Mutation in the calcium-binding domain of the mitochondrial glycerophosphate dehydrogenase gene in a family of diabetic subjects

Biochem Biophys Res Commun. 1997 Feb 24;231(3):570-2. doi: 10.1006/bbrc.1997.6147.

Abstract

The Ca(2+)-sensitive and mitochondrial enzyme FAD-linked glycerophosphate dehydrogenase (m-GDH) represents an essential component of the pancreatic B-cell glucose-sensing device. This report deals with the first identified case of mutation in the calcium-binding domain of the m-GDH gene in a patient with type-2 diabetes and his glucose-intolerant half sister. Single strand conformation polymorphism analysis indeed revealed an abnormal mobility of the 32P-labelled polymerase chain reaction product in these two subjects. The corresponding base pair mutations and amino acid changes were documented. In the diabetic proband, the relative extent of the Ca(2+)-induced activation of m-GDH in CD3+ T-lymphocytes was lower than in his brother with a normal m-GDH gene sequence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Binding Sites
  • Calcium / metabolism*
  • Diabetes Mellitus, Type 2 / genetics*
  • Female
  • Glucose Intolerance
  • Glycerolphosphate Dehydrogenase / genetics*
  • Humans
  • Male
  • Middle Aged
  • Mitochondria / enzymology*
  • Molecular Sequence Data
  • Point Mutation
  • Polymorphism, Single-Stranded Conformational

Substances

  • Glycerolphosphate Dehydrogenase
  • Calcium

Associated data

  • GENBANK/U12424
  • SWISSPROT/P43304