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Title: | Ischaemia causes externalization of endothelin-1 binding sites in rat cardiac membranes. | Austin 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 | Publication information: | 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. | Gov't Doc #: | 2556121 | URI: | http://ahro.austin.org.au/austinjspui/handle/1/12561 | Journal: | Biochemical and biophysical research communications | URL: | https://pubmed.ncbi.nlm.nih.gov/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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