Abstract
We studied the distribution of dystrophin at the sarcolemma of normal human muscle fibers using high resolution immunofluorescence and confocal laser scanning optical microscopy (CLSOM). We found that the dystrophin lattice is organized at the muscle plasma membrane in an array of thick bands interconnected by a finer network. The bands encircle the muscle fiber perpendicular to the long axis of the fiber and they matched the sites of attachment of the sarcomeres to the plasma membrane. Dystrophin co-localized with vinculin, and dystrophin and vinculin co-localized with alpha-actinin at the region of the I-band. Dystrophin may be one of the proteins involved in the linkage of the sarcomeres to the extracellular matrix.
| Original language | English |
|---|---|
| Pages (from-to) | 99-109 |
| Number of pages | 11 |
| Journal | Neuromuscular Disorders |
| Volume | 2 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1992 |
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Keywords
- costameres
- Dystrophin lattice
- extracellular matrix
- sarcomere-attachment
ASJC Scopus subject areas
- Clinical Neurology
- Pediatrics, Perinatology, and Child Health
- Developmental Neuroscience
- Neurology
Cite this
Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization. / Minetti, Carlo; Beltrame, Francesco; Marcenaro, Gianpiero; Bonilla, Eduardo.
In: Neuromuscular Disorders, Vol. 2, No. 2, 1992, p. 99-109.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dystrophin at the plasma membrane of human muscle fibers shows a costameric localization
AU - Minetti, Carlo
AU - Beltrame, Francesco
AU - Marcenaro, Gianpiero
AU - Bonilla, Eduardo
PY - 1992
Y1 - 1992
N2 - We studied the distribution of dystrophin at the sarcolemma of normal human muscle fibers using high resolution immunofluorescence and confocal laser scanning optical microscopy (CLSOM). We found that the dystrophin lattice is organized at the muscle plasma membrane in an array of thick bands interconnected by a finer network. The bands encircle the muscle fiber perpendicular to the long axis of the fiber and they matched the sites of attachment of the sarcomeres to the plasma membrane. Dystrophin co-localized with vinculin, and dystrophin and vinculin co-localized with alpha-actinin at the region of the I-band. Dystrophin may be one of the proteins involved in the linkage of the sarcomeres to the extracellular matrix.
AB - We studied the distribution of dystrophin at the sarcolemma of normal human muscle fibers using high resolution immunofluorescence and confocal laser scanning optical microscopy (CLSOM). We found that the dystrophin lattice is organized at the muscle plasma membrane in an array of thick bands interconnected by a finer network. The bands encircle the muscle fiber perpendicular to the long axis of the fiber and they matched the sites of attachment of the sarcomeres to the plasma membrane. Dystrophin co-localized with vinculin, and dystrophin and vinculin co-localized with alpha-actinin at the region of the I-band. Dystrophin may be one of the proteins involved in the linkage of the sarcomeres to the extracellular matrix.
KW - costameres
KW - Dystrophin lattice
KW - extracellular matrix
KW - sarcomere-attachment
UR - http://www.scopus.com/inward/record.url?scp=0026785988&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026785988&partnerID=8YFLogxK
U2 - 10.1016/0960-8966(92)90041-4
DO - 10.1016/0960-8966(92)90041-4
M3 - Article
C2 - 1422204
AN - SCOPUS:0026785988
VL - 2
SP - 99
EP - 109
JO - Neuromuscular Disorders
JF - Neuromuscular Disorders
SN - 0960-8966
IS - 2
ER -