Abstract

CORRELATION APPROACHES OF FATTY ACID BINDING PROTEINS AND MYOCARDIAL INFARCTION

*Prof. Dr. Badmanaban Ramalingam, Dr. Bharat Mishra, Prof. Dr. Dhrubo Jyoti Sen, Manu Jose and Fels Saju

Abstract

Fatty acid-binding proteins (FABPs) are small cytoplasmic proteins that are abundantly expressed in tissues with an active fatty acid metabolism, such as the heart and liver, with their primary function being the facilitation of intracellular long-chain fatty acid transport. Nine distinct types of the FABP family have been identified, with Heart-type FABP (H-FABP) being the most widely studied, largely due to the fact that it is found in abundance in the cardiomyocytes. The combination of their low molecular weight and cytoplasmic location means that H-FABP proteins are released very rapidly following Acute Myocardial Infarction (AMI). Fatty acid-binding proteins (FABPs) are members of the intracellular lipid-binding protein (iLBP) family and are involved in reversibly binding intracellular hydrophobic ligands and trafficking them throughout cellular compartments, including the peroxisomes, mitochondria, endoplasmic reticulum and nucleus. FABPs are small, structurally conserved cytosolic proteins consisting of a water-filled, interior-binding pocket surrounded by ten anti parallel β sheets, forming a β barrel. At the superior surface, two α-helices cap the pocket and are thought to regulate binding. FABPs have broad specificity, including the ability to bind long-chain (C16-C20) fatty acids, eicosanoids, bile salts and peroxisome proliferators. FABPs demonstrate strong evolutionary conservation and are present in a spectrum of species including Drosophila melanogaster, Caenorhabditis elegans, mouse and human. The human genome consists of nine putatively functional protein-coding FABP genes. The most recently identified family member, FABP12, has been less studied.

Keywords: FABP, AMI, myocardial infarction, intracellular lipid-binding proteins, uptake and trafficking of lipids, metabolic diseases, human genome.