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Titolo:
PROTEIN-KINASE-C AND INSULIN REGULATION OF RED-BLOOD-CELL NA+ H+ EXCHANGE/
Autore:
CEOLOTTO G; CONLIN P; CLARI G; SEMPLICINI A; CANESSA M;
Indirizzi:
HARVARD UNIV,BRIGHAM & WOMENS HOSP,DEPT MED,SCH MED,ENDOCRINE HYPERTENS DIV BOSTON MA 02115 UNIV PADUA,SCH MED,DEPT CLIN MED I-35216 PADUA ITALY UNIV PADUA,SCH MED,DEPT BIOCHEM I-35216 PADUA ITALY UNIV CHILE,FAC CIENCIAS,DEPT BIOL SANTIAGO CHILE
Titolo Testata:
American journal of physiology. Cell physiology
fascicolo: 3, volume: 41, anno: 1997,
pagine: 818 - 826
SICI:
0363-6143(1997)41:3<818:PAIROR>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM-PROTON EXCHANGE; OKADAIC ACID; HUMAN-ERYTHROCYTES; MOLECULAR-CLONING; RAT ADIPOCYTES; GROWTH-FACTOR; GENE FAMILY; PHOSPHORYLATION; MEMBRANE; ANTIPORT;
Keywords:
SODIUM EXCHANGERS; TRANSPORT KINETICS; PHORBOL ESTER; ERYTHROCYTES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
G. Ceolotto et al., "PROTEIN-KINASE-C AND INSULIN REGULATION OF RED-BLOOD-CELL NA+ H+ EXCHANGE/", American journal of physiology. Cell physiology, 41(3), 1997, pp. 818-826

Abstract

Insulin activation of red blood cell (RBC) Na+/H+ (NKE) and Na+/Li+ (NLiE) exchanges is mimicked by okadaic acid, thus suggesting that it may change the state of phosphorylation of serine/threonine NHE residues. To investigate the role of the serine/threonine protein kinase C (PKC) in insulin regulation, we evaluated the effect of phorbol 12-myristate 13-acetate (PMA; 1 mu M) and insulin on PKC activity, membrane protein phosphorylation, and the activation kinetics of both exchangers. Our studies revealed that PMA decreased cytosolic PKC activity (4.1 +/- 0.6 to 2.3 +/- 0.5 pmol . mg protein(-1). min(-1), n = 9, P < 0.001), increased membrane PKC activity (42.3 +/- 5 to 132 +/- 12 pmol . mg. protein(-1). min(-1), n = 11, P < 0.001), and enhanced serine phosphorylation of bands 3, 4.1, and 4.9 membrane proteins. PIMA markedly reduced the Michaelis constant (K-m) for intracellular H+ (415 +/- 48 to 227 +/- 38 nM, n = 11, P < 0.01) but had no effect on the maximal transport rate (V-max) of NHE and the K-m for Na+ of NLiE. NHE activation and PKC activity were affected differently by insulin (100 mu U/ml) and PMA. Insulin increased the V-max of NHE and the K-m for Na+ of NLiE but had no effect on the K-m for intracellular H+ and membrane PKC activity. These findings lead us to conclude that in the human RBC, NHEis modulated by PKC and insulin through different biochemical mechanisms.

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Documento generato il 17/01/21 alle ore 18:12:07