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Angaben zur Quelle [Bearbeiten]

Autor     Muthu Periasamy und Sabine Huke
Titel    SERCA Pump Level is a Critical Determinant of Ca2+ Homeostasis and Cardiac Contractility
Zeitschrift    J Mol Cell Cardiol
Jahr    2001
Nummer    33
Seiten    1053–1063
DOI    10.1006/jmcc.2001.1366
URL    http://www.ncbi.nlm.nih.gov/pubmed/11444913, http://www.med.uc.edu/pharmacology/IHL/pbl/P2_Periasamy_SERCA.pdf

Literaturverz.   

ja
Fußnoten    nein
Fragmente    3


Fragmente der Quelle:
[1.] Analyse:Aa/Fragment 009 25 - Diskussion
Zuletzt bearbeitet: 2013-01-22 17:15:42 Graf Isolan
Aa, Fragment, KeineWertung, Periasamy und Huke 2001, SMWFragment, Schutzlevel, ZuSichten

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A regulated release and uptake of intracellular Ca2+ between sarcoplasmic reticulum (SR) and cytoplasm tightly controls the contraction and relaxation cycle of the heart. A regulated release and uptake of intracellular Ca2+ between SR and cytoplasm tightly controls the contraction–relaxation cycle of the heart.
Anmerkungen

Beginn der wortwörtlichen Übernahme eines zusammenhängenden Abschnitts aus Periasamy und huke (2001), welcher in Aa/Fragment_010_06 nahtlos fortgeführt wird. Kein Hinweis auf eine Übernahme.

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[2.] Analyse:Aa/Fragment 010 06 - Diskussion
Zuletzt bearbeitet: 2013-01-22 17:07:05 Graf Isolan
Aa, Fragment, Periasamy und Huke 2001, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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Muscle contraction is initiated when Ca2+ enters the cell via L-type Ca2+ channels in the plasmalemma and as a consequence, triggers the release of a much larger amount of Ca2+ from the SR via SR Ca2+ release channels (ryanodine receptor) (Fabiato A, 1983; Bers and Perez-Reyes 1999) (Fig: 1.4.1).[...] The free cytosolic Ca2+ concentration determines the extent of the muscle activation and therefore regulates force development. The SR Ca2+ ATPase (SERCA) pumps the Ca2+ back into the SR and is therefore, responsible for muscle relaxation and for replenishing Ca2+ stores needed for the next contraction (MacLennan DH, 1970) (Fig: 4.1.1). SERCA pump activity is regulated by the small, 52-amino acid phosphoprotein phospholamban (PLB), which in its unphosphorylated state lowers the affinity of SERCA for Ca2+ (Simmermann and Jones, 1998).

Bers DM and Perez-Reyes E (1999) Ca channels in cardiac myocytes: structure and function in Ca2+ influx and intracellular Ca2+ release. Cardiovasc Res 42: 339–360.

Fabiato A (1983) Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol 245: C1–C14.

MacLennan DH (1970) Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem 245: 4508–4518.

Simmermann HK and Jones LR (1998) Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol Rev 78: 921–947.

Muscle contraction is initiated when Ca2+ enters the cell via L-type Ca2+ channels in the sarcolemma and, as a consequence, triggers the release of a much larger amount of Ca2+ from the SR via SR Ca2+ release channels (ryanodine receptor, RyR).1,2 The free cytosolic Ca2+ concentration determines the extent of muscle activation and therefore regulates force development. The SR Ca2+ ATPase (SERCA) pumps the Ca2+ back into the SR and is therefore responsible for muscle relaxation and for replenishing Ca2+ stores needed for the next contraction.3 SERCA pump activity is regulated by the small 52-aminoacid phosphoprotein phospholamban (PLB), which in its unphosphorylated state lowers the affinity of SERCA for Ca2+.4

1. FABIATO A. Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum. Am J Physiol 1983; 245: C1–C14.

2. BERS DM, PEREZ-REYES E. Ca channels in cardiac myocytes: structure and function in Ca influx and intracellular Ca release. Cardiovasc Res 1999; 42: 339–360.

