The effect of calcium ions on subcellular localization of aldolase–FBPase complex in skeletal muscle

Mamczur, Piotr; Rakus, Dariusz; Gizak, Agnieszka; Duś, Danuta; Dżugaj, Andrzej

doi:10.1016/j.febslet.2005.01.071

Cited by 30 publications

(28 citation statements)

References 27 publications

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“…1A). This result concurs with a previously presented hypothesis concerning the existence of a glyconeogenic metabolon around this compartment (Rakus et al, 2003a,b;Mamczur et al, 2005). The immunogold method also indicated colocalisation of both enzymes inside the cardiomyocyte nuclei, where it was restricted to the heterochromatin region (Fig.…”

Section: Immunocytochemistrysupporting

confidence: 95%

“…On the other hand, enzymes catalyzing reversible reactions, like aldolase, might create either glycolytic or glyconeogenic complexes, depending on cellular requirements (Rakus et al, 2004;Mamczur et al, 2005). In the glycogen synthesis, aldolase not only provides the substrate for FBPase but also protects it against AMP inhibition (Rakus and Dzugaj, 2000;Rakus et al, 2003b).…”

Section: Discussionmentioning

confidence: 99%

“…2C, D). Additionally, TRITC-aldolase, as in the skeletal muscle (Rakus et al, 2003a,b;Mamczur et al, 2005), localised around the M-line of the sarcomer (Fig. 2A).…”

Section: Colocalisation Of the Enzymes In Permeabilised Cardiomyocytesmentioning

confidence: 94%

“…Therefore, the existence of in vivo heterologous complex, consisting of aldolase, FBPase and a-actinin has been postulated (Rakus et al, 2003a;Mamczur et al, 2005). The investigation ex vivo revealed the colocalisation of the proteins on the Zline (Rakus et al, 2003a;Mamczur et al, 2005).…”

Section: Introductionmentioning

confidence: 93%

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Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes

Mamczur¹,

Duś²,

Dżugaj³

2007

Cell Biology International

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The protein exchange method, immunocytochemistry and the nuclear import of fluorophore-labeled enzymes were used to investigate the colocalisation of aldolase and FBPase in cardiomyocytes. The results indicate in vivo interaction of these two enzymes. In the cardiomyocyte cytoplasm, these enzymes were found to colocalise at the Z-line and on intercalated discs. The translocation of both enzymes through the nuclear pores was also investigated. The immunocytochemistry revealed the colocalisation of aldolase and FBPase in the heterochromatin region of cardiomyocyte nuclei. The Pearson's correlation coefficients, which represent the degree of colocalisation were 0.47, 0.52 and 0.66 in the sarcomer, the intercalated disc and the nucleus, respectively. This is the first report on aldolase and FBPase colocalisation in cardiomyocytes. Interaction of aldolase with FBPase, which results in heterologous complex formation, is necessary for glyconeogenesis to proceed. Therefore, this metabolic pathway in the sarcomer, in the intercalated disc as well as in the nucleus might be expected.

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Section: Immunocytochemistrysupporting

confidence: 95%

Section: Discussionmentioning

confidence: 99%

“…2C, D). Additionally, TRITC-aldolase, as in the skeletal muscle (Rakus et al, 2003a,b;Mamczur et al, 2005), localised around the M-line of the sarcomer (Fig. 2A).…”

Section: Colocalisation Of the Enzymes In Permeabilised Cardiomyocytesmentioning

confidence: 94%

Section: Introductionmentioning

confidence: 93%

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Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes

Mamczur¹,

Duś²,

Dżugaj³

2007

Cell Biology International

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“…An increasing body of evidence suggests that the association of FBPase with subcellular elements and other proteins (especially with aldolase and sarcomeric aactinin) [4,25,26] plays an important role in the regulation of FBPase activity. In striated muscles, this association is inhibited by Ca 2+ concentrations characteristic for contracting muscle [8,27], which indicates that binding of FBPase to cellular structures may play a role in controlling the speed of glyconeogenesis.…”

Section: Discussionmentioning

confidence: 99%

Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

et al. 2006

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Subcellular localization of FBPase, a regulatory enzyme of glyconeogenesis, was examined inside dividing and differentiating satellite cells from rat muscle. In dividing myoblasts, FBPase was located in cytosol and nuclei. When divisions ceased, FBPase became restricted to the cytosolic compartment and finally was found to associate with the Z-lines, as in adult muscle. Moreover, a 12-fold decrease was observed in the number of FBPase-positive nuclei associated with muscle fibres of adult rat, as compared with young muscle, possibly reflecting the reduction in number of active satellite cells during muscle maturation. The data might suggest that FBPase participates in some nuclear processes during development and regeneration of skeletal muscle.

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Survey of the year 2005 commercial optical biosensor literature

2006

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We identified 1113 articles (103 reviews, 1010 primary research articles) published in 2005 that describe experiments performed using commercially available optical biosensors. While this number of publications is impressive, we find that the quality of the biosensor work in these articles is often pretty poor. It is a little disappointing that there appears to be only a small set of researchers who know how to properly perform, analyze, and present biosensor data. To help focus the field, we spotlight work published by 10 research groups that exemplify the quality of data one should expect to see from a biosensor experiment. Also, in an effort to raise awareness of the common problems in the biosensor field, we provide side-by-side examples of good and bad data sets from the 2005 literature.

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The effect of calcium ions on subcellular localization of aldolase–FBPase complex in skeletal muscle

Cited by 30 publications

References 27 publications

Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes

Colocalization of aldolase and FBPase in cytoplasm and nucleus of cardiomyocytes

Changes in subcellular localization of fructose 1,6‐bisphosphatase during differentiation of isolated muscle satellite cells

Survey of the year 2005 commercial optical biosensor literature

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