ArticleBiochemical and biophysical research communications2006
A novel isoform of delta-sarcoglycan is localized at the sarcoplasmic reticulum of mouse skeletal muscle.
Article in Biochemical and biophysical research communications, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Diversification of the muscle proteome through alternative splicing.Skeletal muscle · 2018Review
- Nanospan, an alternatively spliced isoform of sarcospan, localizes to the sarcoplasmic reticulum in skeletal muscle and is absent in limb girdle muscular dystrophy 2F.Skeletal muscle · 2017Article
- Dystrophin-compromised sarcoglycan-δ-knockout diaphragm requires full wild-type embryonic stem cell reconstitution for correction.Journal of cell science · 2012Article
- The zebrafish dag1 mutant: a novel genetic model for dystroglycanopathies.Human molecular genetics · 2011Article
- δ-Sarcoglycan-deficient muscular dystrophy: from discovery to therapeutic approaches.Skeletal muscle · 2011Article
- Altered calcium pump and secondary deficiency of gamma-sarcoglycan and microspan in sarcoplasmic reticulum membranes isolated from delta-sarcoglycan knockout mice.Cell calcium · 2010Article
- Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sarcoglycan-sarcospan complex (alpha-, beta-, gamma-, delta-, epsilon-, and zeta-SG-SSPN), a component of the dystrophin-associated glycoprotein complex (DAGC), is located at the sarcolemma of muscle fibers where it contributes to maintain cell integrity during contraction-relaxation cycles; gamma- and delta-SG are also expressed in the sarcoplasmic reticulum (SR). In this study, we report the identification of a novel isoform of murine delta-SG produced by alternative splicing that we named delta-SG3. This isoform is present at transcript level in several tissues, with its highest expression in skeletal and cardiac muscle. The delta-SG3 protein lacks the last 122 amino acids at the C-terminal, which are replaced by 10 new amino acids (EGFLNMQLAG). Interestingly, double immunofluorescence analysis for delta-SG3 and the dihydropyridine receptor (DHPR) shows a close localization of these two proteins. We propose the subcellular distribution of this novel delta-SG3 isoform at the SR and its involvement in intracellular calcium concentration regulation.
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