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MSMB

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Template:PBB Beta-microseminoprotein is a protein that in humans is encoded by the MSMB gene.[1][2]. For historical reasons, the scientific literature may also refer to this protein as Prostate secretory protein 94 (PSP94), microseminoprotein (MSP), microseminoprotein-beta (MSMB), beta-inhibitin, prostatic inhibin peptide (PIP), and inhibitin like material (ILM).

Distribution

MSMB is one of the three major proteins secreted by the epithelial cells of the prostate[3] and has a concentration in seminal plasma of 0.5 to 1 mg/mL[4]. Two comprehensive studies of beta-microseminoprotein in tissue have shown that it is secreted by epithelial cells in many other organs: liver, lung, breast, kidney, colon, stomach, pancreas, esophagus, duodenum, salivary glands, fallopian tube, corpus uteri, bulbourethral glands and cervix[5][6]. Interestingly, this list corresponds closely to the sites from which all late onset cancers develop[citation needed].

Evolution and Structure

MSMB is a rapidly evolving protein[7]. Solution structures of human and porcine MSMB show remarkable similarity despite having only 51% of amino acids in common[8]. The C-terminus domain of MSMB contains two two-stranded β-sheets; these have no resemblance to other structural motifs[9]. The rapid evolution of MSMB can be attributed to either sexual selection or innate pathogen defense[10]; the wide distribution of MSMB in the body and the fungicidal properties of the C-terminus suggest that innate pathogen defense plays a role in driving this evolution.

Function

Beta-microseminoprotein is a member of the immunoglobulin binding factor family. This protein has been reported to have inhibin-like properties[11], though this finding has been disputed[12][13]. It may have a role as an autocrine paracrine factor in uterine, breast and other female reproductive tissues. Two alternatively spliced transcript variants encoding different isoforms are described for this gene. The use of alternate polyadenylation sites has been found for this gene.[2] Beta-microseminoprotein is the main component in seminal plasma active against Candida albicans after sexual intercourse.[14] Despite having only 4 out of 11 amino acids in common, both the porcine and human fungicidal peptide on MSMB's C-terminus are potently fungicidal in the absence of calcium ions.[14] The protein inhibits growth of cancer cells in an experimental model of prostate cancer[15] [16][17], though this property is cell line specific[18].

Clinical significance

Two large genome-wide association studies showed that decreased expression of the MSMB protein caused by the rs10993994 single nucleotide polymorphism is associated with an increased risk of developing prostate cancer (odds ratio for CT allele pair ~1.2x, and for TT allele pair ~1.6x when compared to the low risk CC allele pair)[19][20]. A 2003 study proposed using a truncated form of the MSMB protein called PSP61 as a biomarker for benign prostatic hyperplasia (BPH): this study found PSP61 in the expressed prostatic secretion of 10 out of ten 10 men suffering from BPH, but did not find it in 10 out of 10 aged matched BPH free men[21]. This truncated form of the MSMB protein lacks the fungicidal peptide identified in 2012[14]. The expression of MSMB is found to be decreased in prostate cancer, so it may be used as a biomarker for prostate cancer.[22]. Urinary MSMB has been found to be superior than urinary PSA at differentiating men with prostate cancer at all Gleason grades.[23]

