| Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. | |
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MedLine Citation:
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PMID: 10490978 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Galectin-1 induces apoptosis of human thymocytes and activated T cells by an unknown mechanism. Apoptosis is a novel function for a mammalian lectin; moreover, given the ubiquitous distribution of the oligosaccharide ligand recognized by galectin-1, it is not clear how susceptibility to and signaling by galectin-1 is regulated. We have determined that galectin-1 binds to a restricted set of T cell surface glycoproteins, and that only CD45, CD43, and CD7 appear to directly participate in galectin-1-induced apoptosis. To determine whether these specific glycoproteins interact cooperatively or independently to deliver the galectin-1 death signal, we examined the cell surface localization of CD45, CD43, CD7, and CD3 after galectin-1 binding to human T cell lines and human thymocytes. We found that galectin-1 binding resulted in a dramatic redistribution of these glycoproteins into segregated membrane microdomains on the cell surface. CD45 and CD3 colocalized on large islands on apoptotic blebs protruding from the cell surface. These islands also included externalized phosphatidylserine. In addition, the exposure of phosphatidylserine on the surface of galectin-1-treated cells occurred very rapidly. CD7 and CD43 colocalized in small patches away from the membrane blebs, which excluded externalized phosphatidylserine. Receptor segregation was not seen on cells that did not die in response to galectin-1, including mature thymocytes, suggesting that spatial redistribution of receptors into specific microdomains is required for triggering apoptosis. |
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Authors:
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K E Pace; C Lee; P L Stewart; L G Baum |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of immunology (Baltimore, Md. : 1950) Volume: 163 ISSN: 0022-1767 ISO Abbreviation: J. Immunol. Publication Date: 1999 Oct |
Date Detail:
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Created Date: 1999-10-21 Completed Date: 1999-10-21 Revised Date: 2011-09-07 |
Medline Journal Info:
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Nlm Unique ID: 2985117R Medline TA: J Immunol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 3801-11 Citation Subset: AIM; IM |
Affiliation:
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Department of Pathology, University of California, Los Angeles, School of Medicine 90095, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Antigens, CD* Antigens, CD43 Antigens, CD45 / metabolism Antigens, CD7 / metabolism Apoptosis / immunology* Cell Line, Transformed Cell Membrane / chemistry, metabolism Galectin 1 Hemagglutinins / metabolism, physiology* Humans Membrane Glycoproteins / isolation & purification, metabolism Peptide Fragments / chemistry, isolation & purification, metabolism* Phosphatidylserines / metabolism Protein Binding / immunology Protein Structure, Tertiary Receptor Aggregation / immunology Receptors, Antigen, T-Cell / chemistry, metabolism* Sialoglycoproteins / metabolism Signal Transduction / immunology T-Lymphocytes / cytology*, metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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AI07126-20/AI/NIAID NIH HHS; AI40118/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antigens, CD; 0/Antigens, CD43; 0/Antigens, CD7; 0/Galectin 1; 0/Hemagglutinins; 0/Membrane Glycoproteins; 0/Peptide Fragments; 0/Phosphatidylserines; 0/Receptors, Antigen, T-Cell; 0/Sialoglycoproteins; 0/UN1 sialoglycoprotein, human; EC 3.1.3.48/Antigens, CD45 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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