Proline-rich acidic protein 1, also known as Uterine-specific proline-rich acidic protein, UPA and PRAP1, is a secreted protein. PRAP1 is abundantly expressed in the epithelial cells of the liver, kidney, gastrointestinal tract and cervix. PRAP1 is up-regulated by butyrate, trichostatin A and 5'-aza-2' deoxycytidine. PRAP1 may play an important role in maintaining normal growth homeostasis in epithelial cells. PRAP1 is suppressed through epigenetic mechanisms involving histone deacetylation and methylation. PRAP1 has been shown to cause cell growth inhibition in cancer cell lines.
PRC1 (protein regulator of cytokinesis 1) is a key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. It is essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. PRC1 is required for KIF14 localization to the central spindle and midbody. It is also required to recruit PLK1 to the spindle. PRC1 stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. It is a homodimer and interacts with the C-terminal Rho-GAP domain and the basic region of RACGAP1. The interaction with RACGAP1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. PRC1 also interacts separately via its N-terminal region with the C-terminus of CENPE, KIF4A and KIF23 during late mitosis. It interacts with KIF14, IF20A and PLK1.
Lysosomal Pro-X Carboxypeptidase (PRCP) belongs to the peptidase S28 family. PRCP is detected in many tissues, with highest levels observed in placenta, lung, and liver. It is also present in the heart, brain, pancreas, and kidney. PRCP exists as a homodimer. PRCP cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. PRCP has been shown to be an activator of the cell matrix-associated prekallikrein.
PR domain containing 2; with ZNF domain (PRDM2); also known as zinc finger protein RIZ; is a member of histone methyltransferase (HMT) class enzymes that methylate lysine residues of histones or proteins. HMTs contain a conserved catalytic core termed the SET domain; which shares sequence homology with an independently described sequence motif; the PR domain. PRDM2 contains 8 C2H2-type zinc fingers and a distinct SET domain; and is highly expressed in retinoblastoma cell lines and in brain tumors; as well as in a number of other cell lines and in brain; heart; skeletal muscle; liver and spleen. PRDM2 is a S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3; and is identified as a tumor suppressor. It is reported that intact PR( SET) sequence is required for tumor suppression functions; mutations in the PR domain caused activity reduction in human cancers. Also; S-adenosylhomocysteine or methyl donor deficiency inhibits RIZ1 and other H3 lysine 9 methylation activities. PRDM2 may also function as a DNA-binding transcription factor. It Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and act as a transcriptional activator. In addition; PRDM2 (RIZ) is able to binds to the retinoblastoma protein (RB) and also Interacts with GATA3.
Peroxiredoxin-5, also known as Alu corepressor 1, Antioxidant enzyme B166, Liver tissue 2D-page spot 71B, Peroxisomal antioxidant enzyme, Thioredoxin peroxidase PMP20, Thioredoxin reductase, PRDX5 and ACR1, is cytoplasm protein that belongs to the peroxiredoxin 2 family. Peroxiredoxin-5 / PRDX5 reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Peroxiredoxin-5 / PRDX5 is involved in intracellular redox signaling. The Peroxiredoxins / Prx are a family of 25 kDa peroxidases that can reduce H2O2 using an electron from thioredoxin (Trx) or other substances. The mammalian Peroxiredoxins / Prx family is divided into six groups ( PRDX1，PRDX2, PRDX3, PRDX4, PRDX5, PRDX6 ) on the basis of homology of amino acid sequences. They are located in the cytosol and play a role in the cell signaling system. All six mammalian peroxiredoxins are expressed in the lung. Peroxiredoxins / Prx is overexpressed in breast cancer tissues to a great extent suggesting that Peroxiredoxins / Prx has a proliferative effect and may be related to cancer development or progression.
Bone Marrow Proteoglycan (BMPG) is a secreted protein that contains one C-type lectin domain. BMPG is the predominant constituent of the crystalline core of the eosinophil granule. BMPG is highly expressed in placenta and pregnancy serum. BMPG may be involved in antiparasitic defense mechanisms as a cytotoxin and helminthotoxin. BMPG induces non-cytolytic histamine release from human basophils. In addition, BMPG also participated in antiparasitic defense mechanisms and immune hypersensitivity reactions.
Inserisci la tua e-mail e seleziona le aree di interesse per ricevere le ultime novità, approfondimenti e promozioni.
Seleziona uno o più ambiti di interesse per ricevere comunicazioni più utili e mirate.
2025 TEMA Ricerca - All Rights Reserved.
