Localization of Ca2+ + Mg2+-ATPase of the sarcoplasmic reticulum in adult rat papillary muscle.

Jorgensen, A O; Shen, A. C.-Y.; Daly, Patrick; MacLennan, David H.

doi:10.1083/jcb.93.3.883

Cited by 63 publications

(33 citation statements)

References 47 publications

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“…2a), suggesting the possible close interactions between the two types of membranes in cardiomyocytes. It is noteworthy that SR Ca 2ϩ uptake is reported to take place mainly in the longitudinal SR (away from caveolae), which contains the highest SERCA 2a density (49). In contrast, most of the SR Ca 2ϩ release would occur in proximity of the terminal cisternae (junctional and corbular SR), close to the T-tubules (49), where ryanodine receptors are concentrated (50).…”

Section: Discussionmentioning

confidence: 99%

“…It is noteworthy that SR Ca 2ϩ uptake is reported to take place mainly in the longitudinal SR (away from caveolae), which contains the highest SERCA 2a density (49). In contrast, most of the SR Ca 2ϩ release would occur in proximity of the terminal cisternae (junctional and corbular SR), close to the T-tubules (49), where ryanodine receptors are concentrated (50). We provide confocal microscopic support for the major distribution of the SERCA 2a along the longitudinal SR and around the nucleus in adult rat cardiomyocytes.…”

Section: Discussionmentioning

confidence: 99%

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The Cytosolic Phospholipase A2 Pathway, a Safeguard of β2-Adrenergic Cardiac Effects in Rat

Aït-Mamar

Cailleret

Rücker‐Martin

et al. 2005

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Cytosolic Phospholipase A2 Pathway, a Safeguard of β2-Adrenergic Cardiac Effects in Rat

Aït-Mamar

Cailleret

Rücker‐Martin

et al. 2005

Journal of Biological Chemistry

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“…23,26 Thus, the site of Ca 2ϩ release from the SR appears to be concentrated at the t-tubule, adjacent to the site of transsarcolemmal Ca 2ϩ flux (see Ca 2ϩ -Handling Proteins). Interestingly, the SR Ca 2ϩ uptake pump (SERCA2), which is responsible for removing Ca 2ϩ from the cell cytoplasm to cause relaxation and which, according to structural and biochemical studies (eg, Jorgensen et al 49 ), is thought to be located throughout the SR membrane, has been shown immunohistochemically to be concentrated at the Z line, adjacent to the t-tubule. 25 The regulatory protein phospholamban, which modulates the activity of SERCA2, shows a similar distribution (F. Brette, unpublished data, 2002).…”

Section: Protein Colocalization Within and With Proteins Adjacent Tomentioning

confidence: 99%

T-Tubule Function in Mammalian Cardiac Myocytes

Brette

Orchard

2003

Circulation Research

336

296

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Abstract-The transverse tubules (t-tubules) of mammalian cardiac ventricular myocytes are invaginations of the surface membrane. Recent studies have suggested that the structure and function of the t-tubules are more complex than previously believed; in particular, many of the proteins involved in cellular Ca 2ϩ cycling appear to be concentrated at the t-tubule. Thus, the t-tubules are an important determinant of cardiac cell function, especially as the main site of excitation-contraction coupling, ensuring spatially and temporally synchronous Ca 2ϩ release throughout the cell. Changes in t-tubule structure and protein expression occur during development and in heart failure, so that changes in the t-tubules may contribute to the functional changes observed in these conditions. The purpose of this review is to provide an overview of recent studies of t-tubule structure and function in cardiac myocytes. Key Words: cardiac muscle Ⅲ t-tubules Ⅲ excitation-contraction coupling Ⅲ heart failure T he transverse tubules (t-tubules) of mammalian cardiac ventricular myocytes are invaginations of the surface membrane that occur at the Z line and have both transverse and longitudinal elements. Many of the proteins involved in excitation-contraction coupling appear to be concentrated at the t-tubules. Therefore, it has been suggested that the t-tubules play a central role in cell activation. In the present review, we will consider the immunohistochemical and functional evidence for protein localization at the t-tubules, potential problems in the interpretation of such data, and the functional consequences of such localization. We will also consider the possible role of the t-tubules in the functional changes that occur during cardiac development, hypertrophy, and failure. Occurrence and Morphology of the T-TubulesT-tubules are present in the cardiac tissue of all species of mammals so far investigated (eg, mice, 1 rats, 2 guinea pigs, 3 rabbits, 4 dogs, 5 pigs, 1 and humans 6 ) but appear to be absent in avian, 7 reptile 8 and amphibian 8 cardiac tissue. Within mammalian cardiac tissue, t-tubules occur predominantly in ventricular myocytes, being either absent or far less developed in atrial, pacemaking, and conducting tissue, 9 although a recent report has suggested that Ϸ50% of atrial myocytes possess a sparse irregular tubular system. 10 The following discussion will concentrate on mammalian ventricular myocytes.The t-tubules are invaginations of the sarcolemma and glycocalyx, which appears to remain associated with the sarcolemma within the t-tubules. 11 Early studies of cardiac muscle showed that they occur at the Z line, at the end of each sarcomere 12 ; therefore, they occur at intervals of Ϸ2 m along the longitudinal axis of the ventricular myocyte. Subsequent studies have shown that the t-tubular system also has longitudinal extensions. 13 Although the t-tubules leave the surface membrane at the Z line, forming an approximately rectangular array, only Ϸ60% of the tubular volume occurs near the Z line; the other 40% ...

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“…Free SR vesicles originate from the region of the SR surrounding the myofibrils. Ca 2ϩ is actively transported here into the SR lumen (5,6). Junctional SR vesicles arise from the regions of the SR making contact with the sarcolemma where Ca 2ϩ is released to initiate muscle contraction (1,2,6,7).…”

mentioning

confidence: 99%

Purification, Primary Structure, and Immunological Characterization of the 26-kDa Calsequestrin Binding Protein (Junctin) from Cardiac Junctional Sarcoplasmic Reticulum

Jones

Zhang

Sanborn

et al. 1995

Journal of Biological Chemistry

205

252

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Localization of Ca2+ + Mg2+-ATPase of the sarcoplasmic reticulum in adult rat papillary muscle.

Cited by 63 publications

References 47 publications

The Cytosolic Phospholipase A2 Pathway, a Safeguard of β2-Adrenergic Cardiac Effects in Rat

The Cytosolic Phospholipase A2 Pathway, a Safeguard of β2-Adrenergic Cardiac Effects in Rat

T-Tubule Function in Mammalian Cardiac Myocytes

Purification, Primary Structure, and Immunological Characterization of the 26-kDa Calsequestrin Binding Protein (Junctin) from Cardiac Junctional Sarcoplasmic Reticulum

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