TY - JOUR
T1 - Developmental and tissue-specific regulation of a novel dysferlin isoform
AU - Salani, Sabrina
AU - Lucchiari, Sabrina
AU - Fortunato, Francesco
AU - Crimi, Marco
AU - Corti, Stefania
AU - Locatelli, Federica
AU - Bossolasco, Patrizia
AU - Bresolin, Nereo
AU - Comi, Giacomo Pietro
PY - 2004/9
Y1 - 2004/9
N2 - Dysferlin plays an essential role in the muscle repair machinery, and its deficiency is associated with limb-girdle muscular dystrophy type 2B and with two different distal myopathies (Miyoshi myopathy and distal anterior compartment myopathy). Our aims were to characterize the pattern of dysferlin expression during myogenic cell differentiation and to assess possible differentially spliced isoforms of the DYSF gene. Human primary myogenic cells express a splice variant of dysferlin mRNA lacking exon 17 (A17), together with full-length dysferlin mRNA. Real-time polymerase chain reaction analysis of human myoblasts, myotubes, and normal skeletal muscle showed that A17 expression inversely correlates with muscle differentiation. Indeed, A17 is progressively replaced by the wild type as myoblast fusion proceeds, and it disappears in adult skeletal muscle. Conversely, A17 is the predominant dysferlin variant in mature peripheral nerve. Our findings suggest that the two proteins play different roles in myogenic cell differentiation and that dysferlin function in peripheral nerve might be accomplished by this novel isoform.
AB - Dysferlin plays an essential role in the muscle repair machinery, and its deficiency is associated with limb-girdle muscular dystrophy type 2B and with two different distal myopathies (Miyoshi myopathy and distal anterior compartment myopathy). Our aims were to characterize the pattern of dysferlin expression during myogenic cell differentiation and to assess possible differentially spliced isoforms of the DYSF gene. Human primary myogenic cells express a splice variant of dysferlin mRNA lacking exon 17 (A17), together with full-length dysferlin mRNA. Real-time polymerase chain reaction analysis of human myoblasts, myotubes, and normal skeletal muscle showed that A17 expression inversely correlates with muscle differentiation. Indeed, A17 is progressively replaced by the wild type as myoblast fusion proceeds, and it disappears in adult skeletal muscle. Conversely, A17 is the predominant dysferlin variant in mature peripheral nerve. Our findings suggest that the two proteins play different roles in myogenic cell differentiation and that dysferlin function in peripheral nerve might be accomplished by this novel isoform.
KW - Bidimensional electrophoresis
KW - Differentiation
KW - Dysferlinopathy
KW - Myoblast
KW - Splicing mechanism
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U2 - 10.1002/mus.20106
DO - 10.1002/mus.20106
M3 - Article
C2 - 15318348
AN - SCOPUS:4243139484
VL - 30
SP - 366
EP - 374
JO - Muscle and Nerve
JF - Muscle and Nerve
SN - 0148-639X
IS - 3
ER -