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Related Experiment Videos

Thyroxine-binding globulin cleavage in cord blood.

Navaid S Khan1, George C Schussler, Joshua B Holden

  • 1Department of Pediatrics, Division of Endocrinology, State University of New York, 450 Clarkson Avenue, Brooklyn, NY 11203, USA.

The Journal of Clinical Endocrinology and Metabolism
|July 11, 2002
PubMed
Summary

Thyroxine-binding globulin (TBG) cleavage by polymorphonuclear elastase occurs physiologically in newborns. This process, linked to the neonatal TSH surge, may increase thyroxine (T4) delivery to tissues during critical developmental changes.

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Area of Science:

  • Endocrinology
  • Biochemistry
  • Neonatal Physiology

Background:

  • Thyroxine-binding globulin (TBG) is a serpin that binds and transports thyroxine (T4).
  • Cleavage of TBG by polymorphonuclear elastase releases T4.
  • This cleavage has been observed during sepsis and with inflammatory stimuli.

Purpose of the Study:

  • To investigate TBG cleavage in normal neonatal cord blood.
  • To determine if TBG cleavage is part of a physiological neonatal inflammatory response.

Main Methods:

  • Analysis of neonatal cord blood samples.
  • Detection of TBG cleavage products.

Main Results:

  • TBG cleavage was demonstrated in the cord blood of normal newborns.

Related Experiment Videos

  • This cleavage appears to be a physiological inflammatory response in neonates.
  • Neonatal TBG cleavage correlates with the neonatal TSH surge.

    • Conclusions:

    • Neonatal TBG cleavage is a physiological event, not solely pathological.
    • This process likely enhances T4 delivery to neonatal tissues.
    • Increased T4 flux may support T4-sensitive developmental changes in newborns.