Biomaterial Database

The helical domain of intestinal fatty acid binding protein is critical for collisional transfer of fatty acids to phospholipid membranes. 1998

B Corsico, and D P Cistola, and C Frieden, and J Storch

Department of Nutritional Sciences, Rutgers University, New Brunswick, NJ 08901-8525, USA.

Fatty acid binding proteins (FABPs) exhibit a beta-barrel topology, comprising 10 antiparallel beta-sheets capped by two short alpha-helical segments. Previous studies suggested that fatty acid transfer from several FABPs occurs during interaction between the protein and the acceptor membrane, and that the helical domain of the FABPs plays an important role in this process. In this study, we employed a helix-less variant of intestinal FABP (IFABP-HL) and examined the rate and mechanism of transfer of fluorescent anthroyloxy fatty acids (AOFA) from this protein to model membranes in comparison to the wild type (wIFABP). In marked contrast to wIFABP, IFABP-HL does not show significant modification of the AOFA transfer rate as a function of either the concentration or the composition of the acceptor membranes. These results suggest that the transfer of fatty acids from IFABP-HL occurs by an aqueous diffusion-mediated process, i.e., in the absence of the helical domain, effective collisional transfer of fatty acids to membranes does not occur. Binding of wIFABP and IFABP-HL to membranes was directly analyzed by using a cytochrome c competition assay, and it was shown that IFABP-HL was 80% less efficient in preventing cytochrome c from binding to membranes than the native IFABP. Collectively, these results indicate that the alpha-helical region of IFABP is involved in membrane interactions and thus plays a critical role in the collisional mechanism of fatty acid transfer from IFABP to phospholipid membranes.

UI	MeSH Term	Description	Entries
D007413	Intestinal Mucosa	Lining of the INTESTINES, consisting of an inner EPITHELIUM, a middle LAMINA PROPRIA, and an outer MUSCULARIS MUCOSAE. In the SMALL INTESTINE, the mucosa is characterized by a series of folds and abundance of absorptive cells (ENTEROCYTES) with MICROVILLI.	Intestinal Epithelium,Intestinal Glands,Epithelium, Intestinal,Gland, Intestinal,Glands, Intestinal,Intestinal Gland,Mucosa, Intestinal
D009363	Neoplasm Proteins	Proteins whose abnormal expression (gain or loss) are associated with the development, growth, or progression of NEOPLASMS. Some neoplasm proteins are tumor antigens (ANTIGENS, NEOPLASM), i.e. they induce an immune reaction to their tumor. Many neoplasm proteins have been characterized and are used as tumor markers (BIOMARKERS, TUMOR) when they are detectable in cells and body fluids as monitors for the presence or growth of tumors. Abnormal expression of ONCOGENE PROTEINS is involved in neoplastic transformation, whereas the loss of expression of TUMOR SUPPRESSOR PROTEINS is involved with the loss of growth control and progression of the neoplasm.	Proteins, Neoplasm
D009419	Nerve Tissue Proteins		Proteins, Nerve Tissue,Tissue Proteins, Nerve
D010743	Phospholipids	Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.	Phosphatides,Phospholipid
D011994	Recombinant Proteins	Proteins prepared by recombinant DNA technology.	Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002352	Carrier Proteins	Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes.	Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D000071438	Fatty Acid-Binding Protein 7	A fatty acid-binding protein expressed by ASTROCYTES during CENTRAL NERVOUS SYSTEM development, and by MALIGNANT GLIOMA cells. It is also expressed by ASTROCYTES in response to injury or ISCHEMIA, and may function in repair of the MYELIN SHEATH.	Brain Lipid-Binding Protein,Fatty Acid-Binding Protein, Brain,Mammary-Derived Growth Inhibitor Related Protein,Brain Lipid Binding Protein,Fatty Acid Binding Protein 7,Fatty Acid Binding Protein, Brain,Lipid-Binding Protein, Brain,Mammary Derived Growth Inhibitor Related Protein
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D050556	Fatty Acid-Binding Proteins	Intracellular proteins that reversibly bind hydrophobic ligands including: saturated and unsaturated FATTY ACIDS; EICOSANOIDS; and RETINOIDS. They are considered a highly conserved and ubiquitously expressed family of proteins that may play a role in the metabolism of LIPIDS.	Fatty Acid-Binding Protein,Adipocyte Lipid Binding Protein,Adipocyte-Specific Fatty Acid-Binding Protein,Brain-Type Fatty Acid-Binding Protein,Cytosolic Lipid-Binding Proteins,Fatty Acid-Binding Protein, Cardiac Myocyte,Fatty Acid-Binding Protein, Myocardial,Fatty Acid-Binding Proteins, Adipocyte-Specific,Fatty Acid-Binding Proteins, Brain-Specific,Fatty Acid-Binding Proteins, Cytosolic-Specific,Fatty Acid-Binding Proteins, Intestinal-Specific,Fatty Acid-Binding Proteins, Liver-Specific,Fatty Acid-Binding Proteins, Myocardial-Specific,Fatty Acid-Binding Proteins, Plasma-Membrane Specific,Intestinal Fatty Acid-Binding Protein,Liver Fatty Acid-Binding Protein,Myocardial Fatty Acid-Binding Protein,Plasma Membrane Fatty Acid-Binding Protein,Acid-Binding Protein, Fatty,Adipocyte Specific Fatty Acid Binding Protein,Brain Type Fatty Acid Binding Protein,Cytosolic Lipid Binding Proteins,Fatty Acid Binding Protein,Fatty Acid Binding Protein, Cardiac Myocyte,Fatty Acid Binding Protein, Myocardial,Fatty Acid Binding Proteins,Fatty Acid Binding Proteins, Adipocyte Specific,Fatty Acid Binding Proteins, Brain Specific,Fatty Acid Binding Proteins, Cytosolic Specific,Fatty Acid Binding Proteins, Intestinal Specific,Fatty Acid Binding Proteins, Liver Specific,Fatty Acid Binding Proteins, Myocardial Specific,Fatty Acid Binding Proteins, Plasma Membrane Specific,Intestinal Fatty Acid Binding Protein,Lipid-Binding Proteins, Cytosolic,Liver Fatty Acid Binding Protein,Myocardial Fatty Acid Binding Protein,Plasma Membrane Fatty Acid Binding Protein,Protein, Fatty Acid-Binding