EP-GP and the Lipocalin VEGh, Two Different Human Salivary 20-kDa Proteins

Schenkels, L. C. P. M.; Veerman, E.C.I.; Amerongen, A. van Nieuw

doi:10.1177/00220345950740090701

Cited by 16 publications

(11 citation statements)

References 47 publications

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“…The r‐gp17/GCDFP‐15 dimers were stable when stored at −80 °C, but gave rise to a form of about 70 kDa in about three weeks when stored at 4 °C, as reported for EP‐GP [19]. To determine whether gp17/GCDFP‐15 was also present as the dimeric form in HSP, samples were submitted to anion‐exchange chromatography (Q‐Fast Flow) before gel filtration onto a Superdex 200 column.…”

Section: Resultsmentioning

confidence: 92%

Biosynthesis and immunobiochemical characterization of gp17/GCDFP‐15

Caputo

Carratore

Ciullo

et al. 1999

European Journal of Biochemistry

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The gp17 factor is a secretory product of human seminal vesicle cells which binds to CD4 and acts as a potent inhibitor of T lymphocyte apoptosis induced by CD4 crosslinking and subsequent T-cell receptor (TCR) activation. The protein is identical to gross cystic disease fluid protein-15 (GCDFP-15), a breast tumor secretory marker PIP (prolactin inducible protein), a prolactin-controlled and androgen-controlled protein; secretory actin binding protein (SABP), a seminal plasma actin binding protein and extra-parotid glycoprotein (EP-GP), a secretory protein from the salivary gland. The structure of this protein has not yet been elucidated and no biological function has been clearly attributed to date. Expression of recombinant gp17/GCDFP-15 cDNA in bacteria and insect cells leads to the production of a misfolded insoluble protein. In this study, we describe the production of gp17/GCDFP-15 in two different eukaryotic systems, namely HeLa cells and the Pichia pastoris yeast. Using constructs in which gp17/GCDFP-15 was tagged with enhanced green fluorescent protein (EGFP) in various combinations, we observed expression only when the fusion protein was directed to the secretory compartment by the correct signal peptide. The resulting fluorescent protein was inefficiently secreted, thus suggesting that gp17/GCDFP-15 is not appropriately post-translationally processed and/or transported in HeLa cells. The use of the P. pastoris secretory pathway allowed instead the accumulation in the culture medium of a GCDFP-15/gp17 species which retained the ability to bind to CD4 and also most of the biochemical and immunological properties of the native protein. The production of an active recombinant molecule opens the way to correlate the structural properties of this peculiar factor to its ability to bind several proteins, including CD4, and to block CD4-mediated T cell programmed death.

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Section: Resultsmentioning

confidence: 92%

Biosynthesis and immunobiochemical characterization of gp17/GCDFP‐15

Caputo

Carratore

Ciullo

et al. 1999

European Journal of Biochemistry

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“…EP‐GP is another example of a protein that originally had been implicated in the formation of the dental pellicle, because of its high affinity for hydroxyapatite (Rathman et al , 1989). Later studies demonstrated that EP‐GP protein is present in several excretory body fluids, including sweat, semen and tears, and is identical to secretory actin binding protein (SABP) and Gross Cystic Disease Fluid Protein (GCDFP‐15) (Schenkels et al , 1994, Schenkels, Veerman and Nieuw Amerongen, 1995a, 1995b; Caputo et al , 1999). The ubiquitous presence in mucosal secretions pointed to a more general protective role for EP‐GP, a concept that was supported by the observation that this protein binds to microorganisms (Schenkels et al , 1997) as well as to the CD4 receptor on monocytes (Autiero et al , 1997; Gaubin et al , 1999).…”

Section: Von Ebner Glands Protein (Vegh) and Secretory Leucocyte Protmentioning

confidence: 99%

Saliva – the defender of the oral cavity

2002

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“…Vol. 66,2009 Review Article tract, ear canal and skin [71], resulting in the inhibition of bacterial growth [24]. Its predominance in mucosaltype tissues, as well as its presence in saliva, tears, submucosal glands of the bronchi and apocrine glands of the skin, suggests that PIP may play an important role in mucosal immunity [24].…”

Section: Inhibition Of Bacterial Growthmentioning

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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EP-GP and the Lipocalin VEGh, Two Different Human Salivary 20-kDa Proteins

Cited by 16 publications

References 47 publications

Biosynthesis and immunobiochemical characterization of gp17/GCDFP‐15

Biosynthesis and immunobiochemical characterization of gp17/GCDFP‐15

Saliva – the defender of the oral cavity

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

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