Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04155 (pS2)
 1,234 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Approximately 50% of human breast tumors secrete a small cysteine-rich protein, pS2, of unknown function. pS2 protein was recently found to be homologous to a porcine protein with hormonogastric activity, pancreatic spasmolytic polypeptide (PSP), in which the 5-cysteine domain present in pS2 is tandemly duplicated. We have characterized cDNA species encoding PSP and its human and mouse counterparts, hSP and mSP. We show that hSP and pS2 are separately encoded in the genome, and that the two proteins are co-expressed in normal stomach epithelium. However, expression of hSP was not detected in breast tumors. Computer analysis revealed that the pattern of conserved cysteine residues in hSP and pS2, the P domain, is present at the N termini of two other mammalian proteins, intestinal sucrase-isomaltase and lysosomal alpha-glucosidase.
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PMID:hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma. 230 34

The role of estrogen in the growth of human breast cancers has been investigated at two levels. First, we have studied the pS2 gene, whose transcription is stimulated by estrogen in the human breast cancer cell line, MCF-7. The pS2 gene product is a small, secreted polypeptide currently of unknown function, but with structural features similar to some growth factors. The expression of the pS2 gene has so far been detected only in MCF-7 cells and some breast cancer biopsies. Preliminary studies indicate that pS2 is a potential marker for hormone-dependent breast cancer. Ongoing studies will continue to focus on the implicated role of pS2 in the estrogen-mediated growth of breast cancers and its possible use as a marker for estrogen-dependent tumors. Second, we have analyzed the structure and function of the human ER. The receptor stimulates pS2 gene transcription by interacting with an ERE in the 5'-flanking region of that gene. A mutational analysis of the receptor protein has localized a DNA-binding domain, which determines target gene specificity, and a hormone-binding domain. These domains appear to be the only two regions of the receptor which are absolutely required for the transcription-activating function of the ER in transfection assays with reporter plasmids. The N-terminal region of the protein (regions A and B), which is necessary for increasing the efficiency of gene expression using the pS2 ERE, but not a vitellogenin ERE, may also play a role in transcription activation. Further progress in the characterization of the ER functional domains will require studies on target genes in a more physiological chromatin environment, as well as detailed physical analyses of receptor structure.
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PMID:Structure and function of the pS2 gene and estrogen receptor in human breast cancer cells. 290 50

We have previously shown that the expression of pS2 mRNA, which encodes a secreted 60-amino acid protein of unknown function, is widely distributed throughout the entire body of the mouse including the brain. We report herein that pS2 mRNA is also expressed in the brain and in peripheral tissues of rats. In adult rat brain, pS2 mRNA was predominantly expressed in hippocampus, followed by the cerebral cortex and cerebellum. The developmental expression of pS2 mRNA in hippocampus, which region is known to mature after birth, showed a clear peak in 1- or 3-day-old rats, then gradually decreased by 7 weeks after birth. In midbrain, the maturation of which occurs at an early developmental stage, pS2 mRNA level was retained at a low level from postnatal 1 day to week 7. These results suggest that pS2 protein plays an important role in the development of central nervous system.
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PMID:Expression of pS2 gene in rat brain. 754 26

A sensitive two-site enzyme immunoassay (EIA) system was established for human pS2 protein, a small estrogen-inducible secretory protein of unknown function originally identified in MCF-7 human breast cancer cells. Our EIA system is based on the sandwiching of antigen between anti-recombinant (r) pS2 antibody IgG coated on a polystyrene plate and biotinylated anti-rpS2 antibody IgG. The amount of pS2 protein was quantified by measurement of the bound enzyme activity of subsequently added streptavidin-linked beta-D-galactosidase (beta-D-galactosidase, EC 3.2.1.23). pS2 protein purified from MCF-7 culture supernatants was detectable at a concentration as low as 3 pg/ml (corresponding to 60 fg/well). This EIA system revealed that the amount of pS2-like immunoreactivity (LI) in human urine was 13.6 ng/mg creatinine (median, n = 416) and that there was no correlation between the pS2-LI concentration in urine and sex or aging. pS2-LI levels in plasma and sera of the normal subjects were 392 pg/ml (median, n = 14) and 494 pg/ml (median, n = 12), respectively. The serum level of the patients with breast cancer (528 pg/ml; median, n = 67) was not statistically different from that of normal subjects, although high levels of pS2 protein in breast cancer tissues had been reported.
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PMID:Estimation of pS2 protein level in human body fluids by a sensitive two-site enzyme immunoassay. 798 37

By the reverse transcription-polymerase chain reaction we investigated the localization of pS2 mRNA, which encodes a secreted polypeptide of 60 amino acids with unknown function, in the adult mouse. This method revealed that the expression of pS2 mRNA was not restricted to the stomach as previously reported but was also found in various other tissues such as brain, heart, spleen, and muscle. The pS2 mRNA was additionally detected in astrocytes cultured from the whole brain of the newborn mouse. The pS2 expression in these astrocytes increased with cell growth and sharply declined after the cells reached the stationary phase. In the cells synchronized by the serum deprivation-refeeding technique, the expression of pS2 mRNA was only found at late G1 and S phase. These results suggest that the transcripts of pS2 gene are widely distributed throughout the entire body of the mouse and that they play some important cell cycle-related role in these tissues.
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PMID:pS2 gene especially expressed in the late G1/S phase of mouse astrocytes. 808 97

pS2 protein is a cysteine-rich polypeptide, of unknown function, the expression of which is induced in the human cancer cell line MCF-7 by oestrogen. The availability of a murine monoclonal antibody to human pS2 protein has prompted us to evaluate its expression in 47 cases of primary breast carcinoma. Using a double indirect immunoperoxidase technique, we compared the expression of pS2 protein in fine needle aspiration (FNA) cytology smears with that in formalin-fixed, paraffin-embedded sections from subsequently excised tumours from the same patients. We also compared the expression of pS2 protein and oestrogen receptor (ER) status using immunocytochemical assay (ER-ICA) in formalin-fixed, paraffin-embedded sections from 22 primary breast carcinomas. We found the application of immunocytochemistry in the assessment of pS2 protein expression in FNA cytology to be a reliable and cost-effective technique, having a sensitivity of 84% and a specificity of 100%. There was also a good correlation between the expression of pS2 protein and ER status.
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PMID:Immunocytochemistry in the assessment of pS2 protein expression in fine needle aspiration cytology from breast carcinoma. 811 Sep 71

We describe the isolation and characterization of Friend of Prmt1 (Fop), a novel chromatin target of protein arginine methyltransferases. Human Fop is encoded by C1orf77, a gene of previously unknown function. We show that Fop is tightly associated with chromatin, and that it is modified by both asymmetric and symmetric arginine methylation in vivo. Furthermore, Fop plays an important role in the ligand-dependent activation of estrogen receptor target genes, including TFF1 (pS2). Fop depletion results in an almost complete block of estradiol-induced promoter occupancy by the estrogen receptor. Our data indicate that Fop recruitment to the promoter is an early critical event in the activation of estradiol-dependent transcription.
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PMID:Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases. 1985 91