3. MACLENNAN DH. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem 1970; 245: 4508–4518.

4. SIMMERMANN HK, JONES LR. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol Rev 1998; 78: 921–947.

Anmerkungen

Inkl. Literaturverweise wörtlich übereinstimmend wird ein geschlossener Abschnitt ohne Kennzeichnung übernommen. Einzige Abänderung: aus "sarcolemma" wird das allgemeinere "plasmalemma". Ansonsten erfolgt durch Aa kein Eingriff in den Textkorpus.

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[3.] Analyse:Aa/Fragment 012 06 - Diskussion
Zuletzt bearbeitet: 2013-01-22 13:23:30 Graf Isolan
Aa, Fragment, Periasamy und Huke 2001, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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A number of studies suggest that alterations in SR Ca2+ handling are a critical feature of the hypertrophied or failing myocardium. Alterations in the expression of different SR proteins and associated Ca2+ transport abnormalities in cardiac hypertrophy and heart failure have been reviewed by Houser et al. (2000). The SERCA2a isoform plays a central role in SR Ca2+ handling required for excitation-contraction coupling in the heart. Moreover, it was shown for mouse, rat and rabbit that the expression of SERCA pump gradually increases during development (Luss et al., 1999; Reed et al., 2000; Chen et al., 2000; Fisher et al., 1992; Gombosova et al., 1998). This increase was accompanied by a shortening of relaxation time in neonatal ventricle (Gombosova et al., 1998). In adult heart SERCA levels are not steady but influenced by aging and fluctuations

in thyroid hormone level. A decrease in content and activity of SERCA was described in experimental models of senescence and in senescent human myocardium (Taffet et al., 1993; Cain et al., 1998). This decrease was associated with a prolonged contraction time and depressed myocardial function. Therefore, several naturally occurring variations in SERCA expression level correlate with the contractile status of the heart. The expression level of SERCA pump protein appears to be a critical determinant of cardiac contractility.

Varying degrees of defects in the SR Ca2+ uptake have been identified in animal models of heart disease and have been shown to correlate with altered contractile function (reviewed in Arai et al., 1994). Studies from many laboratories have shown that the expression level of SERCA is significantly decreased in pressure overload-induced hypertrophy/heart failure (Nagai et al., 1989; Feldman et al., 1993; Matsui et al., 1995; Qi et al., 1997; Aoyagi et al., 1999). In these studies decreased SR calcium transport was observed (Arai et [al., 1994; Feldman et al., 1993; 1993; Matsui et al., 1995; Qi et al., 1997; Kiss et al., 1995).]


Arai M, Matsui H and Periasamy M (1994) Sarcoendoplasmic reticulum gene expression in cardiac hypertrophy and heart failure. Circ Res 74: 555–564.

Aoyagi T, Yonekura K, Eto Y, Matsumoto A, Yokoyama I, Sugiura S, Momomura S, Hirata Y, Baker DL and Periasamy M (1999) The sarcoplasmic reticulum Ca2+-ATPase (SERCA2) gene promoter activity is decreased in response to severe left ventricular pressure-overload hypertrophy in rat hearts. J Mol Cell Cardiol 31: 919–926.

Cain BS, Medlum DR, Joo KS, Wang JF, Meng X, Clefeland JC Jr, Banerjee A and Harken AH (1998) Human SERCA2a levels correlate inversely with age in senescent human myocardium. Am J Coll Cardiol 32: 458–467.

Chen F, Ding S, Lee BS and Wetzel GT (2000) Sarcoplasmic reticulum Ca2+ ATPase and cell contraction in developing rabbit heart. J Mol Cell Cardiol 32: 745–755.

Feldman AM, Weinberg EO, Ray PE and Lorell BH (1993) Selective changes in cardiac gene expression during compensated hypertrophy and the transition to cardiac decompensation in rats with chronic aortic banding. Circ Res 73: 184– 192.

Fisher DJ, Tate CA and Phillips S (1992) Developmental regulation of the sarcoplasmic reticulum pump in the rabbit heart. Pediatr Res 31: 474–479.

Gombosova I, Boknik P, Kirchhefer U, Knapp J, Luss H, Muller FU, Muller T, Vahlensiek U, Schmitz W, Bodor GS and Neumann J (1998) Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases. Am J Physiol 274: H2123–H2132.

