Binding of sulfosuccinimidyl fatty acids to adipocyte membrane proteins: Isolation and ammo-terminal sequence of an 88-kD protein implicated in transport of long-chain fatty acids

Caroll M. Harmon, Nada A. Abumrad

Research output: Contribution to journalArticle

154 Scopus citations

Abstract

We recently reported (Harmon et al., J. Membrane Biol.124:261-268, 1991) that sulfo-N-succinimidyl derivatives of long-chain fatty acids (SS-FA) specifically inhibited transport of oleate by rat adipocytes. These compounds bound to an 85-90 kD membrane protein which was also labeled by another inhibitor of FA transport [3H]DIDS (4,4′-diisothiocyanostilbene-2-2′-sulfonate). These results indicated that the protein was a strong candidate as the transporter for long-chain fatty acids. In this report we determined that the apparent size of the protein is 88 kD and its isoelectric point is 6.9. We used [3H]SS-oleate (SSO), which specifically labels the 88-kD protein, to isolate it from rat adipocyte plasma membranes. Identification of 15 amino acids at the N-terminus region revealed strong sequence homology with two previously described membrane glycoproteins: CD36, a ubiquitous protein originally identified in platelets and PAS IV, a protein that is enriched in the apical membranes of lipidsecreting mammary cells during lactation. Antibody against PAS IV cross-reacted with the adipocyte protein. This, together with the N-terminal sequence homology, suggested that the adipocyte protein belongs to a family of related intrinsic membrane proteins which include CD36 and PAS IV.

Original languageEnglish
Pages (from-to)43-49
Number of pages7
JournalThe Journal of Membrane Biology
Volume133
Issue number1
DOIs
StatePublished - Apr 1 1993
Externally publishedYes

Keywords

  • Sulfosuccinimidyl fatty acid
  • adipocyte
  • fatty acids
  • plasma membrane
  • proteins
  • transport

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