Fatty Acid-Binding Protein 4 (FABP4) is a cytoplasm protein that belongs to the fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small; highly conserved; cytoplasmic proteins that bind long-chain fatty acids. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells. FABP4 is thought to participate in Lipid transport protein in adipocytes. FABP4 binds to the long chain fatty acids and retinoic acid; delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. FABP4 modulates inflammatory responses and cholesterol ester accumulation. FABP4 is a plasma marker of metabolic disturbances in HIV-infected patients; and therefore; could serve to guide therapeutic intervention in this group of patients.
Fatty acid-binding protein; also known as Epidermal-type fatty acid-binding protein; Fatty acid-binding protein 5; Psoriasis-associated fatty acid-binding protein homolog; E-FABP and FABP5; is a cytoplasm protein which Belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid-binding proteins ( FABPs ) are postulated to serve as lipid shuttles that solubilize hydrophobic fatty acids and deliver them to appropriate intracellular sites. E-FABP / FABP5 is predominantly expressed in keratinocytes and is overexpressed in the actively proliferating tissue characteristic of psoriasis and wound healing. E-FABP / FABP5 exhibits an important role in binding free fatty acids; as well as regulating lipid metabolism and transport. E-FABP / FABP5 has high specificity for fatty acids. It has highest affinity for C18 chain length. Decreasing the chain length or introducing double bonds reduces the affinity of FABP5. E-FABP / FABP5 may be involved in keratinocyte differentiation.
Fatty acid-binding protein 5 (FABP5) is a cytoplasm protein that belongs to the fatty-acid binding protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small; highly conserved; cytoplasmic proteins that bind long-chain fatty acids. FABP5 can be expressed in keratinocytes; and is highly expressed in psoriatic skin. FABP5 has been shown to be involved in keratinocyte differentiation. FABP5 has high specificity for fatty acids; the highest affinity for C18 chain length. FABP5 can decrease the chain length or introduce double bonds to reduce the affinity.
Gastrotropin, also known as Fatty acid-binding protein 6, Ileal lipid-binding protein, ILBP, Intestinal 15 kDa protein, Intestinal bile acid-binding protein, I-BABP and FABP6, is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Isoform2 of FABP6 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform1of FABP6 is expressed in the jejunum, ileum, cecum and ascending colon intestine. Isoform2is expressed in the gallbladder, duodenum, jejunum, ileum, cecum, ascending, transverse and descending colon, sigmoid colon and rectum. FABP6 / I-BABP is a cancer-related protein that acts as an intracellular transporter of bile acid in the ileal epithelium. FABP6 / I-BABP may also play an important role in early carcinogenesis.
Fatty Acid-Binding Protein 6 (FABP6) is cytoplasmic protein that binds long-chain fatty acids and other hydrophobic ligands which belongs to the calycin superfamily. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. FABP6 forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. It seems to be able to bind to bile salts and bilirubins.
Complement factor D; also known as adipsin; is a member of the chymotrypsin family of serine proteases; which plays an essential role in host defense as the rate-limiting enzyme in the alternative pathway of complement activation. Complement factor D activates a convertase (C3bBb) responsible for cleavage of the complement protein C3; which leads to the activation of terminal complement component C5-9 to form the membrane attack complex on microbial or cellular surfaces. It also functions in the regulation of systemic energy balance and physiologic and pathologic processes; including immunity and inflammation.
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