Linked Life Data

8858095

Source:http://linkedlifedata.com/resource/pubmed/id/8858095

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-11-25
pubmed:abstractText
Zn2+ has a paradoxical effect on IF1-ATPase interaction in cardiac muscle mitochondria in so-called slow heart-rate mammalian species like rabbit. In such slow heart-rate mammalian species, it completely prevents IF1-mediated ATPase inhibition regardless of pH while concomitantly causing full IF1 binding to the ATPase, again, regardless of pH (Rouslin et al. (1993) J. Bioenerget. Biomembr. 25, 297-306). While our earlier study suggested that there are two kinds of IF1-ATPase interaction, a docking interaction and an ATPase inhibitory interaction with Zn2+ promoting docking and interfering with inhibition, it did not yield information on whether Zn2+ interacted primarily with IF1, with the ATPase, or with both. In the present study we show that, in contrast to its effects in rabbit cardiomyocytes, mitochondria, and SMP in which Zn2+ fully blocked IF1-mediated ATPase inhibition, Zn2+ actually enhanced ATPase inhibition in rat cardiomyocytes, although the extent of this effect was limited by the low level of IF1 in rat cardiomyocytes. Moreover, Zn2+ had no effect on IF1-mediated ATPase inhibition in rat heart mitochondria and, as suggested by inter and intra-species IF1 binding to SMP, the different effects of Zn2+ in rabbit versus those in rat appear to be mediated primarily through the different reactivities of rabbit and rat IF1 to Zn2+.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
227
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8-14
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Novel difference in IF1 reactivity to Zn2+ in rabbit versus rat cardiomyocytes, mitochondria, and submitochondrial particles.
pubmed:affiliation
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0575, USA. william.rouslin@uc.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.