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A highly conserved protein secreted by the prostate cancer cell line PC-3 is expressed in benign and malignant prostate tissue.

Valtonen-André, Camilla LU ; Bjartell, Anders LU ; Hellsten, Rebecka LU ; Lilja, Hans LU ; Härkönen, Pirkko LU and Lundwall, Åke LU (2007) In Biological Chemistry 388(3). p.289-295
Abstract
In this study we characterize a novel gene on human chromosome 9 and its translation product, PC3-secreted microprotein (PSMP). The gene contains three exons that encode a protein of 139 amino acid residues, including a predicted signal peptide of 36 residues. The molecule is homologous to P-microseminoprotein (MSP), a protein of unknown function, secreted at high concentration by the prostate gland. These two proteins have only 23% sequence identity, but their common origin is revealed by a preserved pattern of Cys residues. In contrast to IMSP, which shows poor conservation between species, PSMP is very conserved. High transcript levels were detected in the prostate cancer cell line PC-3. Antiserum raised against PSMP detected a protein... (More)
In this study we characterize a novel gene on human chromosome 9 and its translation product, PC3-secreted microprotein (PSMP). The gene contains three exons that encode a protein of 139 amino acid residues, including a predicted signal peptide of 36 residues. The molecule is homologous to P-microseminoprotein (MSP), a protein of unknown function, secreted at high concentration by the prostate gland. These two proteins have only 23% sequence identity, but their common origin is revealed by a preserved pattern of Cys residues. In contrast to IMSP, which shows poor conservation between species, PSMP is very conserved. High transcript levels were detected in the prostate cancer cell line PC-3. Antiserum raised against PSMP detected a protein with an apparent molecular mass of 18 kDa in culture medium conditioned by PC-3 cells, but in cell lysates the antiserum also recognized a molecular species of 16 kDa, suggesting that PSMP undergoes post-translational modification. Xeno-grafted PC-3 cell tumors in athymic nude mice showed strong staining for both PSMP protein and mRNA. Studies on human prostate cancer specimens showed immunohistochemical staining of both tumor and benign glandular cells. Our results suggest that PSMP is an important protein with significance in prostate cancer. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
semen, trachea, gene, homology, evolution
in
Biological Chemistry
volume
388
issue
3
pages
289 - 295
publisher
De Gruyter
external identifiers
  • wos:000244847300005
  • scopus:33847643281
ISSN
1437-4315
DOI
10.1515/BC.2007.032
language
English
LU publication?
yes
id
5f2245fb-f1be-421a-9c55-6cdf0def9516 (old id 166812)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17338636&dopt=Abstract
date added to LUP
2007-07-06 09:46:57
date last changed
2017-07-30 03:30:31
@article{5f2245fb-f1be-421a-9c55-6cdf0def9516,
  abstract     = {In this study we characterize a novel gene on human chromosome 9 and its translation product, PC3-secreted microprotein (PSMP). The gene contains three exons that encode a protein of 139 amino acid residues, including a predicted signal peptide of 36 residues. The molecule is homologous to P-microseminoprotein (MSP), a protein of unknown function, secreted at high concentration by the prostate gland. These two proteins have only 23% sequence identity, but their common origin is revealed by a preserved pattern of Cys residues. In contrast to IMSP, which shows poor conservation between species, PSMP is very conserved. High transcript levels were detected in the prostate cancer cell line PC-3. Antiserum raised against PSMP detected a protein with an apparent molecular mass of 18 kDa in culture medium conditioned by PC-3 cells, but in cell lysates the antiserum also recognized a molecular species of 16 kDa, suggesting that PSMP undergoes post-translational modification. Xeno-grafted PC-3 cell tumors in athymic nude mice showed strong staining for both PSMP protein and mRNA. Studies on human prostate cancer specimens showed immunohistochemical staining of both tumor and benign glandular cells. Our results suggest that PSMP is an important protein with significance in prostate cancer.},
  author       = {Valtonen-André, Camilla and Bjartell, Anders and Hellsten, Rebecka and Lilja, Hans and Härkönen, Pirkko and Lundwall, Åke},
  issn         = {1437-4315},
  keyword      = {semen,trachea,gene,homology,evolution},
  language     = {eng},
  number       = {3},
  pages        = {289--295},
  publisher    = {De Gruyter},
  series       = {Biological Chemistry},
  title        = {A highly conserved protein secreted by the prostate cancer cell line PC-3 is expressed in benign and malignant prostate tissue.},
  url          = {http://dx.doi.org/10.1515/BC.2007.032},
  volume       = {388},
  year         = {2007},
}