Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers

Chen MF, Jockusch H (1999)
Biochemical and biophysical research communications 261(2): 528-533.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Chloride currents (I-Cl) were investigated with the two-electrode voltage-clamp technique in enzymatically isolated fibers from interosseus muscles of wildtype (WT), denervated WT, and myotonic (ADR, ClC-1-deficient) mice. Characteristics of I-Cl were consistent with previous observations on rat muscle fibers and cultured nonmuscle cells transfected with hClC-1 cDNA. In the presence of 0.1 mM anthracene-9-carboxylic acid and in ADR fibers, I-Cl was reduced by > 90%. WT interosseus fibers denervated 6-7 days prior to isolation showed similar to 50% I-Cl compared to control fibers. Addition of 3.3 mu M staurosporine, a nonspecific inhibitor of protein kinases, increased I-Cl. in WT interosseus fibers by a factor of approximately two and altered its kinetic characteristics, We conclude that in dissociated fibers cultured for 1-2 days, in contrast to freshly isolated muscles, chloride conductance is downregulated by a mechanism involving protein phosphorylation. In situ this short-term regulation may complement transcriptional long-term regulation Of ClC-1. (C) 1999 Academic Press.
Erscheinungsjahr
Zeitschriftentitel
Biochemical and biophysical research communications
Band
261
Zeitschriftennummer
2
Seite
528-533
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Chen MF, Jockusch H. Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers. Biochemical and biophysical research communications. 1999;261(2):528-533.
Chen, M. F., & Jockusch, H. (1999). Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers. Biochemical and biophysical research communications, 261(2), 528-533. doi:10.1006/bbrc.1999.1061
Chen, M. F., and Jockusch, H. (1999). Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers. Biochemical and biophysical research communications 261, 528-533.
Chen, M.F., & Jockusch, H., 1999. Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers. Biochemical and biophysical research communications, 261(2), p 528-533.
M.F. Chen and H. Jockusch, “Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers”, Biochemical and biophysical research communications, vol. 261, 1999, pp. 528-533.
Chen, M.F., Jockusch, H.: Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers. Biochemical and biophysical research communications. 261, 528-533 (1999).
Chen, MF, and Jockusch, Harald. “Role of phosphorylation and physiological state in the regulation of the muscular chloride channel CIC-1: A voltage-clamp study on isolated M-interosseus fibers”. Biochemical and biophysical research communications 261.2 (1999): 528-533.

6 Zitationen in Europe PMC

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Protein kinase C-dependent regulation of ClC-1 channels in active human muscle and its effect on fast and slow gating.
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Muscle chloride channel dysfunction in two mouse models of myotonic dystrophy.
Lueck JD, Mankodi A, Swanson MS, Thornton CA, Dirksen RT., J Gen Physiol 129(1), 2007
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Disuse of rat muscle in vivo reduces protein kinase C activity controlling the sarcolemma chloride conductance.
Pierno S, Desaphy JF, Liantonio A, De Luca A, Zarrilli A, Mastrofrancesco L, Procino G, Valenti G, Conte Camerino D., J Physiol 584(pt 3), 2007
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Papponen H, Kaisto T, Myllylä VV, Myllylä R, Metsikkö K., Exp Neurol 191(1), 2005
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