%0 Journal Article %1 MacL_2000_5291 %A MacLennan, D. H. %D 2000 %J Eur. J. Biochem. %K 10951187 Animals, Calcium Calcium-Bindi, Calreticulin, Calsequestrin, Central Channels, Core, Gov't, Humans, Hyperthermia, Knockout, L-Type, Malignant Mice, Mutation, Myopathy, Non-U.S. Proteins, Research Ribonucleoproteins, Signaling, Support, Transgenic, ng %N 17 %P 5291--5297 %R 10.1046/j.1432-1327.2000.01566.x %T Ca$^2+$ signalling and muscle disease. %U http://dx.doi.org/10.1046/j.1432-1327.2000.01566.x %V 267 %X Transient elevations of intracellular Ca$^2+$ play a signalling role in such complex cellular functions as contraction, secretion, fertilization, proliferation, metabolism, heartbeat and memory. However, prolonged elevation of Ca$^2+$ above about 10 microM is deleterious to a cell and can activate apoptosis. In muscle, there is a narrow window of Ca$^2+$ dysregulation in which abnormalities in Ca$^2+$ regulatory proteins can lead to disease, rather than apoptosis. Key proteins in the regulation of muscle Ca$^2+$ are the voltage-dependent, dihydropyridine-sensitive, L-type Ca$^2+$ channels located in the transverse tubule and Ca$^2+$ release channels in the junctional terminal cisternae of the sarcoplasmic reticulum. Abnormalities in these proteins play a key role in malignant hyperthermia (MH), a toxic response to anesthetics, and in central core disease (CCD), a muscle myopathy. Sarco(endo)plasmic reticulum Ca$^2+$ ATPases (SERCAs) return sarcoplasmic Ca$^2+$ to the lumen of the sarcoplasmic reticulum. Loss of SERCA1a Ca$^2+$ pump function is one cause of exercise-induced impairment of the relaxation of skeletal muscle, in Brody disease. Phospholamban expressed in cardiac muscle and sarcolipin expressed in skeletal muscle regulate SERCA activity. Studies with knockout and transgenic mice show that gain of inhibitory function of phospholamban alters cardiac contractility and could be a causal feature in some cardiomyopathies. Calsequestrin, calreticulin, and a series of other acidic, lumenal, Ca$^2+$ binding proteins provide a buffer for Ca$^2+$ stored in the sarcoplasmic reticulum. Overexpression of cardiac calsequestrin leads to cardiomyopathy and ablation of calreticulin alters cardiac development.

@article{MacL_2000_5291, abstract = {Transient elevations of intracellular {C}a$^{2+}$ play a signalling role in such complex cellular functions as contraction, secretion, fertilization, proliferation, metabolism, heartbeat and memory. However, prolonged elevation of {C}a$^{2+}$ above about 10 microM is deleterious to a cell and can activate apoptosis. In muscle, there is a narrow window of {C}a$^{2+}$ dysregulation in which abnormalities in {C}a$^{2+}$ regulatory proteins can lead to disease, rather than apoptosis. Key proteins in the regulation of muscle {C}a$^{2+}$ are the voltage-dependent, dihydropyridine-sensitive, L-type {C}a$^{2+}$ channels located in the transverse tubule and {C}a$^{2+}$ release channels in the junctional terminal cisternae of the sarcoplasmic reticulum. Abnormalities in these proteins play a key role in malignant hyperthermia (MH), a toxic response to anesthetics, and in central core disease (CCD), a muscle myopathy. Sarco(endo)plasmic reticulum {C}a$^{2+}$ ATPases (SERCAs) return sarcoplasmic {C}a$^{2+}$ to the lumen of the sarcoplasmic reticulum. Loss of SERCA1a {C}a$^{2+}$ pump function is one cause of exercise-induced impairment of the relaxation of skeletal muscle, in Brody disease. Phospholamban expressed in cardiac muscle and sarcolipin expressed in skeletal muscle regulate SERCA activity. Studies with knockout and transgenic mice show that gain of inhibitory function of phospholamban alters cardiac contractility and could be a causal feature in some cardiomyopathies. Calsequestrin, calreticulin, and a series of other acidic, lumenal, {C}a$^{2+}$ binding proteins provide a buffer for {C}a$^{2+}$ stored in the sarcoplasmic reticulum. Overexpression of cardiac calsequestrin leads to cardiomyopathy and ablation of calreticulin alters cardiac development.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {MacLennan, D. H.}, biburl = {https://www.bibsonomy.org/bibtex/2b30ba0dc552080da502606ef7b8da59f/hake}, description = {The whole bibliography file I use.}, doi = {10.1046/j.1432-1327.2000.01566.x}, file = {MacL_2000_5291.pdf:MacL_2000_5291.pdf:PDF}, interhash = {4969a3098218f719acf84475eb27ce74}, intrahash = {b30ba0dc552080da502606ef7b8da59f}, journal = {Eur. J. Biochem.}, keywords = {10951187 Animals, Calcium Calcium-Bindi, Calreticulin, Calsequestrin, Central Channels, Core, Gov't, Humans, Hyperthermia, Knockout, L-Type, Malignant Mice, Mutation, Myopathy, Non-U.S. Proteins, Research Ribonucleoproteins, Signaling, Support, Transgenic, ng}, month = Sep, number = 17, pages = {5291--5297}, pii = {ejb1566}, pmid = {10951187}, timestamp = {2009-06-03T11:21:21.000+0200}, title = {{C}a$^{2+}$ signalling and muscle disease.}, url = {http://dx.doi.org/10.1046/j.1432-1327.2000.01566.x}, volume = 267, year = 2000 }