دورية أكاديمية

Novel difference in IF1 reactivity to Zn2+ in rabbit versus rat cardiomyocytes, mitochondria, and submitochondrial particles.

التفاصيل البيبلوغرافية
العنوان: Novel difference in IF1 reactivity to Zn2+ in rabbit versus rat cardiomyocytes, mitochondria, and submitochondrial particles.
المؤلفون: Rouslin W; Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Ohio 45267-0575, USA. william.rouslin@uc.edu, Broge CW
المصدر: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1996 Oct 03; Vol. 227 (1), pp. 8-14.
نوع المنشور: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print Cited Medium: Print ISSN: 0006-291X (Print) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE
أسماء مطبوعة: Publication: <2002- >: San Diego, CA : Elsevier
Original Publication: New York, Academic Press.
مواضيع طبية MeSH: Enzyme Inhibitors*/metabolism, Mitochondria, Heart/*drug effects , Myocardium/*metabolism , Proteins/*drug effects , Proton-Translocating ATPases/*antagonists & inhibitors , Submitochondrial Particles/*drug effects , Zinc/*pharmacology, Animals ; Male ; Mitochondria, Heart/enzymology ; Mitochondria, Heart/metabolism ; Myocardium/cytology ; Myocardium/enzymology ; Proteins/metabolism ; Rabbits ; Rats ; Rats, Sprague-Dawley ; Species Specificity ; Submitochondrial Particles/metabolism ; ATPase Inhibitory Protein
مستخلص: 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+.
معلومات مُعتمدة: HL30926 United States HL NHLBI NIH HHS
المشرفين على المادة: 0 (Enzyme Inhibitors)
0 (Proteins)
EC 3.6.3.14 (Proton-Translocating ATPases)
J41CSQ7QDS (Zinc)
تواريخ الأحداث: Date Created: 19961003 Date Completed: 19961125 Latest Revision: 20231213
رمز التحديث: 20240627
DOI: 10.1006/bbrc.1996.1459
PMID: 8858095
قاعدة البيانات: MEDLINE
الوصف
تدمد:0006-291X
DOI:10.1006/bbrc.1996.1459