Localization of dystrophin and β-spectrin in vacuolar myopathies

Jan L. De Bleecker, Andrew G Engel, John C. Winkelmann

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

We examined the expression of the cytoskeletal proteins dystrophin and β- spectrin on vacuolar boundaries in vacuolar myopathies. We also localized utrophin, a dystrophin homologue, and laminin, which served as a marker for the basal lamina. Four types of vacuoles were identified. Type 1 vacuoles, found in all diseases, were lined by laminin, dystrophin, and β-spectrin and arose from infoldings of the basal lamina and sarcolemma into splitting or branching fibers. Type 2 vacuoles were lined by dystrophin and β-spectrin and were most common in adult acid maltase deficiency, chloroquine myopathy, and periodic paralysis. Traces of utrophin were also noted on the boundaries of some type 2 vacuoles, but only in those fibers that also expressed utrophin on their surface membrane. Type 3 vacuoles were lined by small patches of dystrophin and β-spectrin and occurred in any vacuolar myopathy. Type 4 vacuoles were unlined by any of the above antigens and were most common in infantile acid maltase deficiency and in the nonlysosomal glycogenoses. Immunoelectron microscopy confirmed the dystrophin label on vacuolar boundaries but revealed no reaction product on any other membranous component within the muscle fiber. We conclude that dystrophin and β- spectrin provide cytoskeletal support for a species of membrane-bound vacuoles in diverse myopathies.

Original languageEnglish (US)
Pages (from-to)1200-1208
Number of pages9
JournalAmerican Journal of Pathology
Volume143
Issue number4
StatePublished - 1993

Fingerprint

Spectrin
Dystrophin
Vacuoles
Utrophin
Glycogen Storage Disease Type II
Laminin
Muscular Diseases
Basement Membrane
Glycogen Storage Disease
Sarcolemma
Cytoskeletal Proteins
Membranes
Immunoelectron Microscopy
Chloroquine
Vacuolar myopathy
Paralysis
Antigens
Muscles

ASJC Scopus subject areas

  • Pathology and Forensic Medicine

Cite this

Localization of dystrophin and β-spectrin in vacuolar myopathies. / De Bleecker, Jan L.; Engel, Andrew G; Winkelmann, John C.

In: American Journal of Pathology, Vol. 143, No. 4, 1993, p. 1200-1208.

Research output: Contribution to journalArticle

De Bleecker, JL, Engel, AG & Winkelmann, JC 1993, 'Localization of dystrophin and β-spectrin in vacuolar myopathies', American Journal of Pathology, vol. 143, no. 4, pp. 1200-1208.
De Bleecker, Jan L. ; Engel, Andrew G ; Winkelmann, John C. / Localization of dystrophin and β-spectrin in vacuolar myopathies. In: American Journal of Pathology. 1993 ; Vol. 143, No. 4. pp. 1200-1208.
@article{dc14ddea3757478ab460fa2823900d29,
title = "Localization of dystrophin and β-spectrin in vacuolar myopathies",
abstract = "We examined the expression of the cytoskeletal proteins dystrophin and β- spectrin on vacuolar boundaries in vacuolar myopathies. We also localized utrophin, a dystrophin homologue, and laminin, which served as a marker for the basal lamina. Four types of vacuoles were identified. Type 1 vacuoles, found in all diseases, were lined by laminin, dystrophin, and β-spectrin and arose from infoldings of the basal lamina and sarcolemma into splitting or branching fibers. Type 2 vacuoles were lined by dystrophin and β-spectrin and were most common in adult acid maltase deficiency, chloroquine myopathy, and periodic paralysis. Traces of utrophin were also noted on the boundaries of some type 2 vacuoles, but only in those fibers that also expressed utrophin on their surface membrane. Type 3 vacuoles were lined by small patches of dystrophin and β-spectrin and occurred in any vacuolar myopathy. Type 4 vacuoles were unlined by any of the above antigens and were most common in infantile acid maltase deficiency and in the nonlysosomal glycogenoses. Immunoelectron microscopy confirmed the dystrophin label on vacuolar boundaries but revealed no reaction product on any other membranous component within the muscle fiber. We conclude that dystrophin and β- spectrin provide cytoskeletal support for a species of membrane-bound vacuoles in diverse myopathies.",
author = "{De Bleecker}, {Jan L.} and Engel, {Andrew G} and Winkelmann, {John C.}",
year = "1993",
language = "English (US)",
volume = "143",
pages = "1200--1208",
journal = "American Journal of Pathology",
issn = "0002-9440",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Localization of dystrophin and β-spectrin in vacuolar myopathies

AU - De Bleecker, Jan L.

AU - Engel, Andrew G

AU - Winkelmann, John C.

PY - 1993

Y1 - 1993

N2 - We examined the expression of the cytoskeletal proteins dystrophin and β- spectrin on vacuolar boundaries in vacuolar myopathies. We also localized utrophin, a dystrophin homologue, and laminin, which served as a marker for the basal lamina. Four types of vacuoles were identified. Type 1 vacuoles, found in all diseases, were lined by laminin, dystrophin, and β-spectrin and arose from infoldings of the basal lamina and sarcolemma into splitting or branching fibers. Type 2 vacuoles were lined by dystrophin and β-spectrin and were most common in adult acid maltase deficiency, chloroquine myopathy, and periodic paralysis. Traces of utrophin were also noted on the boundaries of some type 2 vacuoles, but only in those fibers that also expressed utrophin on their surface membrane. Type 3 vacuoles were lined by small patches of dystrophin and β-spectrin and occurred in any vacuolar myopathy. Type 4 vacuoles were unlined by any of the above antigens and were most common in infantile acid maltase deficiency and in the nonlysosomal glycogenoses. Immunoelectron microscopy confirmed the dystrophin label on vacuolar boundaries but revealed no reaction product on any other membranous component within the muscle fiber. We conclude that dystrophin and β- spectrin provide cytoskeletal support for a species of membrane-bound vacuoles in diverse myopathies.

AB - We examined the expression of the cytoskeletal proteins dystrophin and β- spectrin on vacuolar boundaries in vacuolar myopathies. We also localized utrophin, a dystrophin homologue, and laminin, which served as a marker for the basal lamina. Four types of vacuoles were identified. Type 1 vacuoles, found in all diseases, were lined by laminin, dystrophin, and β-spectrin and arose from infoldings of the basal lamina and sarcolemma into splitting or branching fibers. Type 2 vacuoles were lined by dystrophin and β-spectrin and were most common in adult acid maltase deficiency, chloroquine myopathy, and periodic paralysis. Traces of utrophin were also noted on the boundaries of some type 2 vacuoles, but only in those fibers that also expressed utrophin on their surface membrane. Type 3 vacuoles were lined by small patches of dystrophin and β-spectrin and occurred in any vacuolar myopathy. Type 4 vacuoles were unlined by any of the above antigens and were most common in infantile acid maltase deficiency and in the nonlysosomal glycogenoses. Immunoelectron microscopy confirmed the dystrophin label on vacuolar boundaries but revealed no reaction product on any other membranous component within the muscle fiber. We conclude that dystrophin and β- spectrin provide cytoskeletal support for a species of membrane-bound vacuoles in diverse myopathies.

UR - http://www.scopus.com/inward/record.url?scp=0027813494&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027813494&partnerID=8YFLogxK

M3 - Article

VL - 143

SP - 1200

EP - 1208

JO - American Journal of Pathology

JF - American Journal of Pathology

SN - 0002-9440

IS - 4

ER -