Leptin: From laboratory to clinic

José F. Caro, Robert V. Considine

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

Abstract

Figure 1 Stucture of leptin and defective leptin proteins. The gene for leptin in both humans and rodents encodes a 167amino acid protein with an amino terminal secretory signal sequence of21 amino acids (4). The signal sequence is cleaved during protein processing and leptin circulates in the blood as a 16 kDa protein. In C57BL/61 ob/ob mice a T to C substitution in the first position of codon 105 changes an arginine to a premature stop codon. Two families with mutations in the LEP gene have been identified. In family No.1, a guanine nucleotide in codon 133 is deleted, which results in a frameshift and the synthesis of a truncated leptin protein (91). In the second family a C to T substitution in the first base of codon 105 changes arginine to tryptophan (92). The mutant leptin protein in the ob/ob mouse and in both families is not secreted but is degraded in the adipocyte.

Original languageEnglish (US)
Title of host publicationHandbook of Obesity
Subtitle of host publicationClinical Applications
PublisherCRC Press
Pages275-295
Number of pages21
ISBN (Electronic)9780824758622
ISBN (Print)0824747739, 9780824747732
StatePublished - Jan 1 2003

ASJC Scopus subject areas

  • Medicine(all)

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    Caro, J. F., & Considine, R. V. (2003). Leptin: From laboratory to clinic. In Handbook of Obesity: Clinical Applications (pp. 275-295). CRC Press.