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.
Protachykinin-1(TAC1) is a secreted protein and belongs to the tachykinin family. TAC1 is encoded by the TAC1 gene. This gene encodes four products of the tachykinin peptide hormone family, substance P and neurokinin A, as well as the related peptides, neuropeptide K and neuropeptide gamma. These hormones are thought to function as neurotransmitters which interact with nerve receptors and smooth muscle cells. They are known to induce behavioral responses and function as vasodilators and secretagogues.
Ribonucleoside-Diphosphate Reductase Subunit M2 (RRM2) belongs to the ribonucleoside diphosphate reductase small chain family. The reductase of RRM2 catalyzes the formation of deoxyribonucleotides from ribonucleotides. Synthesis of the encoded protein (M2) is regulated in a cell-cycle dependent fashion. RRM2 supplies the precursors essential for DNA synthesis. RRM2 catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.
Proteinase-3 is a neutral serine proteinase that belongs to the peptidase S1 family and Elastase subfamily. It contains one peptidase S1 domain and it is expressed mainly in neutrophil granulocytes. The primary function of Proteinase-3 is thought to be degradation of extracellular proteins at sites of inflammation, but excessive or prolonged proteolytic activity may cause harmful effects in the body. It is the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the cANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease Wegener's granulomatosis.
May function as calcium sensor and contribute to cellular calcium signaling. In a calcium-dependent manner, functions by interacting with other proteins, such as EZR and PPP5C, and indirectly plays a role in physiological processes like the formation of microvilli in epithelial cells. May stimulate cell proliferation in an autocrine manner via activation of the receptor for activated glycation end products (RAGE).
Protein Delta Homolog 1 (DLK-1) is a transmembrane protein which contains a signal peptide, an extracellular domain with six tandem epidermai growth factor (EGF)-like domains, a single pass transmembrane domain, and a short cytoplasmic tail. It is found within the stromal cells in close contact to the vascular structure of placental villi, yolk sac, fetal liver, adrenal cortex and pancreas and in the beta cells of the islets of Langerhans in the adult pancreas. In addition, it is detected in some forms of neuroendocrine lung tumor tissue. DLK-1 may have a improtant role in neuroendocrine differentiation.
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