Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation

G Coulis; M A Sentandreu; N Bleimling; M Gautel; Y Benyamin; A Ouali

doi:10.1016/S0014-5793(03)01436-4

Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation

G Coulis, M A Sentandreu, N Bleimling, M Gautel, Y Benyamin, A Ouali

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Abstract

In muscle cells, part of the calcium is tightly bound to the N1- and N2-line of the sarcomere but its physiological significance was unknown. In the present work we reported the ability of a recombinant titin fragment spanning titin domains Z9 to I1 to tightly bind calcium ions with a K-d of 0.049 +/- 0.004 nM. We further showed that calcium induced a spontaneous aggregation of the titin fragment and that the major aggregate is a tetramer. The implication of these findings on the organization of the six titin strands that emanate from the end of the thick filament within the I-band is discussed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original language	English
Pages (from-to)	271 - 275
Number of pages	5
Journal	FEBS Letters
Volume	556
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)01436-4
Publication status	Published - 2 Jan 2004

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title = "Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation",

abstract = "In muscle cells, part of the calcium is tightly bound to the N1- and N2-line of the sarcomere but its physiological significance was unknown. In the present work we reported the ability of a recombinant titin fragment spanning titin domains Z9 to I1 to tightly bind calcium ions with a K-d of 0.049 +/- 0.004 nM. We further showed that calcium induced a spontaneous aggregation of the titin fragment and that the major aggregate is a tetramer. The implication of these findings on the organization of the six titin strands that emanate from the end of the thick filament within the I-band is discussed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",

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AU - Coulis, G

AU - Sentandreu, M A

AU - Bleimling, N

AU - Gautel, M

AU - Benyamin, Y

AU - Ouali, A

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N2 - In muscle cells, part of the calcium is tightly bound to the N1- and N2-line of the sarcomere but its physiological significance was unknown. In the present work we reported the ability of a recombinant titin fragment spanning titin domains Z9 to I1 to tightly bind calcium ions with a K-d of 0.049 +/- 0.004 nM. We further showed that calcium induced a spontaneous aggregation of the titin fragment and that the major aggregate is a tetramer. The implication of these findings on the organization of the six titin strands that emanate from the end of the thick filament within the I-band is discussed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

AB - In muscle cells, part of the calcium is tightly bound to the N1- and N2-line of the sarcomere but its physiological significance was unknown. In the present work we reported the ability of a recombinant titin fragment spanning titin domains Z9 to I1 to tightly bind calcium ions with a K-d of 0.049 +/- 0.004 nM. We further showed that calcium induced a spontaneous aggregation of the titin fragment and that the major aggregate is a tetramer. The implication of these findings on the organization of the six titin strands that emanate from the end of the thick filament within the I-band is discussed. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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DO - 10.1016/S0014-5793(03)01436-4

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EP - 275

JO - FEBS Letters

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IS - 1-3

ER -

Myofibrillar tightly bound calcium in skeletal muscle fibers: a possible role of this cation in titin strands aggregation

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