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2009 | 56 | 3 | 487-493
Article title

The slow sarco/endoplasmic reticulum Ca2+-ATPase declines independently of slow myosin in soleus muscle of diabetic rats

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EN
Abstracts
EN
The sarcoplasmic reticulum Ca2+-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions. In the streptozotocin-induced diabetes of rats (stz-rats), the soleus muscle showed peripheral neuropathy and the SERCA2a level decreased in type I (slow-oxidative) fibers compared to the control muscles, whereas the expression of the corresponding slow MyHC1 did not change. No difference was found at the mRNA and protein levels of SERCA and MyHC isoforms in the whole soleus, except that the level of the SERCA2a protein specifically declined in stz-rats compared to the controls. This shows that the coordinated expression of SERCA2a and MyHC1 is disrupted at the SERCA2a protein level in the diabetic soleus. The results are in line with previous observations that regulators of the Ca-homeostasis may adapt faster to type I diabetes than the contractile elements.
Keywords
Publisher

Year
Volume
56
Issue
3
Pages
487-493
Physical description
Dates
published
2009
received
2009-05-28
revised
2009-07-23
accepted
2009-09-01
(unknown)
2009-09-07
Contributors
author
  • Institute of Biochemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary
  • Institute of Biochemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary
author
  • Institute of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University Budapest, Budapest, Hungary
author
  • Institute of Biochemistry, Faculty of Medicine, University of Szeged, Szeged, Hungary
References
  • Algenstaedt P, Antonetti DA, Yaffe MB, Kahn CR (1997) Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. J Biol Chem 272: 23696-23702.
  • Aragno M, Mastrocola R, Catalano MG, Brignardello E, Danni O, Boccuzzi G (2004) Oxidative stress impairs skeletal muscle repair in diabetic rats. Diabetes 53: 1082-1088.
  • Aughsteen AA, Khair AM, Suleiman AA (2006) Quantitative morphometric study of the skeletal muscles of normal and streptozotocin-diabetic rats. JOP 7: 382-389.
  • Bassel-Duby R, Olson EN (2006) Signaling pathways in skeletal muscle remodeling. Annu Rev Biochem 75: 19-37.
  • Belke DD, Swanson EA, Dillmann WH (2004) Decreased sarcoplasmic reticulum activity and contractility in diabetic db/db mouse heart. Diabetes 53: 3201-3208.
  • Bidasee KR, Zhang Y, Shao CH, Wang M, Patel KP, Dincer UD, Besch HR Jr (2004) Diabetes increases formation of advanced glycation end products on sarco(endo)plasmic reticulum Ca2+-ATPase. Diabetes 53: 463-473.
  • Costelli P, Almendro V, Figueras MT, Reffo P, Penna F, Aragno M, Mastrocola R, Boccuzzi G, Busquets S, Bonelli G, Lopez Soriano FJ, Argilés JM, Baccino FM (2007) Modulations of the calcineurin/NF-AT pathway in skeletal muscle atrophy. Biochim Biophys Acta 1770: 1028-1036.
  • Fenyvesi R, Rácz G, Wuytack F, Zádor E (2004) The calcineurin activity and MCIP1.4 mRNA levels are increased by innervation in regenerating soleus muscle. Biochem Biophys Res Commun 320: 599-605.
  • Hämäläinen N, Pette D (1997) Coordinated fast-to-slow transitions of myosin and SERCA isoforms in chronically stimulated muscles of euthyroid and hyperthyroid rabbits. J Muscle Res Cell Motil 18: 545-554.
  • Hino S, Kondo S, Sekiya H, Saito A, Kanemoto S, Murakami T, Chihara K, Aoki Y, Nakamori M, Takahashi MP, Imaizumi K (2007) Molecular mechanisms responsible for aberrant splicing of SERCA1 in myotonic dystrophy type 1. Hum Mol Genet 16: 2834-2843.
  • Ho TH, Charlet-B N, Poulos MG, Singh G, Swanson MS, Cooper TA (2004) Muscleblind proteins regulate alternative splicing. EMBO J 23: 3103-3112.
  • Jaweed MM, Herbison GJ, Ditunno JF (1975) Denervation and reinnervation of fast and slow muscles. A histochemical study in rats. J Histochem Cytochem 23: 808-827.
  • Karpati G, Engel W (1968) 'Type grouping' in skeletal muscle after experimental reinnervation. Neurology 18: 447-455.
  • Klueber KM, Feczko JD (1994) Ultrastructural, histochemical, and morphometric analysis of skeletal muscle in a murine model of type I diabetes. Anat Rec 239: 18-34.
  • Kobayashi T, Matsumoto T, Kamata K (2005) The PI3-K/Akt pathway: roles related to alterations in vasomotor responses in diabetic models. J Smooth Muscle Res 41: 283-302.
  • Lee SW, Dai G, Hu Z, Wang X, Du J, Mitch WE (2004) Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol 15: 1537-1545.
  • Long YC, Glund S, Garcia-Roves PM, Zierath JR (2007) Calcineurin regulates skeletal muscle metabolism via coordinated changes in gene expression. J Biol Chem 282: 1607-1614.
  • Mastrocola R, Reffo P, Penna F, Tomasinelli CE, Boccuzzi G, Baccino FM, Aragno M, Costelli P (2008) Muscle wasting in diabetic and in tumor-bearing rats: role of oxidative stress. Free Radic Biol Med 44: 584-493.
