Regional specificity of ASP binding in human adipose tissue

Jumana Saleh, Nick Christou, Katherine Cianflone

Research output: Contribution to journalArticle

32 Citations (Scopus)

Abstract

Obesity, in particular omental (OM) adiposity, is associated with diabetes and cardiovascular disease. Thus site-specific regulation of fat storage is important to understand. Acylation-stimulating protein (ASP) is a potent stimulator of glucose transport and triglyceride synthesis in adipocytes. In the present study, we characterized receptor binding of 125I-labeled ASP to human adipocyte plasma membranes from paired OM and subcutaneous (SC) sites in normal (N) and obese (O) male (M) and female (F) subjects (n = 24). Overall, specific binding of 125I-ASP was in the order of SC > OM and O > N (in SC tissue, particularly in F). Receptor affinity of 125I-ASP was higher [lower dissociation constant (K(d))] in SC than in OM (63.6 ± 16.2 vs. 160.7 ± 38.6 nM, P <0.02), especially in F (37.0 ± 11.1 F-N and 26.3 ± 6.7 nM F-O) and lower (higher K(d)) in male OM (291.8 ± 116.8 M-N and 149.4 ± 56.4 M-O). The greater binding and higher affinity of 125I-ASP binding to SC suggests that ASP may be an important factor in maintaining regional adipose tissue mass. Conversely, lower binding and receptor affinity in male OM adipose tissue may contribute to the fatty acid imbalance and metabolic complications associated with this syndrome, by reducing the efficiency of adipose fatty acid trapping by the ASP pathway.

Original languageEnglish
JournalAmerican Journal of Physiology - Endocrinology and Metabolism
Volume276
Issue number5 39-5
Publication statusPublished - May 1999
Externally publishedYes

Keywords

  • Acylation-stimulating protein
  • Complement C3a
  • Receptor
  • Triglyceride synthesis

ASJC Scopus subject areas

  • Physiology
  • Endocrinology
  • Biochemistry
  • Physiology (medical)

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