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SERCA

SERCA, or sarco/endoplasmic reticulum Ca2+-ATPase, or SR Ca2+-ATPase, is a calcium ATPase-type P-ATPase. Its major function is to transport calcium from the cytosol into the sarcoplasmic reticulum.

Contents

SERCA is a P-type ATPase. It resides in the sarcoplasmic reticulum (SR) within myocytes. It is a Ca2+ ATPase that transfers Ca2+ from the cytosol of the cell to the lumen of the SR. This uses energy from ATP hydrolysis during muscle relaxation.

There are 3 major domains on the cytoplasmic face of SERCA: the phosphorylation and nucleotide-binding domains, which form the catalytic site, and the actuator domain, which is involved in the transmission of major conformational changes.

In addition to its calcium-transporting functions, SERCA1 generates heat in brown adipose tissue and in skeletal muscles. Along with the heat it naturally produces due to its inefficiency in pumpingCa2+
ions, when it binds to a regulator called sarcolipin it stops pumping and functions solely as an ATP hydrolase. This mechanism of thermogenesis is widespread in mammals and in endothermic fishes.

The rate at which SERCA moves Ca2+ across the SR membrane can be controlled by the regulatory protein phospholamban (PLB/PLN). SERCA is not as active when PLB is bound to it. Increased β-adrenergic stimulation reduces the association between SERCA and PLB by the phosphorylation of PLB by PKA. When PLB is associated with SERCA, the rate of Ca2+ movement is reduced; upon dissociation of PLB, Ca2+ movement increases.

Another protein, calsequestrin, binds calcium within the SR and helps to reduce the concentration of free calcium within the SR, which assists SERCA so that it does not have to pump against such a high concentration gradient. The SR has a much higher concentration of Ca2+ (10,000x) inside when compared to the cytoplasmic Ca2+ concentration. SERCA2 can be regulated by microRNAs, for instance miR-25 suppresses SERCA2 in heart failure.

For experimental purposes, SERCA can be inhibited by thapsigargin and induced by istaroxime.

There are 3 major paralogs, SERCA1-3, which are expressed at various levels in different cell types.

There are additional post-translational isoforms of both SERCA2 and SERCA3, which serve to introduce the possibility of cell-type-specific Ca2+-reuptake responses as well as increasing the overall complexity of the Ca2+ signaling mechanism.

  1. Marín-García, José (2014-01-01), Marín-García, José (ed.), "Chapter 23 - Gene- and Cell-Based Therapy for Cardiovascular Disease", Post-Genomic Cardiology (Second Edition), Boston: Academic Press, pp. 783–833, doi:10.1016/b978-0-12-404599-6.00023-8, ISBN 978-0-12-404599-6, retrieved2020-12-28
  2. de Meis L; Oliveira GM; Arruda AP; Santos R; Costa RM; Benchimol M (2005). "The thermogenic activity of rat brown adipose tissue and rabbit white muscle Ca2+-ATPase". IUBMB Life. 57 (4–5): 337–45. doi:10.1080/15216540500092534. PMID 16036618.
  3. Arruda AP; Nigro M; Oliveira GM; de Meis L (June 2007). "Thermogenic activity of Ca2+-ATPase from skeletal muscle heavy sarcoplasmic reticulum: the role of ryanodine Ca2+ channel". Biochim. Biophys. Acta. 1768 (6): 1498–505. doi:10.1016/j.bbamem.2007.03.016. PMID 17466935.
  4. Bal, Naresh C.; Periasamy, Muthu (2020-03-02). "Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis". Philosophical Transactions of the Royal Society B: Biological Sciences. 375 (1793): 20190135. doi:10.1098/rstb.2019.0135. PMC7017432. PMID 31928193.
  5. Legendre, Lucas J.; Davesne, Donald (2020-03-02). "The evolution of mechanisms involved in vertebrate endothermy". Philosophical Transactions of the Royal Society B: Biological Sciences. 375 (1793): 20190136. doi:10.1098/rstb.2019.0136. PMC7017440. PMID 31928191.
  6. MacLennan, David H.; Kranias, Evangelia G. (July 2003). "Phospholamban: a crucial regulator of cardiac contractility". Nature Reviews Molecular Cell Biology. 4 (7): 566–577. doi:10.1038/nrm1151. PMID 12838339. S2CID 3050392.

