ArticleHistochemistry1989
Localization of a putative cell adhesion molecule (gp110) in Wistar and Fischer rat tissues.
Article in Histochemistry, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 16 citations in OpenAlex.
- N-glycosylation of the carcinoembryonic antigen related cell adhesion molecule, C-CAM, from rat liver: detection of oversialylated bi- and triantennary structures.Glycobiology · 1999Article
- Distribution and quantification of alpha 1-integrin subunit in rat organs.The Histochemical journal · 1995Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A plasma membrane glycoprotein (gp110) involved in cellular adhesion was studied in Wistar and Fischer rats. For quantitative analysis of the gp110 molecule a sandwich-ELISA was used. High quantities of gp110 were found especially in the liver, small intestine, submandibular gland and lung. The distribution and localization of the gp110 were investigated by immunohistochemistry utilizing soluble complexes of alkaline phosphatase and monoclonal anti-alkaline phosphatase antibodies. Immunoreactivity was present in plasma membranes of vascular endothelial cells of some organs. Furthermore, immunostaining also occurred in plasma membranes of lymphocytes, exocrine gland cells, excretory duct cells, hepatocytes, epithelial cells of the small intestine, kidney and vesicular gland and in the cytoplasm of renal connecting and collecting duct cells. The localization of gp110 in the luminal domain of the plasma membrane at many sites suggests that this glycoprotein is also involved in processes distinct from cell adhesion.
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