دورية أكاديمية
Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C.
| العنوان: | Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C. |
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| المؤلفون: | Danilov YN; Department of Biomedical Research, St. Elizabeth's Hospital, Boston, Massachusetts 02135., Fennell R, Ling E, Cohen CM |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 1990 Feb 15; Vol. 265 (5), pp. 2556-62. |
| نوع المنشور: | Journal Article; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Cytoskeletal Proteins* , Neuropeptides*, Erythrocyte Membrane/*metabolism , Membrane Proteins/*metabolism , Protein Kinase C/*metabolism, Electrophoresis, Polyacrylamide Gel ; Humans ; Kinetics ; Membrane Proteins/isolation & purification ; Molecular Weight ; Phosphorylation ; Protein Binding ; Trypsin/pharmacology |
| مستخلص: | We have studied the effects of band 4.1 phosphorylation on its association with red cell inside-out vesicles stripped of all peripheral proteins. Band 4.1 bound to these vesicles in a saturable manner, and binding was characterized by a linear Scatchard plot with an apparent Kd of 1-2 x 10(-7) M. Phosphorylation of band 4.1 by purified protein kinase C reduced its ability to bind to membranes, resulting in a reduction in the apparent binding capacity of the membrane by 60-70% but little or no change in the apparent Kd of binding. By contrast, phosphorylation of band 4.1 by cAMP-dependent kinase had no effect on membrane binding. Digestion of the stripped inside-out vesicles with trypsin cleaved 100% of the cytoplasmic domain of band 3 but had little or no effect on glycophorin. Binding of band 4.1 to these digested vesicles was reduced by 70%. Phosphorylation of band 4.1 by protein kinase C had no effect on its binding to the digested vesicles, suggesting that the cytoplasmic domain of band 3 contained the phosphorylation-sensitive binding sites. This was confirmed by direct measurement of band 4.1 binding to the purified cytoplasmic domain of band 3. Phosphorylation of band 4.1 by protein kinase C reduced its binding to the purified 43-kDa domain by as much as 90%, while phosphorylation by cAMP-dependent kinase was without effect. These results show a selective effect of protein kinase C phosphorylation on the binding of band 4.1 to one of its membrane receptors, band 3, and suggest a mechanism whereby one of the key red cell-skeletal membrane associations may be modulated. |
| معلومات مُعتمدة: | HL 24382 United States HL NHLBI NIH HHS; P01 HL 37462 United States HL NHLBI NIH HHS |
| المشرفين على المادة: | 0 (Cytoskeletal Proteins) 0 (Membrane Proteins) 0 (Neuropeptides) 0 (erythrocyte membrane band 4.1 protein) 0 (erythrocyte membrane protein band 4.1-like 1) EC 2.7.11.13 (Protein Kinase C) EC 3.4.21.4 (Trypsin) |
| تواريخ الأحداث: | Date Created: 19900215 Date Completed: 19900323 Latest Revision: 20210210 |
| رمز التحديث: | 20221213 |
| PMID: | 2303415 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0021-9258 |
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