The rat heart contains an abundant cytosolic protein which binds long chain fatty acids. We have determined its primary structure by Edman degradation of peptides generated from chymotryptic, tryptic, and elastase digestions. This polypeptide (M(r) = 14,992) contains 134 amino acids and has a blocked (acetylated) NH2 terminus. The sequence of rat heart fatty acid-binding protein (FABP) is remarkably similar to the murine adipocyte 422 protein and the P2 protein of peripheral nerve myelin. Computer-assisted alignment of heart FABP and 422 revealed that 82 of 132 comparable residues are identical (62%). There are 77 identities out of 131 possible matches between this protein and the human myelin P2 protein (59%). Similar comparisons demonstrate that heart FABP has significant homology to several other proteins which bind hydrophobic ligands. The rank of order of similarity to heart FABP is: 422 > myelin P2 > cellular retinoic acid-binding protein > cellular retinol-binding protein II > cellular retinol-binding protein > intestinal FABP > liver FABP. These eight sequences form a family of paralogous homologues. Heart FABP has a region of internal homology involving tandemly arrayed oligopeptides spanning residues 71-100 and 101-131. This feature is not found in the 422 and P2 sequences. The endogenous ligands bound by the 422, P2, and heart FABP sequences have not been defined. Interpretation of the biological significance of their structural similarities and differences will require information about their ligand specificities and affinities.
|Number of pages||6|
|Journal||Journal of Biological Chemistry|
|State||Published - 1986|