Immunoreactive protein to rat estramustine binding protein in human seminal plasma: its relationship to prostatic acid phosphatase and zinc

Background: A well-known tissue marker of ovarian cancer, Human Epididymis protein 4 (HE4) is the member of whey acidic four-disulfide core proteins family. Purified from human seminal plasma and characterized as a cross-class protease inhibitor, HE4 was proposed to shield spermatozoa against proteolytic factors. However, its exact biological function is unknown. Proteins usually function in conjunction with other proteins in the system and thus, identification and analysis of protein networks become essential to decode protein functions. Objective: This study was performed to explore possible role(s) of HE4 in reproductive physiology via identification of its interactome in human seminal plasma. Methods: HE4 binding proteins were identified through co-immunoprecipitation and MALDITOF/ MS analysis. Also, HE4 was quantified by ELISA in fertile and infertile human seminal plasma samples. Results: Ten HE4 binding proteins were identified, viz. protein phosphatase 1 regulatory subunit 21, protein kinase CLK3, Ankyrin repeat domain-containing protein36A, prostatic acid phosphatase, KIF5C, Spectrin repeat containing, nuclear envelope 1, isoform CRAf, tropomyosin 4, vezatin, utrophin and fibronectin1. This interaction network suggests that HE4 plays multiple roles, specifically in capacitation, sperm motility and maturation. Further, HE4 concentration in human seminal plasma samples was determined by Elisa. Higher HE4 expression in normozoospermia compared to azoospermia and asthenozoospermia affirms its importance in fertilization. Conclusion: Based on identified interactome, it is plausible that HE4 plays a crucial role in fertilization, specifically in sperm maturation, motility and capacitation.

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Simple, rapid determination of zinc and acid phosphatase in seminal plasma with an ABA-100 bichromatic analyzer.

Clinical Chemistry ◽

10.1093/clinchem/34.8.1605 ◽

1988 ◽

Vol 34 (8) ◽

pp. 1605-1607 ◽

Cited By ~ 11

Author(s):

M Gavella

Keyword(s):

Acid Phosphatase ◽

Male Infertility ◽

Seminal Plasma ◽

Rapid Determination ◽

Assay System ◽

Human Seminal Plasma ◽

Automated Assay ◽

Sensitivity Specificity

Abstract I describe an automated assay for zinc and acid phosphatase in seminal plasma. These, which are markers of the function of the prostate, were assayed bichromatically with an Abbott ABA-100 analyzer. As many as 25 samples of human seminal plasma can be analyzed sequentially with CVs of 3.1% for zinc and 1.5% for acid phosphatase. The sensitivity, specificity, and speed of this assay system make it practicable for use in investigation of male infertility.

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Isolation and Identification of Concanavalin A Binding Glycoproteins from Human Seminal Plasma: A Step Towards Identification of Male Infertility Marker Proteins

Disease Markers ◽

10.1155/2011/798072 ◽

2011 ◽

Vol 31 (6) ◽

pp. 379-386 ◽

Cited By ~ 11

Author(s):

Anil Kumar Tomar ◽

Balwinder Singh Sooch ◽

Isha Raj ◽

Sarman Singh ◽

Tej P. Singh ◽

...

Keyword(s):

Male Infertility ◽

Seminal Plasma ◽

Concanavalin A ◽

Specific Antigen ◽

Clinical Importance ◽

Prostatic Acid Phosphatase ◽

Human Seminal Plasma ◽

Isolation And Identification ◽

Altered Expression ◽

Marker Proteins

Human seminal plasma contains a large array of proteins of clinical importance which are essentially needed to maintain the reproductive physiology of spermatozoa and for successful fertilization. Thus, isolation and identification of seminal plasma proteins is of paramount significance for their biophysical characterization and functional analysis in reproductive physiological processes. In this study, we have isolated Concanavalin-A binding glycoproteins from human seminal plasma and subsequently identified them by MALDI-TOF/MS analysis. The major proteins, as identified in this study, are Aminopeptidase N, lactoferrin, prostatic acid phosphatase, zinc-alpha-2-glycoprotein, prostate specific antigen, progestagen-associated endometrial protein, Izumo sperm-egg fusion protein and prolactin inducible protein. This paper also reports preliminary studies to identify altered expression of these proteins in oligospermia and azoospermia in comparison to normospermia. In oligospermia, five proteins were found to be downregulated while in azoospermia, four proteins were downregulated and two proteins were upregulated. Thus, this study is of immense biomedical interest towards identification of potential male infertility marker proteins in seminal plasma.

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