Journal article
Zinc ions and alkaline PH alter the phosphorylated state of proteins 3 and 4.2 in human erythrocyte membranes
Thrombosis research, v 66(6), pp 637-647
1992
PMID: 1519224
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The phosphorylation patterns of isolated red blood cell (RBC) membranes labeled with [ γ-
32p]ATP are altered by Zn
++ ions. Zn
++ ions caused an increased phosphate incorporation into a 72 KDa protein and several proteins in the 40–60 KDa region and a decrease in the labeling of a 53 KDa protein. The 72 KDa and 53 KDa proteins have been identified as protein 4.2 and a protease-cleaved fragment of protein 3, respectively. Evidence suggests that the changes in phosphorylation pattern may be due to the stimulation of endogenous membrane alkaline phosphatase(s). Our results suggest that Zn
++, at physiological concentrations in the intact erythrocyte, could modulate the phosphorylation of selected proteins which may regulate their association in the cytoskeletal network.
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Details
- Title
- Zinc ions and alkaline PH alter the phosphorylated state of proteins 3 and 4.2 in human erythrocyte membranes
- Creators
- Richard L. Fennell - Hahnemann University HospitalGerald Soslau - Hahnemann University Hospital
- Publication Details
- Thrombosis research, v 66(6), pp 637-647
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1992JF90500003
- Scopus ID
- 2-s2.0-0026664112
- Other Identifier
- 991019184089904721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Hematology
- Peripheral Vascular Disease