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TFPI is a protease inhibitor that regulates the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process initiates with the formation of a factor VIIa-TF complex, which proteolytically activates additional proteases (factors IX and X) and ultimately leads to the formation of a fibrin clot. TFPI inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. TFPI is glycosylated and predominantly found in the vascular endothelium and plasma in both

Myotonic dystrophy (DM) is an autosomal dominant neuromuscular disease that is associated with a (CTG)n repeat expansion in the 3’-untranslated region of the myotonin protein kinase gene (DMPK). CUG-BP1 and CUG-BP2 are proteins that bind specifically to (CUG)8 oligonucleotides in vitro. While CUG-BP1 has the major binding activity in normal cells, nuclear CUG-BP2 binding activity increases in DM cells. Both CUG-BP1 and CUG-BP2 are isoforms of a novel heterogeneous nuclear ribonucleoprotein (

FKBP8 is an immunophilin family member lacking PPIase/arotamase activity that influences immunoregulation, protein folding and trafficking in neurons associated with memory function. The FKBPr38 form derives from a truncated ORF. Presenilin 1 and 2 form molecular complexes with梐nd promote degradation of桭KBPr38, and Bcl-2, and sequester these proteins in ER/Golgi, thereby inhibiting FKBPr38-mediated, ?secretase-independent, mitochondrial targeting of Bcl-2. FKBP8 present in the central ne

MFF belongs to the tango11 family and plays a role in mitochondrial and peroxisomal fission. It is highly expressed in heart, kidney, liver, brain, muscle and stomach. There are five named isoforms.

Somatostatin and its related peptide cortistatin exert multiple biological actions on normal and tumoral tissue targets by interacting with somatostatin receptors (SSTRs). The protein encoded by this gene is one of the SSTRs, which is a multi-pass membrane protein and belongs to the G-protein coupled receptor 1 family. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase, and different regions of this receptor molecule are required for the activation of dif