments of Pediatrics (N.S.K.), Internal Medicine (G.C.S.), and Obstetrics and Gynecology (J.B.H.), Division of Endocrinology, State University of New York, Brooklyn, New York 11203; Immunochemistry Laboratory (A.F.), Health Science Center at Brooklyn, Brooklyn, New York 11203; and Division of Endocrinology, Department of Pediatrics (N.S.K.), Maimonides Hospital, Brooklyn, New York 11219

Address all correspondence and requests for reprints to: Dr. George C. Schussler, Box 57, 450 Clarkson Avenue, Brooklyn, New York 11203. E-mail: . george.c.schussler-new-york{at}worldnet.att.net

Abstract

Thyroxine-binding globulin, a member of the serine protease inhibitor superfamily of proteins (serpins), releases T₄ on cleavage by polymorphonuclear elastase. Such cleavage, previously shown to occur during sepsis and with an exogenous inflammatory stimulus, is now demonstrated in the cord blood of normal babies and appears to be part of a physiological inflammatory response in the newborn. In association with the neonatal TSH surge, thyroxine-binding globulin cleavage is likely to contribute to an increased flux of T₄ to neonatal tissues at a time when T₄-sensitive morphogenic and biochemical changes are occurring.

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