Placental membrane fatty acid-binding protein preferentially binds arachidonic and docosahexaenoic acids

Life Sci. 1998;63(4):235-40. doi: 10.1016/s0024-3205(98)00267-7.

Abstract

To elucidate further the role of placental membrane fatty acid-binding protein (p-FABPpm) in preferential transfer of maternal plasma long chain polyunsaturated fatty acids (LCPUFA) across the human placenta, direct binding of the purified protein with various radiolabelled fatty acids (docosahexaenoic, arachidonic, linoleic and oleic acids) was investigated. Binding of these fatty acids to the protein revealed that p-FABPpm had higher affinities and binding capacities for arachidonic and docosahexaenoic acids compared with linoleic and oleic acids. The apparent binding capacities (Bmax) values for oleic, linoleic, arachidonic and docosahexaenoic acids were 2.0 +/- 0.14, 2.1 +/- 0.17, 3.5 +/- 0.11, 4.0 +/- 0.10 mol per mol of p-FABPpm whereas the apparent dissociation constant (Kd) values were 1.0 +/- .0.07, 0.73 +/- 0.04, 0.45 +/- 0.03 and 0.4 +/- 0.02 microM, respectively (n=3). In the case of human serum albumin, the Kd and Bmax values for all fatty acids were around 1 microM and 5 mol/mol of protein, respectively. These data provide direct evidence for the role of p-FABPpm in preferential sequestration of maternal arachidonic and docosahexaenoic acids by the placenta for transport to the fetus by virtue of its preferential binding of these fatty acids.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arachidonic Acids / metabolism*
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism
  • Docosahexaenoic Acids / metabolism*
  • Fatty Acid-Binding Protein 7
  • Fatty Acid-Binding Proteins
  • Female
  • Humans
  • Myelin P2 Protein / metabolism*
  • Neoplasm Proteins*
  • Placenta / metabolism*
  • Pregnancy
  • Protein Binding
  • Tumor Suppressor Proteins*

Substances

  • Arachidonic Acids
  • Carrier Proteins
  • FABP7 protein, human
  • Fatty Acid-Binding Protein 7
  • Fatty Acid-Binding Proteins
  • Myelin P2 Protein
  • Neoplasm Proteins
  • Tumor Suppressor Proteins
  • Docosahexaenoic Acids