PSP94 (prostate secretory protein of 94 amino acids), an abundant protein within semen, has reported local functions within the reproductive tract and reported systemic functions. Mechanisms of action remain poorly understood, but binding to undefined molecules within the prostate, pituitary, testis and blood may initiate some of these actions. PSP94 serum measurements, especially of bound and free forms, have potential clinical utility in prostate cancer management. Identification of the binding molecules will help in the understanding of PSP94's action, and enable further development of PSP94 serum assays. PSPBP (PSP94-binding protein) was purified from human serum by ammonium sulphate fractionation, ion-exchange and affinity chromatography. The glycosylated protein ran as two bands on SDS/PAGE (70 and 95 kDa). N-terminal sequencing yielded a 30-amino-acid sequence, identical with the translated N-terminal region of a previously published cDNA (GenBank® accession number AX136261). Reverse transcriptase PCR and plaque hybridization demonstrated PSPBP mRNA in peripheral blood leucocytes and in a prostate cDNA library. Northern blotting showed 2 kb mRNA species in prostate, testis, ovary and intestine. Immunohistochemistry demonstrated PSPBP in tissues, including pituitary and Leydig cells, supporting a role for PSP94 in hormonal control at the pituitary gonadal axis. ELISA demonstrated that PSPBP levels were significantly lower (P=0.0014) in the serum of a prostate cancer population (n=65) compared with a control population (n=70). PSPBP identification will help the understanding of PSP94's functions and facilitate ELISA development to address the clinical value of PSP94 serum assays.
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Research Article|
December 14 2004
Identification, purification and characterization of a novel human blood protein with binding affinity for prostate secretory protein of 94 amino acids
Jonathan R. REEVES;
Jonathan R. REEVES
1
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
1To whom correspondence should be addressed (email jreeves@procyonbiopharma.com).
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Jim W. XUAN;
Jim W. XUAN
†Department of Surgery, University of Western Ontario, London, Canada, N6A 4G5
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Katerina ARFANIS;
Katerina ARFANIS
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Catherine MORIN;
Catherine MORIN
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Seema V. GARDE;
Seema V. GARDE
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Marcia T. RUIZ;
Marcia T. RUIZ
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Jan WISNIEWSKI;
Jan WISNIEWSKI
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Chandra PANCHAL;
Chandra PANCHAL
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Jerome E. TANNER
Jerome E. TANNER
*Procyon Biopharma Inc., 1650 TransCanada, Suite 200, Dorval, Québec, Canada H9P 1H7
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Publisher: Portland Press Ltd
Received:
February 23 2004
Revision Received:
June 30 2004
Accepted:
September 02 2004
Accepted Manuscript online:
September 02 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 385 (1): 105–114.
Article history
Received:
February 23 2004
Revision Received:
June 30 2004
Accepted:
September 02 2004
Accepted Manuscript online:
September 02 2004
Citation
Jonathan R. REEVES, Jim W. XUAN, Katerina ARFANIS, Catherine MORIN, Seema V. GARDE, Marcia T. RUIZ, Jan WISNIEWSKI, Chandra PANCHAL, Jerome E. TANNER; Identification, purification and characterization of a novel human blood protein with binding affinity for prostate secretory protein of 94 amino acids. Biochem J 1 January 2005; 385 (1): 105–114. doi: https://doi.org/10.1042/BJ20040290
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