A functional Tyr1306Cys variant in LARG is associated with increased insulin action in vivo

Diabetes. 2006 May;55(5):1497-503. doi: 10.2337/db05-1331.

Abstract

Diminished insulin sensitivity is a characteristic feature of type 2 diabetes. Inhibition of insulin action, resulting in reduced skeletal muscle glucose uptake, is mediated in part through stimulation of RhoA activity. One regulator of RhoA activity is leukemia-associated Rho guanine nucleotide exchange factor (LARG). The LARG gene maps to a region on chromosome 11q23-24 that shows genetic linkage to BMI and type 2 diabetes in Pima Indians. Because of its role in RhoA activation, the LARG gene was analyzed as a positional candidate gene for this linkage. Sequencing of the LARG gene and genotyping of variants identified several polymorphisms that were associated with in vivo rates of insulin-mediated glucose uptake, at both physiological and maximally stimulating insulin concentrations, among 322 nondiabetic Pima Indians who had undergone a hyperinsulinemic-euglycemic clamp. The strongest association with rate of glucose uptake was found with a Tyr1306Cys polymorphism (P < 0.0001, adjusted for age, sex, percent body fat, and nuclear family membership). In transient transfection studies in NIH3T3 cells, the LARG(Cys1306) protein had reduced activity compared with LARG(Tyr1306) protein (P < 0.05). We propose that the Tyr1306Cys substitution in LARG, through its differential activation of RhoA, increases insulin sensitivity in nondiabetic Pima Indians.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • 3T3 Cells
  • Amino Acid Substitution
  • Animals
  • Arizona
  • Chromosome Mapping
  • Chromosomes, Human, Pair 11*
  • Diabetes Mellitus, Type 2 / genetics*
  • Ethnicity
  • Genetic Variation*
  • Guanine Nucleotide Exchange Factors / genetics*
  • Humans
  • Indians, North American
  • Insulin / physiology*
  • Longitudinal Studies
  • Mice
  • Muscle, Skeletal / physiology
  • Polymorphism, Single Nucleotide*
  • Reference Values
  • Rho Guanine Nucleotide Exchange Factors
  • Transfection

Substances

  • ARHGEF12 protein, human
  • Guanine Nucleotide Exchange Factors
  • Insulin
  • Rho Guanine Nucleotide Exchange Factors