Isolation and characterization of two fatty acid binding proteins from mouse brain

Sean C. Myers-Payne, Timothy Hubbell, Lixia Pu, Frank Schnütgen, Torsten Börchers, W. Gibson Wood, Friedrich Spener, Friedhelm Schroeder

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

Two fatty acid binding proteins (FABPs) were isolated from Swiss Webster mouse brains. Neither protein cross-reacted with antisera to recombinant liver L-FABP. One protein, designated brain H-FABP, migrated on tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as a single band at 14.5 kDa with pl 4.9. Brain H-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.02 and 0.5 μM, respectively. Brain H-FABP cross-reacted with affinity-purified antisera to recombinant heart H-FABP. The second protein, mouse brain B-FABP, migrated on tricine SDS-PAGE gels as a doublet at 16.0 and 15.5 kDa with pI values of 4.5 and 4.7, respectively. Brain B-FABP bound NBD-stearic acid and cis-parinaric acid with K(D) values near 0.01 and 0.7 μM, respectively. The brain B-FABP doublet was immunoreactive with affinity-purified antibodies against recombinant mouse brain B-FABP, but not with affinity-purified antibodies against heart H-FABP. [3H]Oleate competition binding indicated that the two brain FABPs had distinct ligand binding specificities. Both bound fatty acids, fatty acyl CoA, and lysophosphatidic acid. Although both preferentially bound unsaturated fatty acids, twofold differences in specific saturated fatty acid binding were observed. Brain B-FABP and brain H-FABP represented 0.1 and 0.01% of brain total cytosolic protein, respectively. In summary, mouse brain contains two native fatty acid binding proteins, brain H-FABP and brain B-FABP.

Original languageEnglish (US)
Pages (from-to)1648-1656
Number of pages9
JournalJournal of Neurochemistry
Volume66
Issue number4
DOIs
StatePublished - Apr 1996

Keywords

  • Brain
  • Fatty acid
  • Fatty acid binding protein
  • Mouse

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