Crystal Structure of the Novel Complex Formed between Zinc α2-Glycoprotein (ZAG) and Prolactin-Inducible Protein (PIP) from Human Seminal Plasma

Hassan, Md. Imtaiyaz; Bilgrami, S.; Kumar, Vijay; Singh, Nagendra; Yadav, Savita; Kaur, Punit; Singh, T.P.

doi:10.1016/j.jmb.2008.09.072

Cited by 63 publications

(42 citation statements)

References 55 publications

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“…Isoforms of ZAG along with PAP and PIP were also found to be assembled, making a large PPI network in this MPC. The native ZAG-PIP complex is already reported in our previous work [38,39]; PSA is also reported to form complexes individually with other seminal plasma proteins [40,41]. PIP is an aspartyl protease and known to cleave fibronectin.…”

Section: Discussionsupporting

confidence: 53%

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

Yadav

Kumar

Chhikara

et al. 2011

J of Separation Science

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The seminal plasma comprises secretions from various accessory sex glands. During fertilization spermatozoa undergo complex sequences of precisely timed events that are regulated by the activation of different intracellular signaling pathways. The precision and efficacy of these pathways are often influenced by the assembly and interactions of multiprotein complexes, thereby directing the flow of regulatory information. Our knowledge about these protein complexes present in human seminal plasma (HuSP) is limited. Here we report the identification and characterization of a native high molecular weight zinc-binding multiprotein complex from HuSP by utilizing 2-DE followed by MS. Twenty-six proteins representing isoforms and/or fragments of 11 different proteins were found to be assembled in this complex. Prostate-specific antigen, zinc α2-glycoprotein, prostatic acid phosphatase, and prolactin inducible protein were the major proteins of this complex. Dynamic light scattering experiments revealed changes in aggregation pattern accompanied with deviation from physiological pH and in presence of SDS. However, no significant changes were observed in the presence of physiological ligands such as zinc and fructose. The present study will be useful and contribute to guide the future studies performed for elucidation of biological significance of this native complex in HuSP.

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Section: Discussionsupporting

confidence: 53%

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

Yadav

Kumar

Chhikara

et al. 2011

J of Separation Science

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“…Albumin is known to bind a wide variety of ligands including lipids and androgens [18]. PIP structure has a sandwich beta-sheet with many hydrophobic residues [19] and apart from hydrogen bonding hydrophobic interactions might be playing part in the interaction of PIP with HSA. This complex seems to be stable up to 200 mM NaCl concentration (near physiological range) which further suggests that it is natively formed complex of these proteins.…”

Section: Discussionmentioning

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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“…A large number of studies have been documented on structure and function of PIP [2,27,32,47,58,69,70]. Although exact function(s) of PIP is (are) still not known, due to its presence in different body fluids and similarity with proteins of known functions, various possible functions have been proposed.…”

Section: Functions Of Pipmentioning

confidence: 99%

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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Crystal Structure of the Novel Complex Formed between Zinc α2-Glycoprotein (ZAG) and Prolactin-Inducible Protein (PIP) from Human Seminal Plasma

Cited by 63 publications

References 55 publications

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

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

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

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