دورية أكاديمية

Wheat germ agglutinin but not concanavalin A modulates protein kinase C-mediated phosphorylation of red cell skeletal proteins.

التفاصيل البيبلوغرافية
العنوان: Wheat germ agglutinin but not concanavalin A modulates protein kinase C-mediated phosphorylation of red cell skeletal proteins.
المؤلفون: Danilov YN; Department of Biomedical Research, St. Elizabeth's Hospital, Boston, MA 02135., Cohen CM
المصدر: FEBS letters [FEBS Lett] 1989 Nov 06; Vol. 257 (2), pp. 431-4.
نوع المنشور: Journal Article; Research Support, U.S. Gov't, P.H.S.
اللغة: English
بيانات الدورية: Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print Cited Medium: Print ISSN: 0014-5793 (Print) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE
أسماء مطبوعة: Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd.
Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies.
مواضيع طبية MeSH: Neuropeptides*, Concanavalin A/*pharmacology , Cytoskeletal Proteins/*blood , Erythrocytes/*metabolism , Membrane Proteins/*metabolism , Protein Kinase C/*blood , Wheat Germ Agglutinins/*pharmacology, Anion Exchange Protein 1, Erythrocyte/metabolism ; Erythrocyte Membrane/metabolism ; Glycophorins/metabolism ; Humans ; In Vitro Techniques ; Phosphorylation ; Tetradecanoylphorbol Acetate/pharmacology
مستخلص: Human red blood cells contain protein kinase C (PKC) which acts exclusively on the membrane skeletal proteins band 4.1, band 4.9 and adducin. PKC activity can be stimulated by the addition of the phorbol ester 12-O-tetradecanoyl phorbol 13-acetate to intact cells. Phosphorylation of band 4.1 by PKC in vitro results in a dramatic reduction in band 4.1 binding to spectrin and actin, as well as to the cytoplasmic domain of band 3. Here we show that the lectin wheat germ agglutinin (WGA), which binds to the extracellular domain of glycophorin results in the inhibition of PKC catalyzed phosphorylation of band 4.1, band 4.9 and likely adducin as well. The lectin concanavalin A, which binds to band 3 was without effect. Our results suggest that the binding of WGA to glycophorin results in a major rearrangement of the membrane skeletal network which correlates with reduced phosphorylation of membrane skeletal proteins by PKC.
معلومات مُعتمدة: HL 24382 United States HL NHLBI NIH HHS; HL 37462 United States HL NHLBI NIH HHS
المشرفين على المادة: 0 (Anion Exchange Protein 1, Erythrocyte)
0 (Cytoskeletal Proteins)
0 (Glycophorins)
0 (Membrane Proteins)
0 (Neuropeptides)
0 (Wheat Germ Agglutinins)
0 (erythrocyte membrane band 4.1 protein)
0 (erythrocyte membrane protein band 4.1-like 1)
11028-71-0 (Concanavalin A)
EC 2.7.11.13 (Protein Kinase C)
NI40JAQ945 (Tetradecanoylphorbol Acetate)
تواريخ الأحداث: Date Created: 19891106 Date Completed: 19900108 Latest Revision: 20191210
رمز التحديث: 20221208
DOI: 10.1016/0014-5793(89)81589-3
PMID: 2583288
قاعدة البيانات: MEDLINE
الوصف
تدمد:0014-5793
DOI:10.1016/0014-5793(89)81589-3