Histochemical localization of heart-type fatty-acid binding protein in human and murine tissues

• Published in: Histochemistry and Cell Biology Vol. 103; no. 2; pp. 147 - 156
• Main Authors: Zschiesche, W, Kleine, A H, Spitzer, E, Veerkamp, J H, Glatz, J F
• Format: Journal Article
• Language: English
• Published: Germany 01-02-1995
• Subjects: Animals; Blotting, Western; Carrier Proteins - metabolism; Cattle; Fatty Acid Binding Protein 3; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Fatty Acids - metabolism; Female; Growth Inhibitors - metabolism; Humans; Immunohistochemistry; Male; Mice; Mice, Inbred BALB C; Muscle, Skeletal - metabolism; Muscle, Smooth - metabolism; Myocardium - cytology; Myocardium - metabolism; Neoplasm Proteins; Nerve Tissue Proteins; Peptides - metabolism; Recombinant Proteins - metabolism; Tumor Suppressor Proteins
• ISSN: 0948-6143; 0301-5564; 1432-119X
• DOI: 10.1007/BF01454012

Cellular fatty acid-binding proteins (FABP) are a highly conserved family of proteins consisting of several subtypes, among them the mammary-derived growth inhibitor (MDGI) which is quite homologous to or even identical with the heart-type FABP (H-FABP). The FABPs and MDGI have been suggested to be involved in intracellular fatty acid metabolism and trafficking. Recently, evidence for growth and differentiation regulating properties of MDGI and H-FABP was provided. Using four affinity-purified polyclonal antibodies against bovine and human antigen preparations, the cellular localization of MDGI/H-FABP in human and mouse tissues and organs was studied. The antibodies were weakly cross-reactive with adipose tissue extracts known to lack H-FABP, but failed to react by Western blot analysis with liver-type FABP (L-FABP) and intestinal-type FABP (I-FABP). MDGI/H-FABP protein was mainly detected in myocardium, skeletal and smooth muscle fibres, lipid and/or steroid synthesising cells (adrenals, Leydig cells, sebaceous glands, lactating mammary gland) and terminally differentiated epithelia of the respiratory, intestinal and urogenital tracts. The results provide evidence that expression of H-FABP is associated with an irreversibly postmitotic and terminally differentiated status of cells. Since all the antisera employed showed spatially identical and qualitatively equal immunostaining, it is suggested that human, bovine and mouse MDGI/H-FABP proteins share highly homologous epitopes.