ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society
Expression of Glycoprotein 2 and Its Glycosylation in Human Cowper's Gland.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed.
- Pre-ejaculate - an overlooked body fluid with high amounts of DNA.International journal of legal medicine · 2026Article
- Stem cell-based tactics in the remodeling and treatment of intestinal diseases.Stem cell research & therapy · 2026Review
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Authors and funding
8 authors.
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Abstract
Glycoprotein 2 (GP2), initially identified as a primary membrane protein of zymogen granules in pancreatic acinar cells, is a marker of intestinal microfold cells (M cells) and involved in bacterial transcytosis in M cells. Recent studies have reported GP2 expression in the pancreas and intestine among various other organs. We aimed to elucidate the expression of GP2 and its glycosylation modifications in human Cowper's glands. We generated an anti-human GP2 monoclonal antibody suitable for formalin-fixed, paraffin-embedded tissue sections. This antibody, designated GP2-71, successfully stained both the plasma membrane and cytoplasm of normal pancreatic acinar cells. Subsequently, we performed GP2-71 immunostaining on normal human Cowper's gland tissues. Our findings revealed that the luminal cell membrane and contents of the Cowper's glands reacted strongly with GP2-71. Moreover, the regions stained with GP2-71 were partially immunostained with the anti-sialyl Lewis x (sLe
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