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== Function ==
== Function ==


Beta-microseminoprotein is a member of the immunoglobulin binding factor family. It is one of the three major proteins secreted by the epithelial cells of the prostate<ref name="pmid3347596">{{cite journal | author = Lilja H, Abrahamsson PA | title = Three predominant proteins secreted by the human prostate gland | journal = Prostate | volume = 12 | issue = 1 | pages = 29–38 | year = 1988 | pmid = 3347596 | doi = 10.1002/pros.2990120105}}</ref> and has a concentration in seminal plasma of 0.5 to 1 mg/mL<ref name="pmid18222915">{{cite journal | author = Valtonen-André C, Sävblom C, Fernlund P, Lilja H, Giwercman A, Lundwall A | title = Beta-microseminoprotein in serum correlates with the levels in seminal plasma of young, healthy males | journal = J. Androl. | volume = 29 | issue = 3 | pages = 330–7 | year = 2008 | pmid = 18222915 | doi = 10.2164/jandrol.107.003616 }}</ref>. Two comprehensive studies of beta-microseminoprotein in tissue have shown that it is secreted by epithelial cells in many organs: liver, lung, breast, kidney, colon, stomach, pancreas, esophagus, duodenum, salivary glands, fallopian tube, corpus uteri, bulbourethral glands and cervix<ref>{{cite journal|last=Weiber|first=H|coauthors=Andersson, C; Murne, A; Rannevik, G; Lindström, C; Lilja, H; Fernlund, P|title=Beta microseminoprotein is not a prostate-specific protein. Its identification in mucous glands and secretions.|journal=The American journal of pathology|date=1990 Sep|volume=137|issue=3|pages=593-603|pmid=2205099}}</ref><ref>{{cite journal|last=Ohkubo|first=I|coauthors=Tada, T; Ochiai, Y; Ueyama, H; Eimoto, T; Sasaki, M|title=Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization.|journal=The international journal of biochemistry & cell biology|date=1995 Jun|volume=27|issue=6|pages=603-11|pmid=7671139}}</ref>. Interestingly, this list corresponds closely to the sites from which all late onset cancers develop{{Citation needed}}. This protein has been reported to have [[inhibin]]-like properties<ref>{{cite journal|last=Sheth|first=AR|title=Characterization of a polypeptide from human seminal plasma with inhibin (inhibition of FSH secretion)-like activity|journal=FEBS Lett|year=1984|pmid=6692908}}</ref>, though this finding has been disputed<ref>{{cite journal|last=Kohan|first=S|coauthors=Fröysa, B; Cederlund, E; Fairwell, T; Lerner, R; Johansson, J; Khan, S; Ritzen, M; Jörnvall, H; Cekan, S|title=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.|journal=FEBS letters|date=1986 Apr 21|year=1986|volume=199|issue=2|pages=242-8|pmid=3084296}}</ref><ref>{{cite journal|last=Gordon|first=WL|coauthors=Liu, WK; Akiyama, K; Tsuda, R; Hara, M; Schmid, K; Ward, DN|title=Beta-microseminoprotein (beta-MSP) is not an inhibin.|journal=Biology of reproduction|date=1987 May|volume=36|issue=4|pages=829-35|pmid=3109514}}</ref>. 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.<ref name="entrez" /> Beta-microseminoprotein is the main component in seminal plasma active against ''[[Candida albicans]]'' after sexual intercourse.<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref> Despite having only 4 out of 11 amino acids in common, both the porcine and human fungicidal peptide on the MSMB protein's C-terminus are potently fungicidal in the absence of calcium ions.<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref> The protein inhibits growth of cancer cells in an experimental model of prostate cancer<ref name="pmid12727822">{{cite journal | author = Shukeir N, Arakelian A, Kadhim S, Garde S, Rabbani SA | title = Prostate secretory protein PSP-94 decreases tumor growth and hypercalcemia of malignancy in a syngenic in vivo model of prostate cancer | journal = Cancer Res. | volume = 63 | issue = 9 | pages = 2072–8 | year = 2003 | month = May | pmid = 12727822 | doi = }}</ref> and is used as a biomarker for prostate cancer.<ref name="pmid19790236">{{cite journal | author = Whitaker HC, Warren AY, Eeles R, Kote-Jarai Z, Neal DE | title = The potential value of microseminoprotein-beta as a prostate cancer biomarker and therapeutic target | journal = Prostate | volume = 70 | issue = 3 | pages = 333–40 | year = 2010 | month = February | pmid = 19790236 | doi = 10.1002/pros.21059 }}</ref>
Beta-microseminoprotein is a member of the immunoglobulin binding factor family. It is one of the three major proteins secreted by the epithelial cells of the prostate<ref name="pmid3347596">{{cite journal | author = Lilja H, Abrahamsson PA | title = Three predominant proteins secreted by the human prostate gland | journal = Prostate | volume = 12 | issue = 1 | pages = 29–38 | year = 1988 | pmid = 3347596 | doi = 10.1002/pros.2990120105}}</ref> and has a concentration in seminal plasma of 0.5 to 1 mg/mL<ref name="pmid18222915">{{cite journal | author = Valtonen-André C, Sävblom C, Fernlund P, Lilja H, Giwercman A, Lundwall A | title = Beta-microseminoprotein in serum correlates with the levels in seminal plasma of young, healthy males | journal = J. Androl. | volume = 29 | issue = 3 | pages = 330–7 | year = 2008 | pmid = 18222915 | doi = 10.2164/jandrol.107.003616 }}</ref>. Two comprehensive studies of beta-microseminoprotein in tissue have shown that it is secreted by epithelial cells in many organs: liver, lung, breast, kidney, colon, stomach, pancreas, esophagus, duodenum, salivary glands, fallopian tube, corpus uteri, bulbourethral glands and cervix<ref>{{cite journal|last=Weiber|first=H|coauthors=Andersson, C; Murne, A; Rannevik, G; Lindström, C; Lilja, H; Fernlund, P|title=Beta microseminoprotein is not a prostate-specific protein. Its identification in mucous glands and secretions.|journal=The American journal of pathology|date=1990 Sep|volume=137|issue=3|pages=593-603|pmid=2205099}}</ref><ref>{{cite journal|last=Ohkubo|first=I|coauthors=Tada, T; Ochiai, Y; Ueyama, H; Eimoto, T; Sasaki, M|title=Human seminal plasma beta-microseminoprotein: its purification, characterization, and immunohistochemical localization.|journal=The international journal of biochemistry & cell biology|date=1995 Jun|volume=27|issue=6|pages=603-11|pmid=7671139}}</ref>. Interestingly, this list corresponds closely to the sites from which all late onset cancers develop{{Citation needed}}. This protein has been reported to have [[inhibin]]-like properties<ref>{{cite journal|last=Sheth|first=AR|title=Characterization of a polypeptide from human seminal plasma with inhibin (inhibition of FSH secretion)-like activity|journal=FEBS Lett|year=1984|pmid=6692908}}</ref>, though this finding has been disputed<ref>{{cite journal|last=Kohan|first=S|coauthors=Fröysa, B; Cederlund, E; Fairwell, T; Lerner, R; Johansson, J; Khan, S; Ritzen, M; Jörnvall, H; Cekan, S|title=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.|journal=FEBS letters|date=1986 Apr 21|year=1986|volume=199|issue=2|pages=242-8|pmid=3084296}}</ref><ref>{{cite journal|last=Gordon|first=WL|coauthors=Liu, WK; Akiyama, K; Tsuda, R; Hara, M; Schmid, K; Ward, DN|title=Beta-microseminoprotein (beta-MSP) is not an inhibin.|journal=Biology of reproduction|date=1987 May|volume=36|issue=4|pages=829-35|pmid=3109514}}</ref>. 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.<ref name="entrez" /> Beta-microseminoprotein is the main component in seminal plasma active against ''[[Candida albicans]]'' after sexual intercourse.<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref> Despite having only 4 out of 11 amino acids in common, both the porcine and human fungicidal peptide on the MSMB protein's C-terminus are potently fungicidal in the absence of calcium ions.<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref> The protein inhibits growth of cancer cells in an experimental model of prostate cancer<ref name="pmid12727822">{{cite journal | author = Shukeir N, Arakelian A, Kadhim S, Garde S, Rabbani SA | title = Prostate secretory protein PSP-94 decreases tumor growth and hypercalcemia of malignancy in a syngenic in vivo model of prostate cancer | journal = Cancer Res. | volume = 63 | issue = 9 | pages = 2072–8 | year = 2003 | month = May | pmid = 12727822 | doi = }}</ref>.


