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A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically

BACKGROUND: CD147 is a broadly distributed integral membrane glycoprotein with two Ig-like domains implicated in a wide range of functions. It is associated at the cell surface with the monocarboxylate transporters MCT1 and 4 but interactions of the extracellular region have not been characterised....

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Autores principales: Hanna, S Melanie, Kirk, Peter, Holt, Oliver J, Puklavec, Michael J, Brown, Marion H, Barclay, A Neil
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC280649/
https://www.ncbi.nlm.nih.gov/pubmed/14606962
http://dx.doi.org/10.1186/1471-2091-4-17
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author Hanna, S Melanie
Kirk, Peter
Holt, Oliver J
Puklavec, Michael J
Brown, Marion H
Barclay, A Neil
author_facet Hanna, S Melanie
Kirk, Peter
Holt, Oliver J
Puklavec, Michael J
Brown, Marion H
Barclay, A Neil
author_sort Hanna, S Melanie
collection PubMed
description BACKGROUND: CD147 is a broadly distributed integral membrane glycoprotein with two Ig-like domains implicated in a wide range of functions. It is associated at the cell surface with the monocarboxylate transporters MCT1 and 4 but interactions of the extracellular region have not been characterised. RESULTS: We report the characterisation of a form of CD147 with an additional membrane-distal Ig-like domain. In contrast to the two domain form, this three domain form of CD147 interacts homophilically. Surface plasmon resonance analysis using recombinant proteins showed that the interaction was of low affinity (K(D )~ 40 μM) and this is typical of many interactions between membrane proteins. cDNA for the 3 domain form are rare but have been identified in human and mouse retina. CONCLUSION: The finding that the three domain form of CD147 has an extracellular ligand, that is it interacts homophilically, suggests this interaction may be important in aligning lactate transporters in the retina where lactate is an important metabolite.
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spelling pubmed-2806492003-11-29 A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically Hanna, S Melanie Kirk, Peter Holt, Oliver J Puklavec, Michael J Brown, Marion H Barclay, A Neil BMC Biochem Research Article BACKGROUND: CD147 is a broadly distributed integral membrane glycoprotein with two Ig-like domains implicated in a wide range of functions. It is associated at the cell surface with the monocarboxylate transporters MCT1 and 4 but interactions of the extracellular region have not been characterised. RESULTS: We report the characterisation of a form of CD147 with an additional membrane-distal Ig-like domain. In contrast to the two domain form, this three domain form of CD147 interacts homophilically. Surface plasmon resonance analysis using recombinant proteins showed that the interaction was of low affinity (K(D )~ 40 μM) and this is typical of many interactions between membrane proteins. cDNA for the 3 domain form are rare but have been identified in human and mouse retina. CONCLUSION: The finding that the three domain form of CD147 has an extracellular ligand, that is it interacts homophilically, suggests this interaction may be important in aligning lactate transporters in the retina where lactate is an important metabolite. BioMed Central 2003-11-07 /pmc/articles/PMC280649/ /pubmed/14606962 http://dx.doi.org/10.1186/1471-2091-4-17 Text en Copyright © 2003 Hanna et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Hanna, S Melanie
Kirk, Peter
Holt, Oliver J
Puklavec, Michael J
Brown, Marion H
Barclay, A Neil
A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title_full A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title_fullStr A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title_full_unstemmed A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title_short A novel form of the membrane protein CD147 that contains an extra Ig-like domain and interacts homophilically
title_sort novel form of the membrane protein cd147 that contains an extra ig-like domain and interacts homophilically
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC280649/
https://www.ncbi.nlm.nih.gov/pubmed/14606962
http://dx.doi.org/10.1186/1471-2091-4-17
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