Novel purification method for mammalian seminal plasma phospholipid-binding proteins reveals the presence of a novel member of this family of protein in stallion seminal fluid

2003 ◽  
Vol 66 (4) ◽  
pp. 349-357 ◽  
Author(s):  
Martin Ménard ◽  
Veronica Nauc ◽  
Claude Lazure ◽  
Denis Vaillancourt ◽  
Puttaswamy Manjunath
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Seminal Fluid ◽  
Plasma Phospholipid ◽  
Purification Method ◽  
Phospholipid Binding

Purification of four gelatin-binding proteins from bovine seminal plasma by affinity chromatography

1987 ◽  
Vol 7 (3) ◽  
pp. 231-238 ◽  
Author(s):  
P. Manjunath ◽  
M. R. Sairam ◽  
J. Uma
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Apparent Molecular Weight ◽  
Single Step ◽  
High Yield ◽  
Property A ◽  
Purification Method ◽  
Elution Pattern

Bovine seminal plasma contains three similar acidic proteins, which we have previously designated as BSP-A1, BSP-A2, and BSP-A3. These proteins contain two homologous domains that are similar to type II structures present in the gelatin-binding domain of fibronectin. The present data have revealed that these proteins, like fibronectin, also form complexes with gelatin, a denatured collagen. Based on this property, a single step affinity purification method has been developed. In addition to these three proteins BSP-A1, −A2 and −A3, another protein with an apparent molecular weight of 30,000 dalton (named BSP-30-kDa) also bound to the gelatin-agarose column. Elution of these proteins from affinity columns using a linear gradient of either urea or arginine gave essentially the same pattern with a high yield of 90–95%. The purified proteins were homogeneous by SDS-polyacrylamide gel electrophoresis, amino acid composition and HPLC. Chromatography of bull seminal vesicular fluid also exhibited an elution pattern similar to that obtained for bull seminal plasma. The availability of these purified proteins should aid in understanding the physiology of these gelatin-binding proteins.

Human Epididymis Protein 4 Quantification and Interaction Network Analysis in Seminal Plasma

2019 ◽  
Vol 26 (6) ◽  
pp. 458-465
Author(s):  
Krishna Kant ◽  
Anil K. Tomar ◽  
Pankaj Sharma ◽  
Bishwajit Kundu ◽  
Sarman Singh ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Interaction Network ◽  
Prostatic Acid Phosphatase ◽  
Regulatory Subunit ◽  
Plasma Samples ◽  
Human Seminal Plasma ◽  
Human Epididymis Protein 4 ◽  
Human Epididymis ◽  
Core Proteins

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.

scholarly journals A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin family.

1992 ◽  
Vol 267 (13) ◽  
pp. 8919-8924
Author(s):  
H Tokumitsu ◽  
A Mizutani ◽  
H Minami ◽  
R Kobayashi ◽  
H Hidaka
Keyword(s):  
Binding Proteins ◽  
Phospholipid Binding

Cutaneous manifestations of antiphospholipid syndrome

Lupus ◽  
2021 ◽  
pp. 096120332199010
Author(s):  
Minerva Gomez-Flores ◽  
Genesis Herrera-Argaez ◽  
Osvaldo Vazquez-Martinez ◽  
Maira Herz-Ruelas ◽  
Jorge Ocampo-Candiani ◽  
...  
Keyword(s):  
Antiphospholipid Syndrome ◽  
Binding Proteins ◽  
Cutaneous Manifestations ◽  
Phospholipid Binding

Antiphospholipid syndrome (APS) is an acquired thrombophilic disorder in which autoantibodies are produced against a variety of phospholipids and phospholipid-binding proteins. The purpose of this article is to review cutaneous findings in patients with APS diagnosis. An overview regarding prevalence, description, pathogenesis and histopathology, are described for cutaneous manifestations of APS.

scholarly journals Proteins of the canine seminal plasma

2016 ◽  
Vol 46 (5) ◽  
pp. 901-908 ◽  
Author(s):  
Annice Aquino-Cortez ◽  
Lúcia Daniel Machado da Silva ◽  
Airton Alencar de Araújo ◽  
Erika da Silva Bezerra de Menezes ◽  
Arlindo de Alencar Araripe Noronha Moura
Keyword(s):  
Alkaline Phosphatase ◽  
Seminal Plasma ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Sperm Quality ◽  
Zinc Binding ◽  
Heparin Binding ◽  
Reproductive Disorders ◽  
The Matrix ◽  
Peroxidase Enzymes

ABSTRACT: Studies have been performed to identify the proteins present in canine seminal plasma (SP) and relate them to sperm quality as well as to discover molecular markers of reproductive tract diseases. There is evidence that heparin-binding proteins, zinc-binding proteins, and lactoferrin as well as the matrix metalloproteinase, superoxide dismutase, catalase, and glutathione peroxidase enzymes are associated with canine sperm quality. Other studies indicate that prolactin and enzymes like arginine esterase, acid phosphatase, and alkaline phosphatase could be successfully used as biomarkers of reproductive disorders. Thus, the present literature review aims to address aspects related to proteins of the canine SP, their influence on fertility, and their importance as biomarkers of reproductive disorders.

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