The presence of sarcolipin results in increased heat production by Ca2+-ATPase
The presence of sarcolipin results in increased heat production by Ca2+-ATPase
Skeletal muscle sarcoplasmic reticulum of large mammals such as rabbit contains sarcolipin (SLN), a small peptide with a single transmembrane -helix. When reconstituted with the Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum into sealed vesicles, the presence of SLN leads to a reduced level of accumulation of Ca2+. Heats of reaction of the reconstituted Ca2+-ATPase with ATP were measured using isothermal calorimetry. The heat released increased linearly with time over 30 min and increased with increasing SLN content. Rates ATP hydrolysis by the reconstituted Ca2+-ATPase were constant over a 30-min time period and were the same when measured in the presence or absence of an ATP-regenerating system. The calculated values of heat released per mol of ATP hydrolyzed increased with increasing SLN content and fitted to a simple binding equation with a dissociation constant for the SLN·ATPase complex of 6.9 x 10–4 ± 2.9 x 10–4 in units of mol fraction per monolayer. It is suggested that the interaction between Ca2+-ATPase and SLN in the sarcoplasmic reticulum could be important in thermogenesis by the sarcoplasmic reticulum.
sarcoplasmic-reticulum CA2+-ATPase, skeletal-muscle, calcium-pump, reconstituted vesicles, CA2+, phospholamban, ATPase, mechanism, (CA-2++MG-2+)-ATPase, accumulation
36597-36602
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Broadbridge, R.
85df8b86-d1d9-42d3-8764-6aaebab3d856
Harrison, S.L.
528e8399-b5f8-434e-8aca-8b1b7908a6a2
Gore, M.G.
7bd6db4b-c5a2-4206-8666-b92208ba7979
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
1 December 2006
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Broadbridge, R.
85df8b86-d1d9-42d3-8764-6aaebab3d856
Harrison, S.L.
528e8399-b5f8-434e-8aca-8b1b7908a6a2
Gore, M.G.
7bd6db4b-c5a2-4206-8666-b92208ba7979
Lee, A.G.
0891914c-e0e2-4ee1-b43e-1b70eb072d8e
East, J.M.
9fe7f794-1d89-4935-9a99-b831d786056e
Mall, S., Broadbridge, R., Harrison, S.L., Gore, M.G., Lee, A.G. and East, J.M.
(2006)
The presence of sarcolipin results in increased heat production by Ca2+-ATPase.
The Journal of Biological Chemistry, 281 (48), .
(doi:10.1074/jbc.M606869200).
Abstract
Skeletal muscle sarcoplasmic reticulum of large mammals such as rabbit contains sarcolipin (SLN), a small peptide with a single transmembrane -helix. When reconstituted with the Ca2+-ATPase from skeletal muscle sarcoplasmic reticulum into sealed vesicles, the presence of SLN leads to a reduced level of accumulation of Ca2+. Heats of reaction of the reconstituted Ca2+-ATPase with ATP were measured using isothermal calorimetry. The heat released increased linearly with time over 30 min and increased with increasing SLN content. Rates ATP hydrolysis by the reconstituted Ca2+-ATPase were constant over a 30-min time period and were the same when measured in the presence or absence of an ATP-regenerating system. The calculated values of heat released per mol of ATP hydrolyzed increased with increasing SLN content and fitted to a simple binding equation with a dissociation constant for the SLN·ATPase complex of 6.9 x 10–4 ± 2.9 x 10–4 in units of mol fraction per monolayer. It is suggested that the interaction between Ca2+-ATPase and SLN in the sarcoplasmic reticulum could be important in thermogenesis by the sarcoplasmic reticulum.
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Published date: 1 December 2006
Keywords:
sarcoplasmic-reticulum CA2+-ATPase, skeletal-muscle, calcium-pump, reconstituted vesicles, CA2+, phospholamban, ATPase, mechanism, (CA-2++MG-2+)-ATPase, accumulation
Identifiers
Local EPrints ID: 45824
URI: http://eprints.soton.ac.uk/id/eprint/45824
ISSN: 0021-9258
PURE UUID: 05743433-2da7-4dce-aaee-18564d2a12b8
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Date deposited: 16 Apr 2007
Last modified: 15 Mar 2024 09:13
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Author:
S. Mall
Author:
R. Broadbridge
Author:
S.L. Harrison
Author:
M.G. Gore
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