Houser SR, Piacentino V and Weisser J (2000) Abnormalities of calcium cycling in the hypertrophied and failing heart. J Mol Cell Cardiol 32: 1595–1607.

Kiss E, Ball NA, Kranias EG and Walsh RA (1995) Differential changes in cardiac phospholamban and sarcoplasmic reticular Ca2+-ATPase protein levels. Effects on Ca2+transport and mechanics in compensated pressure-overload hypertrophy and congestive heart failure. Circ Res 77: 759–764.

Luss I, Boknik P, Jones LR, Kirchhefer U, Knapp J, Linck B, Luss H, Meissner A, Muller FR, Schmitz W, Vahlensieck U and Neumann J (1999) Expression of cardiac calcium regulatory proteins in atrium v ventricle in different species. J Mol Cell Cardiol 31: 1299–1314.

Matsui H, MacLennan DH, Alpert N and Periasamy M (1995) Sarcoplasmic reticulum gene expression in pressure overload-induced cardiac hypertrophy in rabbit. Am J Physiol 268: C252–C258.

Nagai R, Herzberg AZ, Brandl CJ, Fuji J, Tada M, MacLennan DH, Alpert NR and Periasamy M (1989) Regulation of myocardial Ca2+ATPase and phospholamban mRNA expression in response to pressure overload and thyroid hormone. Proc Natl Acad Sci USA 86: 2966–2970.

Qi M, Shannon TR, Euler DE, Bers DM and Samarel AM (1997) Downregulation of sarcoplasmic reticulum Ca2+-ATPase during progression of left ventricular hypertrophy. Am J Physiol 272: H2416–H2424.

Reed TD, Babu GJ, Ji Y, Zilberman A, Ver Heyen M, Wuytack F and Periasamy M (2000) The expression of SR calcium transport ATPase and the Na/Ca exchanger are antithetically regulated during mouse cardiac development and in hypo/hyperthyroidism. J Mol Cell Cardiol 32: 453–464.

Taffet GE, Pham TT, Bick DL, Entman ML, Pownall HJ and Bick RJ (1993) The calcium uptake of the rat heart sarcoplasmic reticulum is altered by dietary lipid. J Membr Biol 131: 963–998.

[Seite 1053]

A number of studies, conducted on animal models of heart failure and human failing hearts, suggest that alterations in SR Ca2+ handling are a critical feature of the hypertrophied or failing myocardium. Alterations in the expression of different SR proteins and its associated Ca2+ transport abnormalities in cardiac hypertrophy and heart failure have been recently reviewed by Houser et al.6

[Seite 1054]

The SERCA2a isoform plays a central role in SR Ca2+ handling required for excitation-contraction coupling in the heart. [...] Moreover, it was shown for mouse, rat and rabbit that the expression of SERCA pump gradually increases during development.16,19–22 This increase was again accompanied by a shortening of relaxation time in adult v neonatal ventricle.22 In addition also in adult hearts SERCA levels are not steady, but are influenced by aging and fluctuations in thyroid hormone levels. A decrease in content and activity of SERCA was described in experimental models of senescence and in senescent human myocardium.23,24 This decrease was associated with a prolonged contraction time and depressed myocardial function. [...]

Therefore, several naturally occurring variations in SERCA expression level correlate with the contractile status of the heart. The expression level of SERCA pump protein appears to be a critical determinant of cardiac contractility. [...]

Varying degrees of defects in the SR Ca2+ uptake function have been identified in animal models of heart disease and have been shown to correlate with altered contractile SERCA2a Pump Expression Level in the function (reviewed in Arai et al.7). Studies from many laboratories have shown that the expression level of SERCA is significantly decreased in pressure overload (PO)-induced hypertrophy/heart failure.30–34 In these studies decreased SR calcium transport and formation of the phosphoenzyme intermediate, E-P, was observed.7,31–33,35


6. HOUSER SR, PIACENTINO V, WEISSER J. Abnormalities of calcium cycling in the hypertrophied and failing heart. J Mol Cell Cardiol 2000; 32: 1595–1607.

7. ARAI M, MATSUI H, PERIASAMY M. Sarcoendoplasmic reticulum gene expression in cardiac hypertrophy and heart failure. Circ Res 1994; 74: 555–564.