== Clinical significance ==
== 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)<ref>{{cite journal|last=Thomas|first=G|title=Multiple loci identified in a genome-wide association study of prostate cancer|journal=Nat Genet|year=2008|pmid=18264096}}</ref><ref>{{cite journal|last=Eeles|first=R.A.|title=Multiple newly identified loci associated with prostate cancer susceptibility|journal=Nat Genet|year=2008|pmid=18264097}}</ref>. 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<ref>{{cite journal|last=Xu|first=K|title=Identification of a specifically expressed modified form of novel PSP-94 protein in the secretion of benign prostatic hyperplasia|journal=Electrophoresis|year=2003|pmid=12707925}}</ref>. This truncated form of the MSMB protein lacks the fungicidal peptide identified in 2012<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref>. The expression of MSMB is found to be decreased in [[prostate cancer]]; urinary MSMB has been found to be superior than urinary [[prostate-specific antigen|PSA]] at differentiating men with prostate cancer at all [[Gleason Grading System|Gleason grades]].<ref name="Whitaker_2010">{{cite journal | author = Whitaker HC | title = The rs10993994 Risk Allele for Prostate Cancer Results in Clinically Relevant Changes in Microseminoprotein-Beta Expression in Tissue and Urine | journal = PLoS ONE | year = 2010 | volume = 5 | issue = 10 | pages = e13363 | doi = 10.1371/journal.pone.0013363 | author-separator = , | author2 = Kote-Jarai Z | author3 = Ross-Adams H | author4 = Warren AY | author5 = Burge J | display-authors = 5 | editor1-last = Vickers | editor1-first = Andrew | last6 = George | first6 = Anne | last7 = Bancroft | first7 = Elizabeth | last8 = Jhavar | first8 = Sameer | last9 = Leongamornlert | first9 = Daniel | pmid = 20967219 | pmc = 2954177 }}</ref>
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)<ref>{{cite journal|last=Thomas|first=G|title=Multiple loci identified in a genome-wide association study of prostate cancer|journal=Nat Genet|year=2008|pmid=18264096}}</ref><ref>{{cite journal|last=Eeles|first=R.A.|title=Multiple newly identified loci associated with prostate cancer susceptibility|journal=Nat Genet|year=2008|pmid=18264097}}</ref>. 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<ref>{{cite journal|last=Xu|first=K|title=Identification of a specifically expressed modified form of novel PSP-94 protein in the secretion of benign prostatic hyperplasia|journal=Electrophoresis|year=2003|pmid=12707925}}</ref>. This truncated form of the MSMB protein lacks the fungicidal peptide identified in 2012<ref name="pmid22496651">{{cite journal | author = Edström Hägerwall AM, Rydengård V, Fernlund P, Mörgelin M, Baumgarten M, Cole AM, Malmsten M, Kragelund BB, Sørensen OE | title = β-Microseminoprotein Endows Post Coital Seminal Plasma with Potent Candidacidal Activity by a Calcium- and pH-Dependent Mechanism | journal = PLoS Pathog. | volume = 8 | issue = 4 | pages = e1002625 | year = 2012 | month = April | pmid = 22496651 | doi = 10.1371/journal.ppat.1002625 }}</ref>. The expression of MSMB is found to be decreased in [[prostate cancer]], so it may be used as a biomarker for prostate cancer.<ref name="pmid19790236">{{cite journal | author = Whitaker HC, Warren AY, Eeles R, Kote-Jarai Z, Neal DE | title = The potential value of microseminoprotein-beta as a prostate cancer biomarker and therapeutic target | journal = Prostate | volume = 70 | issue = 3 | pages = 333–40 | year = 2010 | month = February | pmid = 19790236 | doi = 10.1002/pros.21059 }}</ref>. Urinary MSMB has been found to be superior than urinary [[prostate-specific antigen|PSA]] at differentiating men with prostate cancer at all [[Gleason Grading System|Gleason grades]].<ref name="Whitaker_2010">{{cite journal | author = Whitaker HC | title = The rs10993994 Risk Allele for Prostate Cancer Results in Clinically Relevant Changes in Microseminoprotein-Beta Expression in Tissue and Urine | journal = PLoS ONE | year = 2010 | volume = 5 | issue = 10 | pages = e13363 | doi = 10.1371/journal.pone.0013363 | author-separator = , | author2 = Kote-Jarai Z | author3 = Ross-Adams H | author4 = Warren AY | author5 = Burge J | display-authors = 5 | editor1-last = Vickers | editor1-first = Andrew | last6 = George | first6 = Anne | last7 = Bancroft | first7 = Elizabeth | last8 = Jhavar | first8 = Sameer | last9 = Leongamornlert | first9 = Daniel | pmid = 20967219 | pmc = 2954177 }}</ref>


