Document Detail


Structure and composition of tubular aggregates of skeletal muscle fibres.
MedLine Citation:
PMID:  15113116     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Unusual regions of densely packed membranous tubules known as tubular aggregates (TAs) have been observed in skeletal muscle fibres of mammals under numerous pathological conditions but also in health. Their causality is unclear. It is neither known whether TAs are destructive and should be treated or whether they have a compensating function in an endangered muscle. In spite of many similarities, the histochemical, immunocytochemical and ultrastructural characteristics of tubular aggregates do vary. Histochemistry provided an overall characteristic of TAs as membranous inclusions with a variety of enzymatic activities. Immunocytochemical evidence revealed that tubular aggregates contain miscellaneous proteins and that derive from membranes of sarcoplasmic reticulum and mitochondria. No evidence for the presence of contractile and cytoskeletal proteins in TAs was found. Ultrastructurally, TAs are characterized as more or less densely packed aggregates of vesicular or tubular membranes of variable forms and sizes that may contain amorphous material, filaments or inner tubules. Various reported types of tubular aggregates, namely, proliferating terminal cisterns, vesicular membrane collections, TAs with double-walled tubules, TAs with single-walled tubules, aggregates of dilated tubules with inner tubules, aggregates of tubulo-filamentous structures, filamentous tubules, riesentubuli, and related membranous structures including cylindrical spirals are sumarized and analyzed here in detail.
Authors:
M Pavlovicová; M Novotová; I Zahradník
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  General physiology and biophysics     Volume:  22     ISSN:  0231-5882     ISO Abbreviation:  Gen. Physiol. Biophys.     Publication Date:  2003 Dec 
Date Detail:
Created Date:  2004-04-28     Completed Date:  2004-08-24     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  8400604     Medline TA:  Gen Physiol Biophys     Country:  Slovakia    
Other Details:
Languages:  eng     Pagination:  425-40     Citation Subset:  IM    
Affiliation:
Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, Bratislava, Slovakia.
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MeSH Terms
Descriptor/Qualifier:
Animals
Humans
Microtubules / metabolism*,  ultrastructure*
Mitochondria / metabolism,  ultrastructure
Muscle Fibers, Skeletal / metabolism*,  ultrastructure*
Muscle Proteins / metabolism*
Muscle, Skeletal / metabolism*,  ultrastructure*
Myopathies, Structural, Congenital / metabolism,  pathology
Chemical
Reg. No./Substance:
0/Muscle Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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