  • Mendler L, Szakonyi G, Zádor E, Görbe A, Dux L, Wuytack F (1998) Expression of sarcoplasmic/endoplasmic reticulum Ca2+ ATPases in the rat extensor digitorum longus (EDL) muscle regenerating from notexin-induced necrosis. J Muscle Res Cell Motil 19: 777-785.
  • Misquitta CM, Chen T, Grover AK (2006) Control of protein expression through mRNA stability in calcium signalling. Cell Calcium 40: 329-346.
  • Pette D, Staron RS (2000) Myosin isoforms, muscle fiber types, and transitions. Microsc Res Tech 50: 500-509.
  • Punkt K, Psinia I, Welt K, Barth W, Asmussen G (1999) Effects on skeletal muscle fibres of diabetes and Ginkgo biloba extract treatment. Acta Histochem 101: 53-69.
  • Ryder JW, Bassel-Duby R, Olson EN, Zierath JR (2003) Skeletal muscle reprogramming by activation of calcineurin improves insulin action on metabolic pathways. J Biol Chem 278: 44298-44304.
  • Rupp H, Elimban V, Dhalla NS (1989) Diabetes-like action of intermittent fasting on sarcoplasmic reticulum Ca2+-pump ATPase and myosin isoenzymes can be prevented by sucrose. Biochem Biophys Res Commun 164: 319-325.
  • Rutschmann M, Dahlmann B, Reinauer H (1984) Loss of fast-twitch isomyosins in skeletal muscles of the diabetic rat. Biochem J 221: 645-650.
  • Savkur RS, Philips AV, Cooper TA (2001) Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy. Nat Genet 29: 40-47.
  • Schiaffino S, Reggiani C (1996) Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol Rev 76: 371-423.
  • Schiaffino S, Gorza E, Sartore S, Saggin L, Ansoni S, Vianello M, Gundersen K, Lomo T (1989) Three myosin heavy chain isoforms in type 2 skeletal muscle fibers. J Muscle Res Cell Motil 10: 197-205.
  • Snow LM, Sanchez OA, McLoon LK, Serfass RC Thompson LV (2005) Myosin heavy chain isoform immunolabelling in diabetic rats with peripheral neuropathy. Acta Histochem 107: 221-229.
  • Snow LM, Lynner CB, Nielsen EM, Neu HS, Thompson LV (2006) Advanced glycation end product in diabetic rat skeletal muscle in vivo. Pathobiology 73: 244-251.
  • Sun Z, Liu L, Liu N, Liu Y (2008) Muscular response and adaptation to diabetes mellitus. Front Biosci 13: 4765-4794.
  • Szabó A, Wuytack F, Zádor E (2008) The effect of passive movement on denervated soleus highlights a differential nerve control on SERCA and MyHC isoforms. J Histochem Cytochem 56: 1013-1022.
  • Szkudelski T (2001) The mechanism of alloxan and streptozotocin action in B cells of the rat pancreas. Physiol Res 50: 537-546.
  • Talmadge RJ, Paalani M (2007) Sarco(endo)plasmic reticulum calcium pump isoforms in paralyzed rat slow muscle. Biochim Biophys Acta 1770: 1187-1193.
  • Talmadge RJ, Roy RR, Chalmers GR, Edgerton VR (1996) MHC and sarcoplasmic reticulum protein isoforms in functionally overloaded cat plantaris muscle fibers. J Appl Physiol 80: 1296-1303.
  • Vangheluwe P, Raeymaekers L, Dode L, Wuytack F (2005) Modulating sarco(endo)plasmic reticulum Ca2+-ATPase 2 (SERCA2) activity: cell biological implications. Cell Calcium 38: 291-302.
  • Vasanji Z, Dhalla NS, Netticadan T (2004) Increased inhibition of SERCA2 by phospholamban in the type I diabetic heart. Mol Cell Biochem 261: 245-249.
  • Wuytack F, Eggermont JA, Raeymaekers L, Plessers L, Casteels R (1989) Antibodies against the non-muscle isoform of the endoplasmic reticulum Ca2+-transport ATPase. Biochem J 264: 765-769.
  • Wuytack F, Papp B, Verboomen H, Raeymaekers L, Dode E, Bobe R, Enouf J, Bokkala S, Authi KS, Casteels R (1994) A sarco/endoplasmic reticulum Ca2+-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells and in mast cells. J Biol Chem 269: 1410-1416.
  • Zádor E, Mendler L, Ver Heyen M, Dux L, Wuytack F (1996) Changes in mRNA levels of the sarcoplasmic/endoplasmic-reticulum Ca2+-ATPase isoforms in the rat soleus muscle regenerating from notexin-induced necrosis. Biochem J 320: 107-113.
  • Zádor E, Szakonyi G, Rácz G, Mendler L, Ver Heyen M, Lebacq J, Dux L, Wuytack F (1998) Expression of the sarco/endoplasmic reticulum Ca2+-transport ATPase protein isoforms during regeneration from notexin induced necrosis of rat muscle. Acta Histochem 100: 355-369.
  • Zádor E, Wuytack F (2003) Expression of SERCA2a is independent of innervation in regenerating soleus muscle. Am J Physiol Cell Physiol 285: C853-C861.
  • Zádor E, Fenyvesi R, Wuytack F (2005) Expression of SERCA2a is not regulated by calcineurin or upon mechanical unloading in skeletal muscle regeneration. FEBS Lett 579: 749-752.
  • Zador E, Vangheluwe P, Wuytack F (2007) The expression of the neonatal sarcoplasmic reticulum Ca2+ pump (SERCA1b) hints to a role in muscle growth and development. Cell Calcium 41: 379-388.
  • Zubrzycka-Gaarn E, MacDonald G, Phillips L, Jorgensen AO, MacLennan DH (1984) Monoclonal antibodies to the Ca2+-Mg2+-dependent ATPase of sarcoplasmic reticulum identify polymorphic forms of the enzyme and indicate the presence in the enzyme of a classical high-affinity Ca2+ binding site. J Bioenerg Biomembr 16: 441-464.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv56p487kz
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