Human Seminal Plasma Antibody‐Binding Proteins

Chiu, Will Wei-Cheng; Chamley, Larry

doi:10.1034/j.1600-0897.2003.00067.x

Cited by 15 publications

(11 citation statements)

References 54 publications

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“…In another study, Mirels et al [24] demonstrated that abundance of PIP in mucosal-type tissues, as well as in saliva, tears, submucosal glands of the bronchi and apocrine glands of the skin, indicates that PIP may play an important role in mucosal immunity. The potent binding ability of PIP for IgG further suggests its role as an immunomodulatory protein [29,30].…”

Section: Immune Regulationmentioning

confidence: 96%

“…Binding affinity of PIP with IgG and its associated functions have been well documented [29,30,34,72,76]. It was found that PIP binds to IgG via its Fc fragment.…”

Section: Pip Binding Proteinsmentioning

confidence: 98%

“…ASA is an IgG and nature has provided PIP in seminal fluid to counter the detrimental effects of ASA by binding and neutralization. This mechanism of action of PIP has been extensively studied [29,30,72,76,77]. Among the major constituents of human seminal fluid, fibronectin is one [66] and it acts as a substrate for PIP [64].…”

Section: Fertilizationmentioning

confidence: 99%

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Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications

Hassan

Waheed

Yadav

et al. 2008

Cell. Mol. Life Sci.

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Prolactin inducible protein (PIP) is a 17- kDa single polypeptide chain, known by various names due to its versatile nature and function in human reproductive and immunological systems. It is expressed in several exocrine tissues such as the lacrimal, salivary, and sweat glands. Its expression is up regulated by prolactin and androgens, and estrogens down regulate it. Due to its over-expression in metastatic breast and prostate cancer, presently PIP is considered as a prognostic biomarker. Moreover, its aspartyl-proteinase nature suggests its role in tumor progression. PIP has unique features because it is small in size and plays multiple important functions. Its ability to bind potentially with CD4-T cell receptor, immunoglobulin G (IgG), actin, zinc alpha2-glycoprotein (ZAG), fibronectin and enamel pellicle, reveals its important biological functions. This is the first comprehensive review on the structure and functional analysis of PIP and its clinical applications.

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Section: Immune Regulationmentioning

confidence: 96%

“…Binding affinity of PIP with IgG and its associated functions have been well documented [29,30,34,72,76]. It was found that PIP binds to IgG via its Fc fragment.…”

Section: Pip Binding Proteinsmentioning

confidence: 98%

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Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications

Hassan

Waheed

Yadav

et al. 2008

Cell. Mol. Life Sci.

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“…This protein is also recognized with various alternative names including gross cystic disease fluid protein 15, secretory actin-binding protein and gp17 due to its functional aspects in human reproductive and immunological systems [2]. PIP binds to many proteins, such as fibrinogen, actin, keratin, myosin, tropomyosin [3], immunoglobulin G [4], and human zinc-alpha-2 glycoprotein [5]. The ability of PIP to bind IgG-Fc suggests that it may have an immunomodulatory role.…”

Section: Introductionmentioning

confidence: 99%

Human serum albumin as a new interacting partner of prolactin inducible protein in human seminal plasma

Kumar

Tomar

Singh

et al. 2012

International Journal of Biological Macromolecules

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“…To mitigate such effects, at least in humans, seminal plasma contains IgGBP, which bind IgGs via the Fc fragment and prevent them from reaching the sperm (Chiu & Chamley 2003). To the best of our knowledge, this is the first report of IgGBP in the seminal plasma of either domestic or wild animals.…”

Section: Proteins Associated With Protection Of Sperm Integrity and Fmentioning

confidence: 84%

Protein profile of the seminal plasma of collared peccaries (Pecari tajacu Linnaeus, 1758)

Santos¹,

Sousa²,

Martins³

et al. 2014

Reproduction

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This study was conducted to characterize the major proteins of the peccary seminal plasma, based on the semen samples collected from nine adult and reproductively sound animals. Our approach included the use of two-dimensional electrophoresis followed by Coomassie blue staining and analysis of polypeptide maps with PDQuest Software (Bio-Rad). Proteins were identified by tandem mass spectrometry (LC-MS/MS). We detected 179 protein spots per gel and 98 spots were identified by mass spectrometry, corresponding to 23 different proteins. The combined intensity of those spots accounted for 56.2G6% of the intensities of all spots and 60.9% of the intensities of spots presented in every protein map. Protein spots identified as clusterin represented 19.7G8.3% of the integrated optical densities of all spots detected in the seminal plasma maps. There was a negative association (rZK0.87; P!0.05) between the intensity of a clusterin spot and the percentage of sperm with functional membrane. Spermadhesin porcine seminal plasma protein 1 and bodhesin 2 comprised 5.4G1.9 and 8.8G3.9% of the total intensity of all spots respectively. Many proteins appeared in a polymorphic pattern, such as clusterin (27 spots), epididymal secretory glutathione peroxidase (ten spots), inter-a-trypsin inhibitor (12 spots), and IgG-binding protein (ten spots), among others. In conclusion, we presently describe the major seminal plasma proteome of the peccary, which exhibits a distinct high expression of clusterin isoforms. Knowledge of wild species reproductive biology is crucial for an understanding of their survival strategies and adaptation in a changing environment.

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Human Seminal Plasma Antibody‐Binding Proteins

Abstract: Human seminal plasma contains proteins that can bind antibodies. However, to date our knowledge of these proteins especially, whether they have a physiological role in either the male and female reproductive tracts is limited.

Cited by 15 publications

References 54 publications

Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications

Prolactin inducible protein in cancer, fertility and immunoregulation: structure, function and its clinical implications

Human serum albumin as a new interacting partner of prolactin inducible protein in human seminal plasma

Protein profile of the seminal plasma of collared peccaries (Pecari tajacu Linnaeus, 1758)

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