Unlocking the Potential of FABP6 as a Drug Target and Biomarker

Target Name: FABP6

NCBI ID: G2172

Unlocking the Potential of FABP6 as a Drug Target and Biomarker

Fatty acid binding protein 6 (FABP6) is a protein that plays a crucial role in various cellular processes, including the regulation of lipid metabolism and the transport of fatty acids across cell membranes. FABP6 has been identified as a potential drug target and biomarker due to its unique structure, function, and involvement in several diseases. In this article, we will explore the current state of research on FABP6 and its potential as a drug target and biomarker.

Structure and Function

FABP6 is a 21-kDa protein that belongs to the superfamily of FABP (Fatty Acid Binding) proteins. These proteins are characterized by a conserved catalytic core and a N-terminal region that is involved in protein-protein interactions and may serve as a scaffold. FABP6 is expressed in various tissues and cells, including liver, muscle, heart, and brain, and has been implicated in various physiological processes, including energy metabolism, inflammation, and cell signaling.

One of the most significant functions of FABP6 is its role in the transport of fatty acids across cell membranes. FABP6 is a high-affinity protein for fatty acids, with a KDa of approximately 20 nM, which allows it to transport fatty acids across the inner mitochondrial membrane and the outer mitochondrial membrane, where they can be used for energy production. This function is critical for maintaining cellular energy homeostasis and has been implicated in the pathogenesis of various diseases, including obesity, type 2 diabetes, and cardiovascular disease.

In addition to its role in fatty acid transport, FABP6 has also been shown to play a key role in the regulation of lipid metabolism and inflammation. FABP6 has been shown to regulate the levels of fatty acids in adipose tissue and to modulate the expression of genes involved in lipid metabolism. Additionally, FABP6 has been shown to play a role in the regulation of inflammation and has been implicated in the pathogenesis of various inflammatory diseases, including cardiovascular disease and autoimmune disorders.

Potential Therapeutic Applications

The potential therapeutic applications of FABP6 are vast and span several therapeutic areas, including obesity, type 2 diabetes, cardiovascular disease, and neurodegenerative diseases.

In the context of obesity, FABP6 has been shown to be involved in the regulation of lipid metabolism and to play a role in the development of obesity-related diseases. Several studies have shown that individuals with higher FABP6 levels are more likely to be overweight or obese, and that inhibition of FABP6 activity has the potential to promote weight loss. Additionally, FABP6 has been shown to be involved in the regulation of lipid metabolism and has been implicated in the development of metabolic disorders, including non-alcoholic steatohepatitis (NASH).

In the context of type 2 diabetes, FABP6 has been shown to be involved in the regulation of glucose metabolism and to play a role in the development of diabetes-related diseases. Several studies have shown that individuals with higher FABP6 levels are more likely to have type 2 diabetes, and that inhibition of FABP6 activity has the potential to improve insulin sensitivity and reduce the risk of diabetes-related complications.

In the context of cardiovascular disease, FABP6 has been shown to be involved in the regulation of lipid metabolism and to play a role in the development of cardiovascular disease. Several studies have shown that individuals with higher FABP6 levels are more likely to have cardiovascular disease, and that inhibition of FABP6 activity has the potential

Protein Name: Fatty Acid Binding Protein 6

Functions: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). In vitro binds to bile acids in the order: deoxycholic acid > cholic acid > chenodeoxycholic acid and respective BA conjugation modifies affinities in the order taurine-conjugated > glycine-conjugated > unconjugated bile acids. Stimulates gastric acid and pepsinogen secretion (By similarity)

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