ArticleHistochemistry and cell biology2006
The platelet receptor for type III collagen (TIIICBP) is present in platelet membrane lipid microdomains (rafts).
Article in Histochemistry and cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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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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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Function of Platelet Glycosphingolipid Microdomains/Lipid Rafts.International journal of molecular sciences · 2020Review
- Characterization of lipid rafts in human platelets using nuclear magnetic resonance: A pilot study.Biochemistry and biophysics reports · 2017Article
- Sphingolipids of human umbilical cord vein and their alteration in preeclampsia.Molecular and cellular biochemistry · 2010Article
- Recent progress in histochemistry.Histochemistry and cell biology · 2007Review
- The histochemistry and cell biology vade mecum: a review of 2005-2006.Histochemistry and cell biology · 2006Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Platelet interactions with collagen are orchestrated by the presence or the migration of platelet receptor(s) for collagen into lipid rafts, which are specialized lipid microdomains from the platelet plasma membrane enriched in signalling proteins. Electron microscopy shows that in resting platelets, TIIICBP, a receptor specific for type III collagen, is present on the platelet membrane and associated with the open canalicular system, and redistributes to the platelet membrane upon platelet activation. After platelet lysis by 1% Triton X-100 and the separation of lipid rafts on a discontinuous sucrose gradient, TIIICBP is recovered in lipid raft-containing fractions and Triton X-100 insoluble fractions enriched in cytoskeleton proteins. Platelet aggregation, induced by type III collagen, was inhibited after disruption of the lipid rafts by cholesterol depletion, whereas platelet adhesion under static conditions did not require lipid raft integrity. These results indicate that TIIICBP, a platelet receptor involved in platelet interaction with type III collagen, is localized within platelet lipid rafts where it could interact with other platelet receptors for collagen (GP VI and alpha2beta1 integrin) for efficient platelet activation.
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Registered trials
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