neuregulin-1 (heregulin-1;NRG1) is a member of neuregulin family; which is comprised of four genes that encode a large number of secreted or membrane-bound isoforms. All family members share an EGF-like domain that interacts with the ErbB family of tyrosine kinase receptors. NRG1 isoforms can be classified into type I; type II and type III isoforms. NRG1 directs ligand for ERBB3 and ERBB4 tyrosine kinase receptors; concomitantly recruits ERBB1 and ERBB2 coreceptors; resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. NRG proteins show distinct spatial and temporal expression patterns and play important roles during development of both the nervous system and the heart.
Pro-neuregulin-1;Neuregulin-1 beta 1（NRG1） is a single-pass type I membrane protein and belongs to the neuregulin family .It contains 1 EGF-like domain and 1 Ig-like C2-type (immunoglobulin-like) domain. Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. The protein concomitantly recruits ERBB1 and ERBB2 coreceptors; resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial; glial; neuronal; and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development.
Pro-Neuropeptide Y (NPY) is a member of the NPY family. NPY is a secreted protein and is one of the most abundant peptides in the nervous system. It also can be found in some chromaffin cells of the adrenal medulla. NPY can be cleaved into Neuropeptide Y and C-flanking peptide of NPY chain, which regulates energy usage, and it is involved in learning, memory processing, and epilepsy. NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. In addition, NPY increases the proportion of energy stored as fat and blocks nociceptive signals to the brain.
PROS1, also known as protein S, is a vitamin K-dependent plasma protein that functions as a cofactor for the anticoagulant protease, activated protein C (APC) to inhibit blood coagulation. PROS1 has two isoforms: a free, functionally active form and an inactive form complexed with C4b-binding protein. Besides its anticoagulant function, PROS1 also acts as an agonist for the tyrosine kinase receptors Tyro3, Axl, and Mer. The endothelium expresses Tyro3, Axl, and Mer and produces protein S. The interaction of protein S with endothelial cells and particularly its effects on angiogenesis have not yet been analyzed.
Prostasin (Prss8), also known as channel activating protease 1 (CAP1), is a trypsinlike serine peptidase, and plays important roles in epithelial physiology. It is originally purified as an active, soluble enzyme from human seminal fluid and is highly expressed in prostate, lung, kidney, salivary gland and pancreas. Prostasin is expressed as a glycosyl-phosphatidylinositol (GPI)-anchored membrane protein in prostate epithelial cells, and also exists as a secreted proteolytic enzyme possibly via tryptic cleavage of its COOH-terminal hydrophobic domain. Prostasin is found to activate the epithelial sodium channel (ENaC) which is tightly regulated and is critical for maintaining salt and fluid balance in the lung and kidney in both normal and pathological conditions. Accordingly, prostasin has been proposed as a target for therapeutic inhibition in cystic fibrosis. In addition, prostasin inhibits prostate and breast cancer cell invasion in vitro, suggesting a functional role as a suppressor of tumor invasion, as well as a regulator of gene expression during inflammation.
Prostatic acid phosphatase (PAP, or ACPP), also known as prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. As a non-specific phosphomonoesterase, Prostatic acid phosphatase synthetized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Prostatic acid phosphatase is a clinically important protein for its relevance as a biomarker of prostate carcinoma. Furthermore, it has a potential role in fertilization. The major action of PAP is to dephosphorylate macromolecules with the help of catalytic residues (His(12) and Asp(258)) that are located in the cleft between two domains. Cellular prostatic acid phosphatase (cPAcP), an authentic tyrosine phosphatase, is proposed to function as a negative growth regulator of prostate cancer (PCa) cells in part through its dephosphorylation of ErbB-2. cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Injection of the secretory isoform of PAP has potent antinociceptive effects in mouse models of chronic pain. This enzyme exhibits ecto-5'-nucleotidase activity, is widely distributed, and implicated in the formation of chronic pain. Additionally, PAP could be a target molecule in specific immunotherapy for patients with nonprostate adenocarcinomas including colon and gastric cancers.
Prostatic Acid Phosphatase (PAP) belongs to the histidine acid phosphatase family. PAP can catalyze the hydrolysis of member of phosphate monoestyers, including phosphorylated protein. PAP can high expression in metastasized prostate cancer, moderately expression level in bone diseases, blood cell disease, and the concentration of PAP is used to monitor and assess the proession of prostate cancer. The optimum PH of PAP is from 4 to 6; its activity can be inhibited by L(+)-tartrate.
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