A 20-kDa Protein in Human Seminal Plasma that is Identical to Gross Cystic Disease Fluid Protein 15 and Prolactin-Inducible Protein

1996 ◽  
Vol 36 (1) ◽  
pp. 29-39 ◽  
Author(s):  
M. Osawa ◽  
Y. Seto ◽  
N. Yukawa ◽  
T. Saito ◽  
S. Takeichi
Immunobiology ◽  
2019 ◽  
Vol 224 (6) ◽  
pp. 811-816
Author(s):  
Chidalu A. Edechi ◽  
Michel R. Nasr ◽  
Algernon Karim ◽  
Anne A. Blanchard ◽  
Cynthia A. Ellison ◽  
...  

2012 ◽  
Vol 50 (2) ◽  
pp. 317-322 ◽  
Author(s):  
Sanjay Kumar ◽  
Anil Kumar Tomar ◽  
Sudhuman Singh ◽  
Mayank Saraswat ◽  
Sarman Singh ◽  
...  

The Breast ◽  
1994 ◽  
Vol 3 (3) ◽  
pp. 141-146
Author(s):  
P.D. Robbins ◽  
E. Hähnel ◽  
G.F. Sterrett ◽  
J. Harvey ◽  
S. Carrello ◽  
...  

1998 ◽  
Vol 46 (9) ◽  
pp. 1061-1071 ◽  
Author(s):  
Lily Mirels ◽  
Arthur R. Hand ◽  
Holly J. Branin

Gross cystic disease fluid protein-15 (GCDFP-15)/prolactin-inducible protein (PIP) is present at moderate levels in human submandibular and sublingual glands and is barely detectable in human parotid gland. The rodent homologue, PIP, has previously been identified in adult submandibular and lacrimal glands. Here we present the molecular characterization of rat PIP and show that this protein is a product of neonatal and adult rat submandibular, sublingual, and parotid glands. cDNA clones encoding rat PIP were isolated and sequenced. The deduced amino acid sequence of rat PIP shows 56% overall identity and 80% similarity with mouse PIP. By SDS-PAGE, secreted rat PIP has an apparent Mr of 17,000, with a minor proportion present as Mr 20–22,000 N-glycosylated forms. PIP was localized in rat salivary glands by immunogold silver staining. PIP was identified in acinar cells of developing and mature submandibular and parotid glands and at very low levels in sublingual gland serous demilunes. Typically, rat submandibular gland secretory proteins are produced by either acinar cell progenitors (Type III cells) or mature acinar cells. The expression pattern observed for PIP is similar to that previously reported for salivary peroxidase, an important component of nonimmune mucosal defense.


PLoS ONE ◽  
2014 ◽  
Vol 9 (11) ◽  
pp. e113310 ◽  
Author(s):  
Shrestha Priyadarsini ◽  
Jesper Hjortdal ◽  
Akhee Sarker-Nag ◽  
Henrik Sejersen ◽  
John M. Asara ◽  
...  

Biomarkers ◽  
2012 ◽  
Vol 17 (6) ◽  
pp. 545-551 ◽  
Author(s):  
Anil Kumar Tomar ◽  
Balwinder Singh Sooch ◽  
Sarman Singh ◽  
Savita Yadav

2021 ◽  
Vol 22 (14) ◽  
pp. 7331
Author(s):  
Justyna Szczykutowicz ◽  
Joanna Tkaczuk-Włach ◽  
Mirosława Ferens-Sieczkowska

In light of recent research, there is increasing evidence showing that extracellular semen components have a significant impact on the immune reaction of the female partner, leading to the tolerogenic response enabling the embryo development and implantation as well as further progress of healthy pregnancy. Seminal plasma glycoproteins are rich in the unique immunomodulatory glycoepitopes that may serve as ligands for endogenous lectins that decorate the surface of immune cells. Such interaction may be involved in modulation of the maternal immune response. Among immunomodulatory glycans, Lewis type antigens have been of interest for at least two decades, while the importance of T/Tn antigens and related structures is still far from understanding. In the current work, we applied two plant lectins capable of distinguishing glycoepitopes with terminal GalNAc and Gal to identify glycoproteins that are their efficient carriers. By means of lectin blotting and lectin affinity chromatography followed by LC-MS, we identified lactotransferrin, prolactin inducible protein as well as fibronectin and semenogelins 1 and 2 as lectin-reactive. Net-O-glycosylation analysis results indicated that the latter three may actually carry T and/or Tn antigens, while in the case of prolactin inducible protein and lactotransferrin LacdiNAc and lactosamine glycoepitopes were more probable. STRING bioinformatics analysis linked the identified glycoproteins in the close network, indicating their involvement in immune (partially innate) processes. Overall, our research revealed potential seminal plasma ligands for endogenous Gal/GalNAc specific lectins with a possible role in modulation of maternal immune response during fertilization.


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