Publication:
Annexins sense changes in intracellular pH during hypoxia

cris.virtual.author-orcid0000-0002-3517-3871
cris.virtualsource.author-orcid083943e3-ae7a-4391-91d3-91bed86ab50e
cris.virtualsource.author-orcidb9ad9ebc-8304-482a-9dbf-53f48c21a2f7
cris.virtualsource.author-orcidb4c31f46-29ab-4035-a115-1542a94c1d9a
datacite.rightsmetadata.only
dc.contributor.authorMonastyrskaya, Katia
dc.contributor.authorTschumi, Fabian
dc.contributor.authorBabiichuk, Eduard
dc.contributor.authorKeogh-Stroka, Deborah M.
dc.contributor.authorDraeger, Annette
dc.date.accessioned2024-10-13T17:32:24Z
dc.date.available2024-10-13T17:32:24Z
dc.date.issued2008
dc.description.abstractThe pH(i) (intracellular pH) is an important physiological parameter which is altered during hypoxia and ischaemia, pathological conditions accompanied by a dramatic decrease in pH(i). Sensors of pH(i) include ion transport systems which control intracellular Ca2+ gradients and link changes in pH(i) to functions as diverse as proliferation and apoptosis. The annexins are a protein family characterized by Ca2+-dependent interactions with cellular membranes. Additionally, in vitro evidence points to the existence of pH-dependent, Ca(2+)-independent membrane association of several annexins. We show that hypoxia promotes the interaction of the recombinant annexin A2-S100A10 (p11) and annexin A6 with the plasma membrane. We have investigated in vivo the influence of the pH(i) on the membrane association of human annexins A1, A2, A4, A5 and A6 tagged with fluorescent proteins, and characterized this interaction for endogenous annexins present in smooth muscle and HEK (human embryonic kidney)-293 cells biochemically and by immunofluorescence microscopy. Our results show that annexin A6 and the heterotetramer A2-S100A10 (but not annexins A1, A4 and A5) interact independently of Ca2+ with the plasma membrane at pH 6.2 and 6.6. The dimerization of annexin A2 within the annexin A2-S100A10 complex is essential for the pH-dependent membrane interaction at this pH range. The pH-induced membrane binding of annexins A6 and A2-S100A10 might have consequences for their functions as membrane organizers and channel modulators.
dc.description.numberOfPages11
dc.description.sponsorshipInstitut für Anatomie, Zellbiologie
dc.description.sponsorshipUniversitätsklinik für Viszerale Chirurgie und Medizin, Viszeral- und Transplantationschirurgie
dc.description.sponsorshipInstitut für Anatomie
dc.identifier.isi000252414300006
dc.identifier.pmid17824845
dc.identifier.publisherDOI10.1042/BJ20071116
dc.identifier.urihttps://boris-portal.unibe.ch/handle/20.500.12422/97162
dc.language.isoen
dc.publisherPortland Press
dc.publisher.placeLondon
dc.relation.isbn17824845
dc.relation.ispartofBiochemical journal
dc.relation.issn0264-6021
dc.relation.organizationDCD5A442BD6DE17DE0405C82790C4DE2
dc.relation.organizationDCD5A442C059E17DE0405C82790C4DE2
dc.relation.organizationDCD5A442BCD7E17DE0405C82790C4DE2
dc.titleAnnexins sense changes in intracellular pH during hypoxia
dc.typearticle
dspace.entity.typePublication
oaire.citation.endPage75
oaire.citation.issue1
oaire.citation.startPage65
oaire.citation.volume409
oairecerif.author.affiliationInstitut für Anatomie, Zellbiologie
oairecerif.author.affiliationUniversitätsklinik für Viszerale Chirurgie und Medizin, Viszeral- und Transplantationschirurgie
oairecerif.author.affiliationInstitut für Anatomie
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.contributor.rolecreator
unibe.description.ispublishedpub
unibe.eprints.legacyId23522
unibe.journal.abbrevTitleBIOCHEM J
unibe.subtype.articlejournal

Files

Collections