Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/12561
Title: Ischaemia causes externalization of endothelin-1 binding sites in rat cardiac membranes.
Authors: Liu, J J;Casley, David J;Nayler, W G
Affiliation: Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg, Victoria, Australia
Issue Date: 15-Nov-1989
Citation: Biochemical and Biophysical Research Communications; 164(3): 1220-5
Abstract: Specific, high affinity binding sites for iodinated endothelin-1 ([125I]-ET-1) were identified in crude plasma and light membrane fractions harvested from aerobically perfused and ischaemic rat hearts, to determine whether the ischaemia-induced increase in binding site density (Bmax) involves externalization of the sites. In crude plasma membranes Bmax increased after 60 min ischaemia, from 113.5 +/- 2.15 to 180.6 +/- 4.67 fmol/mg protein (p less than 0.01). In the light membranes, the Bmax fell, from 94.7 +/- 8.70 to 63.80 +/- 6.26 fmol/mg protein (p less than 0.05). Hill coefficients and selectivity of both membrane fractions were unchanged. These results are interpreted as meaning that ischaemia causes externalization of cardiac [125I]-ET-1 binding sites.
Internal ID Number: 2556121
URI: http://ahro.austin.org.au/austinjspui/handle/1/12561
URL: http://www.ncbi.nlm.nih.gov/pubmed/2556121
Type: Journal Article
Subjects: Aerobiosis
Anaerobiosis
Animals
Binding, Competitive
Cell Fractionation
Cell Membrane.metabolism
Coronary Disease.metabolism
Endothelins
Endothelium, Vascular
Female
Kinetics
Male
Myocardium.metabolism
Peptides.metabolism
Rats
Rats, Inbred Strains
Receptors, Cell Surface.metabolism
Receptors, Endothelin
Ultracentrifugation
Appears in Collections:Journal articles

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