SERCA
SERCA Language Watch Edit SERCA or sarco endoplasmic reticulum Ca2 ATPase or SR Ca2 ATPase is a calcium ATPase type P ATPase Its major function is to transport calcium from the cytosol into the sarcoplasmic reticulum Contents 1 Function 2 Regulation 3 Paralogs 4 References 5 External linksFunction EditSERCA is a P type ATPase 1 It resides in the sarcoplasmic reticulum SR within myocytes 1 It is a Ca2 ATPase that transfers Ca2 from the cytosol of the cell to the lumen of the SR 1 This uses energy from ATP hydrolysis during muscle relaxation 1 There are 3 major domains on the cytoplasmic face of SERCA the phosphorylation and nucleotide binding domains which form the catalytic site and the actuator domain which is involved in the transmission of major conformational changes In addition to its calcium transporting functions SERCA1 generates heat in brown adipose tissue and in skeletal muscles 2 3 Along with the heat it naturally produces due to its inefficiency in pumping Ca2 ions when it binds to a regulator called sarcolipin it stops pumping and functions solely as an ATP hydrolase This mechanism of thermogenesis is widespread in mammals and in endothermic fishes 4 5 Regulation EditThe rate at which SERCA moves Ca2 across the SR membrane can be controlled by the regulatory protein phospholamban PLB PLN SERCA is not as active when PLB is bound to it Increased b adrenergic stimulation reduces the association between SERCA and PLB by the phosphorylation of PLB by PKA 6 When PLB is associated with SERCA the rate of Ca2 movement is reduced upon dissociation of PLB Ca2 movement increases Another protein calsequestrin binds calcium within the SR and helps to reduce the concentration of free calcium within the SR which assists SERCA so that it does not have to pump against such a high concentration gradient The SR has a much higher concentration of Ca2 10 000x inside when compared to the cytoplasmic Ca2 concentration SERCA2 can be regulated by microRNAs for instance miR 25 suppresses SERCA2 in heart failure For experimental purposes SERCA can be inhibited by thapsigargin and induced by istaroxime Paralogs EditThere are 3 major paralogs SERCA1 3 which are expressed at various levels in different cell types ATP2A1 SERCA1 ATP2A2 SERCA2 ATP2A3 SERCA3 There are additional post translational isoforms of both SERCA2 and SERCA3 which serve to introduce the possibility of cell type specific Ca2 reuptake responses as well as increasing the overall complexity of the Ca2 signaling mechanism References Edit a b c d Marin Garcia Jose 2014 01 01 Marin Garcia Jose ed Chapter 23 Gene and Cell Based Therapy for Cardiovascular Disease Post Genomic Cardiology Second Edition Boston Academic Press pp 783 833 doi 10 1016 b978 0 12 404599 6 00023 8 ISBN 978 0 12 404599 6 retrieved 2020 12 28 de Meis L Oliveira GM Arruda AP Santos R Costa RM Benchimol M 2005 The thermogenic activity of rat brown adipose tissue and rabbit white muscle Ca2 ATPase IUBMB Life 57 4 5 337 45 doi 10 1080 15216540500092534 PMID 16036618 Arruda AP Nigro M Oliveira GM de Meis L June 2007 Thermogenic activity of Ca2 ATPase from skeletal muscle heavy sarcoplasmic reticulum the role of ryanodine Ca2 channel Biochim Biophys Acta 1768 6 1498 505 doi 10 1016 j bbamem 2007 03 016 PMID 17466935 Bal Naresh C Periasamy Muthu 2020 03 02 Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non shivering thermogenesis Philosophical Transactions of the Royal Society B Biological Sciences 375 1793 20190135 doi 10 1098 rstb 2019 0135 PMC 7017432 PMID 31928193 Legendre Lucas J Davesne Donald 2020 03 02 The evolution of mechanisms involved in vertebrate endothermy Philosophical Transactions of the Royal Society B Biological Sciences 375 1793 20190136 doi 10 1098 rstb 2019 0136 PMC 7017440 PMID 31928191 MacLennan David H Kranias Evangelia G July 2003 Phospholamban a crucial regulator of cardiac contractility Nature Reviews Molecular Cell Biology 4 7 566 577 doi 10 1038 nrm1151 PMID 12838339 S2CID 3050392 External links EditSarcoplasmic Reticulum Calcium Transporting ATPases at the US National Library of Medicine Medical Subject Headings MeSH Retrieved from https en wikipedia org w index php title SERCA amp oldid 1022674775, wikipedia, wiki, book,

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