== References ==
== References ==

Revision as of 20:54, 4 January 2013

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

Function

Beta-microseminoprotein is a member of the immunoglobulin binding factor family. It 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 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]. This protein has been reported to have inhibin-like properties[7], though this finding has been disputed[8][9]. 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.[10] Despite having only 4 out of 11 amino acids in common, both the porcine and human fungicidal peptide on the MSMB protein's C-terminus are potently fungicidal in the absence of calcium ions.[10] The protein inhibits growth of cancer cells in an experimental model of prostate cancer[11].

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)[12][13]. 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[14]. This truncated form of the MSMB protein lacks the fungicidal peptide identified in 2012[10]. The expression of MSMB is found to be decreased in prostate cancer, so it may be used as a biomarker for prostate cancer.[15]. Urinary MSMB has been found to be superior than urinary PSA at differentiating men with prostate cancer at all Gleason grades.[16]

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. ^ Sheth, AR (1984). "Characterization of a polypeptide from human seminal plasma with inhibin (inhibition of FSH secretion)-like activity". FEBS Lett. PMID 6692908.
  8. ^ 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)
  9. ^ 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)
  10. ^ 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)
  11. ^ 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)
  12. ^ Thomas, G (2008). "Multiple loci identified in a genome-wide association study of prostate cancer". Nat Genet. PMID 18264096.
  13. ^ Eeles, R.A. (2008). "Multiple newly identified loci associated with prostate cancer susceptibility". Nat Genet. PMID 18264097.
  14. ^ 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.
  15. ^ 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)
  16. ^ 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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