title: Distribution and localization of vinculin-talin-integrin system and dystrophin-glycoprotein complex in human skeletal muscle. Immunohistochemical study using confocal laser scanning microscopy.
abstract: The vinculin-talin-integrin system and the dystrophin-glycoprotein complex (DGC) are two protein systems with structural and signaling functions, allowing interaction between muscle fibers and extracellular matrix. Although numerous studies have been conducted on these systems, their localization and distribution patterns along the nonjunctional sarcolemma are not clear. On this basis, we carried out an indirect immunofluorescence study on the vastus lateralis muscle of human adults not affected by neuromuscular diseases to better define these patterns. Our results showed that all tested proteins of the two systems have a costameric distribution; all tested proteins of the two systems colocalize with each other (about 90-95% of the cases); only alpha-sarcoglycan in a few cases (about 6%) does not colocalize with other proteins; in about 9-10% of the cases, dystrophin and beta-dystroglycan colocalize partially with other proteins; all tested proteins can be localized in different fibers, both in the region of the sarcolemma over I or A bands. The colocalization between the vinculin-talin-integrin and DGC systems may imply their functional interaction involving the structural aspect, by providing a stronger adhesion between sarcolemma and extracellular matrix in well-defined regions of the muscle fiber. Besides, their colocalization may suggest the existence of a mechanism of mutual modulation of the transmitted signals. This reciprocal control may determine, in different conditions, the prevalence of one system over another with a consequent transmission of different messages to the sarcolemma-associated cytoskeleton.
authors.affiliation: Department of Biomorphology and Biotechnologies, University of Messina, Messina, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Anastasi
authors.forename: A
authors.initials: A
authors.lastname: Amato
authors.forename: G
authors.initials: G
authors.lastname: Tarone
authors.forename: G
authors.initials: G
authors.lastname: Vita
authors.forename: M C
authors.initials: MC
authors.lastname: Monici
authors.forename: L
authors.initials: L
authors.lastname: Magaudda
authors.forename: M
authors.initials: M
authors.lastname: Brancaccio
authors.forename: A
authors.initials: A
authors.lastname: Sidoti
authors.forename: F
authors.initials: F
authors.lastname: Trimarchi
authors.forename: A
authors.initials: A
authors.lastname: Favaloro
authors.forename: G
authors.initials: G
authors.lastname: Cutroneo
mesh_terms: D016189:Dystrophin / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D006801:Humans; D007150:Immunohistochemistry; D016023:Integrins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D018613:Microscopy, Confocal; D018482:Muscle, Skeletal / Q000737:chemistry / Q000166:cytology / Q000378:metabolism*; D012508:Sarcolemma / Q000737:chemistry; D016608:Talin / Q000378:metabolism*; D016596:Vinculin / Q000378:metabolism*
chemical_list: D016189:Dystrophin; D016023:Integrins; D008562:Membrane Glycoproteins; D016608:Talin; D016596:Vinculin