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PLG

Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells.
Protein class

Cancer-related genes, Candidate cardiovascular disease genes, Disease related genes, Enzymes, FDA approved drug targets, Human disease related genes, Metabolic proteins, Plasma proteins

Predicted location

Secreted

Single cell type specificity

Cell type enriched (Hepatocytes)

Immune cell specificity

Not detected in immune cells

Cell line specificity

Not detected

Interaction

Interacts (both mature PLG and the angiostatin peptide) with CSPG4 and AMOT (PubMed:10889192, 16043488). Interacts (via the Kringle domains) with HRG; the interaction tethers PLG to the cell surface and enhances its activation (PubMed:9102401, 19712047). Interacts (via Kringle 4 domain) with ADA; the interaction stimulates PLG activation when in complex with DPP4 (PubMed:15016824). Angiostatin: Interacts with ATP5F1A; the interaction inhibits most of the angiogenic effects of angiostatin (PubMed:10077593). (Microbial infection) Interacts with C. albicans GPD2; the interaction is direct and provides active plasmin on the surface of fungal cells. (Microbial infection) Interacts with Staphylococcus aureus protein FnbB; this interaction provides active plasmin on the surface of bacterial cells. (Microbial infection) Interacts with P. falciparum (strain NF54) enolase ENO (via DKSLVK motif); the interaction occurs at the ookinete cell surface and is required for ookinete invasion of the mosquito midgut.

Molecular function

Hydrolase, Protease, Serine protease

More Types Infomation

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For Research Use Only. Not For Clinical Use.

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