Molecular cloning of a small prostate protein, known as β-microsemenoprotein, PSP94 or β-inhibin, and demonstration of transcripts in non-genital tissues

Ulvsbäck, Magnus; Lindström, C; Weiber, Håkan; Abrahamsson, Per‐Anders; Lilja, Hans; Lundwall, Åke

doi:10.1016/0006-291x(89)91812-3

Cited by 62 publications

(40 citation statements)

References 24 publications

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“…Because PSP94 has been shown to be localized in glandular tissue of the bronchial tissue (38), one might speculate that it is a biomarker of increased glandular activity in any type of airway disease, possibly increasing in expression as a result of smoking. Previous studies have implicated PSP94 (immunoglobulin binding factor, IgBF) in chronic airway disease (39), although no mechanism has been identified.…”

Section: Discussionmentioning

confidence: 99%

Identification of Lipocalin and Apolipoprotein A1 as Biomarkers of Chronic Obstructive Pulmonary Disease

Nicholas

Skipp²,

Barton³

et al. 2010

Am J Respir Crit Care Med

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Rationale: Much effort is being made to discover noninvasive biomarkers of chronic airway disease that might enable better management, predict prognosis, and provide new therapeutic targets. Objectives: To undertake a comprehensive, unbiased proteomic analysis of induced sputum and identify novel noninvasive biomarkers for chronic obstructive pulmonary disease (COPD). Methods: Induced sputum was obtained from patients with COPD with a spectrum of disease severity and from control subjects. Twodimensional gel electrophoresis and mass spectrometric identification of differentially expressed proteins were first applied to induced sputum from patients with GOLD stage 2 COPD and healthy smoker control subjects. Initial results thus obtained were validated by a combination of immunoassays (Western blotting and ELISA) applied to a large subject cohort. The biomarkers were localized to bronchial mucosa by immunohistochemistry. Measurements and Main Results: Of 1,325 individual protein spots identified, 37 were quantitatively and 3 qualitatively different between the two groups (P , 0.05%). Forty protein spots were subjected to tandem mass spectrometry, which identified 15 separate protein species. Seven of these were further quantified in induced sputum from 97 individuals. Using this sequential approach, two of these potential biomarkers (apolipoprotein A1 and lipocalin-1) were found to be significantly reduced in patients with COPD when compared with healthy smokers. Their levels correlated with FEV 1 /FVC, indicating their relationship to disease severity. Conclusions: A potential role for apolipoprotein A1 and lipocalin-1 in innate defense has been postulated previously; our discovery of their reduction in COPD indicates a deficient innate defense system in airway disease that could explain increased susceptibility to infectious exacerbations.

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Section: Discussionmentioning

confidence: 99%

Identification of Lipocalin and Apolipoprotein A1 as Biomarkers of Chronic Obstructive Pulmonary Disease

Nicholas

Skipp²,

Barton³

et al. 2010

Am J Respir Crit Care Med

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“…Sa sequence en acides amines n'indique pas d'homologie globale avec des protEines connues. Cependant, il existe de courtes sequences de la partie carboxyterminale de la protEine qui ont une certaine similarit6 avec les chaines A et B de la 13-inhibine ovarienne (18). On ne croit pas que la PSP94 ait vEritablement d'activit6 de type inhibine in vivo.…”

Section: La Prot~ine De S~cr~tion Prostatique De 94 Acides Aminesunclassified

Les proteines majeures de la secretion prostatique

Dubé

1991

Androl.

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“…Recently, CRISP-1 in rats was shown to inhibit capacitation of spermatozoa and thus prevent premature sperm activation [17]. MSP is not mixed with spermatozoa before ejaculation as it is exclusively secreted by the prostate gland in the human male reproductive tract [7,18]. This implies that CRISP-3 in the epididymal fluid may be available to interact with spermatozoa and epithelium, but that any excess of CRISP-3 will be bound in complex with MSP shortly after ejaculatory mixing with the prostatic fluid.…”

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confidence: 99%

β-Microseminoprotein binds CRISP-3 in human seminal plasma

Udby

Lundwall

Johnsen

et al. 2005

Biochemical and Biophysical Research Communications

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Abstractβ -Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its aminoterminal SCP-domain. KeywordsCysteine-rich secretory protein; β-Microseminoprotein; PSP94; Seminal plasma; Prostate cancer; Protein complex; SCP-domain; Mass spectrometry; Surface plasmon resonance Human cysteine-rich secretory protein 3 (CRISP-3; also known as SGP28) was first isolated from neutrophilic granulocytes, but it is also a constituent of blood plasma and exocrine secretions, such as saliva and seminal plasma [1]. It belongs to a family of CRISPs found in mammals and reptiles, which is characterized by 16 highly conserved cysteine residues of a total of 220-230 amino acids and 35-85% identity in the primary structure [2][3][4]. Recently, the crystal structure of a snake venom CRISP was elucidated [5]. This confirmed the previously proposed two-domain structure of CRISPs with a large N-terminal SCP domain (after sperm coating protein, an alternative name for murine CRISP-1) and a smaller, compact C-terminal domain, separated by a hinge-region [3,5].A novel protein with an N-terminal SCP domain has been identified in human blood plasma and is called PSP94-binding protein (PSPBP) as it binds to β -microseminoprotein (MSP), also known as prostate secretory protein of 94 amino acids (PSP94) [6]. MSP is one of the three predominant proteins secreted by the prostate gland, but it is also present in other body fluids, e.g., tracheobronchial fluid. In general, MSP-synthesis is associated with tissue producing [7,8].It is yet unknown whether MSP binds to PSPBP through the SCP domain or via the large C-terminal part of the molecule [6]. One way to answer this question is to investigate whether MSP binds other proteins with an SCP domain, and the abundance of both MSP and CRISP-3 in human seminal plasma prompted us to test the hypothesis that these proteins form high-affinity complexes. Materials and methods MaterialsHuman MSP was purified from seminal plasma with the method described for the purification of pig MSP [9]. Human CRISP-3 was purified from granulocytes [10]. Specific antisera were raised in rabbits against recombinant C-terminally truncated human CRISP-3 and native human MSP [1,11]. Semen was collected from healthy volunteers and allowed to liquefy for 1 h at room temperature (RT), followed by centrifugation to remove spermatozoa and was subsequently stored at −20 °C until use. Gel filtrationProteins were separated according to their molecular size by gel filtration on a Su...

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Molecular cloning of a small prostate protein, known as β-microsemenoprotein, PSP94 or β-inhibin, and demonstration of transcripts in non-genital tissues

Cited by 62 publications

References 24 publications

Identification of Lipocalin and Apolipoprotein A1 as Biomarkers of Chronic Obstructive Pulmonary Disease

Identification of Lipocalin and Apolipoprotein A1 as Biomarkers of Chronic Obstructive Pulmonary Disease

Les proteines majeures de la secretion prostatique

β-Microseminoprotein binds CRISP-3 in human seminal plasma

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