Persephin is a secreted protein, belongs to the glial cell linederived neurotrophic factor (GDNF) family of the TGF-β superfamily. It shares 38-46% amino acid (aa) identity with family members GDNF, neurturin and artemin. It is expressed at very low levels in most tissues. Mature protein contains a signal sequence, a pro-domain and a 96 aa mature sequence with several cysteines that are conserved among family members. It circulates as an unglycosylated disulfide-linked homodimer. Like other GDNF family members, Persephin acts through engagement of GRFα4, a glycosylphosphatidylinositol (GPI)-linked GDNF receptor family Persephin is reported to promote both the survival and growth of central dopaminergic and motor neurons, and kidney development. These effects are correlated with the expression patterns of GFRα4, and RET.
Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.
The protein encoded by this gene is a chemokine that is highly similar to platelet factor 4. The encoded protein displays a strong antiangiogenic function and is regulated by chemokine (C-X-C motif) receptor 3. This protein also impairs tumor growth and can protect against blood-retinal barrier breakdown in diabetes patients.
Prefoldin Subunit 2 (PFDN2) belongs to the Prefoldin Beta subunit family. The PFDN2 protein is one of six subunits of Prefoldin that act as a molecular chaperone complex that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. PFDN2 binds specifically to Cytosolic Chaperonin (c-CPN) and transfers target proteins to it. PFDN2 also binds to a nascent polypeptide chain and promotes folding in settings where there are many competing pathways for non-native proteins.
Prefoldin Subunit 4 (PFDN4) is a heterohexameric chaperone protein that belongs to the prefoldin subunit beta family. The complex of PFDN4, consisting of two PFD-alpha type and four PFD-beta type subunits, forms a double beta barrel assembly with six protruding coiled-coils. PFDN4 binds and stabilizes newly synthesized polypeptides, thereby allowing them to fold correctly.
PFK1, also known as PFKM, is a regulatory glycolytic enzyme. PFK1 converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. It is a muscle-type isozyme. There are three phosphofructokinase isozymes in humans: muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Mutations in PFK1 gene have been related with glycogen storage disease type VII, also identified as Tarui disease.
6-phosphofructokinase, muscle type is a muscle-type isozyme that in humans is encoded by the PFKM gene. It belongs to the phosphofructokinase family and Two domains subfamily. PFKM functions as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. PFK1 converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP.
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