16. LUSS I, BOKNIK P, JONES LR, KIRCHHEFER U, KNAPP J, LINK B, LUSS H, MEISSNER A, MULLER FR, SCHMITZ W, VAHLENSIECK U, NEUMANN J. Expression of cardiac calcium regulatory proteins in atrium v ventricle in different species. J Mol Cell Cardiol 1999; 31: 1299–1314.

19. REED TD, BABU GJ, JI Y, ZILBERMAN A, VER HEYEN M, WUYTACK F, PERIASAMY M. The expression of SR calcium transport ATPase and the Na/Ca exchanger are antithetically regulated during mouse cardiac development and in hypo/hyperthyroidism. J Mol Cell Cardiol 2000; 32: 453–464.

20. CHEN F, DING S, LEE BS, WETZEL GT. Sarcoplasmic reticulum Ca(2+)ATPase and cell contraction in developing rabbit heart. J Mol Cell Cardiol 2000; 32: 745–755.

21. FISHER DJ, TATE CA, PHILLIPS S. Developmental regulation of the sarcoplasmic reticulum pump in the rabbit heart. Pediatr Res 1992; 31: 474–479.

22. GOMBOSOVA I, BOKNIK P, KIRCHHEFER U, KNAPP J, LUSS H, MULLER FU, MULLER T, VAHLENSIECK U, SCHMITZ W, BODOR GS, NEUMANN J. Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases. Am J Physiol 1998; 274: H2123–H2132.

23. TAFFET GE, PHAM TT, BICK DL, ENTMAN ML, POWNALL HJ, BICK RJ. The calcium uptake of the rat heart sarcoplasmic reticulum is altered by dietary lipid. J Membr Biol 1993; 131: 963–998.

24. CAIN BS, MEDLUM DR, JOO KS, WANG JF, MENG X, CLEFELAND JC JR, BANERJEE A, HARKEN AH. Human SERCA2a levels correlate inversely with age in senescent human myocardium. J Am Cardiol 1998; 32: 458–467.

30. NAGAI R, HERZBERG AZ, BRANDL CJ, FUJI J, TADA M, MACLENNAN DH, ALPERT NR, PERIASAMY M. Regulation of myocardial Ca2+ ATPase and phospholamban mRNA expression in response to pressure overload and thyroid hormone. Proc Natl Acad Sci USA 1989; 86: 2966–2970.

31. FELDMAN AM, WEINBERG EO, RAY PE, LORELL BH. Selective changes in cardiac gene expression during compensated hypertrophy and the transition to cardiac decompensation in rats with chronic aortic banding. Circ Res 1993; 73: 184–192.

32. MATSUI H, MACLENNAN DH, ALPERT N, PERIASAMY M. Sarcoplasmic reticulum gene expression in pressure overload-induced cardiac hypertrophy in rabbit. Am J Physiol 1995; 268: C252–C258.

33. QI M, SHANNON TR, EULER DE, BERS DM, SAMAREL AM. Downregulation of sarcoplasmic reticulum Ca2+-ATPase during progression of left ventricular hypertrophy. Am J Physiol 1997; 272: H2416–H2424.

34. AOYAGI T, YONEKURA K, ETO Y, MATSUMOTO A, YOKOYAMA I, SUGIURA S, MONOMURA S, HIRATAA Y, BAKER DL, PERIASAMY M. The sarcoplasmic reticulum Ca2+-ATPase (SERCA2) gene promoter activity is decreased in response to severe left ventricular pressure-overload hypertrophy in rat hearts. J Mol Cell Cardiol 1999; 31: 919–926.

35. KISS E, BALL NA, KRANIAS EG,WALSH RA. Differential changes in cardiac phospholamban and sarcoplasmic reticular Ca(2+)-ATPase protein levels. Effects on Ca2+ transport and mechanics in compensated pressure-overload hypertrophy and congestive heart failure. Circ Res 1995; 77: 759-764.

Anmerkungen

Ein Zusammenschnitt von kaum veränderten Originalpassagen ohne jede Kennzeichnung. Auch alle Literaturverweise werden übernommen.

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(Graf Isolan)

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