Identification of binding proteins for PSP94 in human prostate adenocarcinoma cell lines LNCaP and PC-3

Yang, Jing-ping; Baijal-Gupta, Madhulika; Garde, Seema V.; Fraser, Jennifer E.; Finkelman, Malcolm; Clarke, Michael W.

doi:10.1002/(sici)1097-0045(19980401)35:1<11::aid-pros2>3.0.co;2-k

Cited by 10 publications

(5 citation statements)

References 22 publications

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“…In the prostate MSMB is found in the cytoplasm and at the membrane of tumor cells and cell lines from where it is secreted. MSMB is expressed in the commonly used LNCaP and PC3 prostate cancer cell lines despite their derivation from tumors that we would expect to have low or lost MSMB expression [37,38]. MSMB binding sites on LNCaP cells are up-regulated following treatment with exogenous MSMB supporting the concept that its regulation may involve autocrine or paracrine signaling [38].…”

Section: The Functionof Msmb Inprostate Cellsmentioning

confidence: 78%

The potential value of microseminoprotein‐β as a prostate cancer biomarker and therapeutic target

et al. 2009

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Section: The Functionof Msmb Inprostate Cellsmentioning

confidence: 78%

The potential value of microseminoprotein‐β as a prostate cancer biomarker and therapeutic target

et al. 2009

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“…MSP has also been suggested to be the major immunoglobulinbinding protein in semen (Liang et al, 1991;Kamada et al, 1998). Several studies have indicated binding sites for MSP in different tissues and cells (Phadke et al, 1982;Vanage and Sheth, 1982;Dandekar et al, 1983;Yang et al, 1998). Recently, a binding protein, denoted PSP94-binding protein (PSPBP), was purified from human serum, and PSPBP-mRNA was detected in blood leucocytes, prostate, testis, ovary, and intestine (Reeves et al, 2005).…”

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confidence: 99%

The Cotton-Top Tamarin (Saguinus oedipus) Has Five β-Microseminoprotein Genes, Two of Which Are Pseudogenes

Valtonen‐André

Lundwall

2008

DNA and Cell Biology

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beta-Microseminoprotein (MSP) is one of the most abundant proteins in human seminal plasma and is secreted from the prostate gland. Its evolution can be traced from primates down to nonvertebrate species such as amphioxus, despite substantial differences in the primary structure. Most mammals are known to have one single MSP gene, but we have previously shown that the cotton-top tamarin and the common marmoset-two New World monkeys-carry several MSP genes. In this study we continue our characterization of MSP genes in the cotton-top tamarin by presenting the full nucleotide sequence of the three previously identified genes, mspA, mspE, and mspJ. A promoter analysis using the luciferase reporter showed that mspE is as transcriptionally active as the single human MSP gene, whereas mspA and mspJ display no activity with this assay. Two novel MSP genes were also identified, mspB and mspH, both of which are pseudogenes. MspB has a frameshift mutation in the third exon resulting in a new C-terminus and premature stop of translation. MspH has the features of a processed pseudogene, originating from a transcript of mspE. It is integrated into the genome together with another processed pseudogene originating from a transcript of the nucleoporin gene NUP88. The MSP genes described in this study probably arose by phylogenetically rather late duplication or retrotransposition, suggesting that they are confined to a limited number of New World monkeys.

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“…Another interesting source of MSP is the ovaries, where it is preferentially expressed in the corpus luteum [17]. Other studies have reported MSP binding to cells, such as spermatozoa and prostate cancer cells, and to other secreted molecules [7, 18, 19]. However, the significance of all these interactions is not clear and the biological function of MSP remains unknown.…”

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New World, but not Old World, monkeys carry several genes encoding β‐microseminoprotein

Makinen¹,

Valtonen‐André²,

Lundwall³

1999

European Journal of Biochemistry

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It was shown by Southern hybridization that cotton-top tamarin and common marmoset, New World monkeys, carry three or more genes encoding b-microseminoprotein, also known as PSP 94 . In contrast, the genomes of Old World monkeys, as represented by rhesus macaque and sacred baboon, contain a single gene. Clones containing three different genes encoding b-microseminoprotein were isolated from a cotton-top tamarin genomic library. They carry two complete genes of four exons and a third gene lacking the first exon. The structure suggests that the three genes are functionally active and give rise to transcripts that are < 86% similar in sequence. By sequencing one gene in full, it was shown that the introns carry an excess of interspersed repeats, on average 29% of the introns consist of Alu repeats. A phylogenetic analysis demonstrated that the genes probably arose in New World monkeys after the separation from Old World primates.Keywords: evolution; mucous; prostate; semen.Semen is formed by the ejaculatory mixing of sperm-rich epididymal fluid and secretions provided by the accessory sex glands, i.e. mainly the seminal vesicles and the prostate. The biological significance of most proteins in these secretions is still unknown, even though some of them are very abundant in seminal plasma. Proteins secreted by the prostate gland have been widely investigated in order to learn more about fertility and to find new ways of detecting and treating prostate cancer. Prostate-specific antigen, prostate-secreted acid phosphatase and b-microseminoprotein (MSP) are proteins expressing the highest levels in prostate fluid [1]. Prostate-specific antigen is well known as a marker for detection and management of prostate cancer [2±4]; it is the most abundant protease in human seminal plasma, where it degrades the major coagulating proteins, the seminal vesicle secreted semenogelin I and semenogelin II [5]. Despite efforts, the function of MSP and prostate-secreted acid phosphatase remain unclear.MSP was originally isolated from human seminal plasma, where it is present at a concentration of approximately 1 mg´mL 21 [1,6±8]. Another name for this protein is`prostatic secretory protein of 94 amino acids' (PSP 94 ) reflecting both the size of the secreted protein and the high concentration in prostatic secretion [9]. It is synthesized as a precursor of 114 amino acid residues from which a signal peptide is cleaved to yield the mature, secreted protein. The primary structure is known both from work on the isolated protein [10±12] and by deduction from the sequence of cloned cDNA [9]. It is a nonglycosylated, disulfide bond-rich protein with a structure unrelated to any other known protein.Earlier research devised a function for the protein as an inhibitor of follicle stimulating hormone release from the pituitary gland and it was therefore named b-inhibin [13], but the inhibin activity was later shown to be false [14,15]. More recent studies have shown expression of MSP in nonprostate tissues, e.g. the gastrointestinal and respirator...

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Identification of binding proteins for PSP94 in human prostate adenocarcinoma cell lines LNCaP and PC-3

Cited by 10 publications

References 22 publications

The potential value of microseminoprotein‐β as a prostate cancer biomarker and therapeutic target

The potential value of microseminoprotein‐β as a prostate cancer biomarker and therapeutic target

The Cotton-Top Tamarin (Saguinus oedipus) Has Five β-Microseminoprotein Genes, Two of Which Are Pseudogenes

New World, but not Old World, monkeys carry several genes encoding β‐microseminoprotein

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