References

  1. ^ Ulvsback M, Spurr NK, Lundwall A (1992). "Assignment of the human gene for beta-microseminoprotein (MSMB) to chromosome 10 and demonstration of related genes in other vertebrates". Genomics. 11 (4): 920–4. doi:10.1016/0888-7543(91)90015-7. PMID 1783399. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  2. ^ a b "Entrez Gene: MSMB microseminoprotein, beta-".
  3. ^ Lilja H, Abrahamsson PA (1988). "Three predominant proteins secreted by the human prostate gland". Prostate. 12 (1): 29–38. doi:10.1002/pros.2990120105. PMID 3347596.
  4. ^ Valtonen-André C, Sävblom C, Fernlund P, Lilja H, Giwercman A, Lundwall A (2008). "Beta-microseminoprotein in serum correlates with the levels in seminal plasma of young, healthy males". J. Androl. 29 (3): 330–7. doi:10.2164/jandrol.107.003616. PMID 18222915.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  5. ^ Weiber, H (1990 Sep). "Beta microseminoprotein is not a prostate-specific protein. Its identification in mucous glands and secretions". The American journal of pathology. 137 (3): 593–603. PMID 2205099. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  6. ^ Ohkubo, I (1995 Jun). "Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization". The international journal of biochemistry & cell biology. 27 (6): 603–11. PMID 7671139. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  7. ^ Nolet, S (1991 Apr). "Rapid evolution of prostatic protein PSP94 suggested by sequence divergence between rhesus monkey and human cDNAs". Genomics. 9 (4): 775–7. PMID 2037304. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  8. ^ Ghasriani, H (2006 Sep 22). "Solution structures of human and porcine beta-microseminoprotein". Journal of molecular biology. 362 (3): 502–15. PMID 16930619. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  9. ^ Ghasriani, H (2006 Sep 22). "Solution structures of human and porcine beta-microseminoprotein". Journal of molecular biology. 362 (3): 502–15. PMID 16930619. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  10. ^ Clark, NL (2005 Sep). "Pervasive adaptive evolution in primate seminal proteins". PLoS genetics. 1 (3): e35. PMID 16170411. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  11. ^ Sheth, AR (1984). "Characterization of a polypeptide from human seminal plasma with inhibin (inhibition of FSH secretion)-like activity". FEBS Lett. PMID 6692908.
  12. ^ Kohan, S (1986 Apr 21). "Peptides of postulated inhibin activity. Lack of in vitro inhibin activity of a 94-residue peptide isolated from human seminal plasma, and of a synthetic replicate of its C-terminal 28-residue segment". FEBS letters. 199 (2): 242–8. PMID 3084296. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)CS1 maint: date and year (link)
  13. ^ Gordon, WL (1987 May). "Beta-microseminoprotein (beta-MSP) is not an inhibin". Biology of reproduction. 36 (4): 829–35. PMID 3109514. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  14. ^ a b c Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE (2012). "β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism". PLoS Pathog. 8 (4): e1002625. doi:10.1371/journal.ppat.1002625. PMID 22496651. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  15. ^ Garde, S (1993). "Effect of prostatic inhibin peptide (PIP) on prostate cancer cell growth in vitro and in vivo". The Prostate. 22 (3): 225–33. PMID 8488155. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  16. ^ Garde, SV (1999 Feb 1). "Prostate secretory protein (PSP94) suppresses the growth of androgen-independent prostate cancer cell line (PC3) and xenografts by inducing apoptosis". The Prostate. 38 (2): 118–25. PMID 9973097. {{cite journal}}: Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  17. ^ Shukeir N, Arakelian A, Kadhim S, Garde S, Rabbani SA (2003). "Prostate secretory protein PSP-94 decreases tumor growth and hypercalcemia of malignancy in a syngenic in vivo model of prostate cancer". Cancer Res. 63 (9): 2072–8. PMID 12727822. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  18. ^ Pathak, BR (2010 Sep). "Growth inhibition mediated by PSP94 or CRISP-3 is prostate cancer cell line specific". Asian journal of andrology. 12 (5): 677–89. PMID /20676114. {{cite journal}}: Check |pmid= value (help); Check date values in: |date= (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  19. ^ Thomas, G (2008). "Multiple loci identified in a genome-wide association study of prostate cancer". Nat Genet. PMID 18264096.
  20. ^ Eeles, R.A. (2008). "Multiple newly identified loci associated with prostate cancer susceptibility". Nat Genet. PMID 18264097.
  21. ^ Xu, K (2003). "Identification of a specifically expressed modified form of novel PSP-94 protein in the secretion of benign prostatic hyperplasia". Electrophoresis. PMID 12707925.
  22. ^ Whitaker HC, Warren AY, Eeles R, Kote-Jarai Z, Neal DE (2010). "The potential value of microseminoprotein-beta as a prostate cancer biomarker and therapeutic target". Prostate. 70 (3): 333–40. doi:10.1002/pros.21059. PMID 19790236. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  23. ^ Whitaker HC; Kote-Jarai Z; Ross-Adams H; Warren AY; Burge J; et al. (2010). Vickers, Andrew (ed.). "The rs10993994 Risk Allele for Prostate Cancer Results in Clinically Relevant Changes in Microseminoprotein-Beta Expression in Tissue and Urine". PLoS ONE. 5 (10): e13363. doi:10.1371/journal.pone.0013363. PMC 2954177. PMID 20967219. {{cite journal}}: Unknown parameter |author-separator= ignored (help)CS1 maint: unflagged free DOI (link)

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