TY - JOUR
T1 - A novel isoform of δ-sarcoglycan is localized at the sarcoplasmic reticulum of mouse skeletal muscle
AU - Estrada, Francisco J.
AU - Mornet, Dominique
AU - Rosas-Vargas, Haydeé
AU - Angulo, Alexandra
AU - Hernández, Manuel
AU - Becker, Viola
AU - Rendón, Alvaro
AU - Ramos-Kuri, Manuel
AU - Coral-Vázquez, Ramón M.
N1 - Funding Information:
F. J. Estrada was supported by the Consejo Nacional de Ciencia y Tecnología (CONACYT) Register Number 165401.
PY - 2006/2/17
Y1 - 2006/2/17
N2 - The sarcoglycan-sarcospan complex (α-, β-, γ-, δ-, ε-, and ζ-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; γ- and δ-SG are also expressed in the sarcoplasmic reticulum (SR). In this study, we report the identification of a novel isoform of murine δ-SG produced by alternative splicing that we named δ-SG3. This isoform is present at transcript level in several tissues, with its highest expression in skeletal and cardiac muscle. The δ-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 δ-SG3 and the dihydropyridine receptor (DHPR) shows a close localization of these two proteins. We propose the subcellular distribution of this novel δ-SG3 isoform at the SR and its involvement in intracellular calcium concentration regulation.
AB - The sarcoglycan-sarcospan complex (α-, β-, γ-, δ-, ε-, and ζ-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; γ- and δ-SG are also expressed in the sarcoplasmic reticulum (SR). In this study, we report the identification of a novel isoform of murine δ-SG produced by alternative splicing that we named δ-SG3. This isoform is present at transcript level in several tissues, with its highest expression in skeletal and cardiac muscle. The δ-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 δ-SG3 and the dihydropyridine receptor (DHPR) shows a close localization of these two proteins. We propose the subcellular distribution of this novel δ-SG3 isoform at the SR and its involvement in intracellular calcium concentration regulation.
KW - Sarcoglycan-sarcospan complex
KW - Sarcoplasmic reticulum
KW - Skeletal muscle
KW - δ-Sarcoglycan isoform
UR - http://www.scopus.com/inward/record.url?scp=30144437402&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2005.12.083
DO - 10.1016/j.bbrc.2005.12.083
M3 - Artículo
SN - 0006-291X
VL - 340
SP - 865
EP - 871
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -