Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques, and the myotendinous and neuromuscular junctions of skeletal muscle

Turner, Christopher E.; Kramarcy, Neal R.; Sealock, Robert; Burridge, Keith

doi:10.1016/0014-4827(91)90090-h

Cited by 97 publications

(69 citation statements)

References 20 publications

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“…A number of proteins are reported to be specifically expressed or to show increased levels at the MTJs (Law et al 1994;Jarvinen et al 2003;Welser et al 2009). Consistent with previous reports (Turner et al 1991;Frenette and Tidball 1998;Koch et al 2004), we confirmed paxillin, talin, and collagen XXII localization to the muscle side of the MTJs. In addition, we have shown for the first time increased accumulation of PRG4 and Eln at the MTJs of young rats, as well as accumulation of SDF1, CTGF, and TGFb1 at the MTJs.…”

Section: Discussionsupporting

confidence: 93%

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Age-related changes in structure and extracellular matrix protein expression levels in rat tendons

Kostrominova

Brooks

2013

AGE

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The musculoskeletal system (muscle-tendonbone) demonstrates numerous age-related changes, with modifications in tendons the least well studied, although increased predisposition to tendinopathy and rupture have been reported. In order to gain insights into the basis of age-associated increase in tendon injuries, we compared Achilles and tibialis anterior tendons and myotendinous junctions (MTJs) from 3-to 5-and 22-to 25-month-old rats for underlying structure and composition. Significant decreases were observed by qRT-PCR for collagen I, III, and V mRNA expression in tendons of old rats, but immunostaining detected no apparent differences in collagen I and V expression on the protein level. Tendons of old compared with young rats had decreased mRNA expression levels of proteoglycan 4 (PRG4) and elastin (Eln), but no differences in the mRNA expression of connective tissue growth factor, TGF-beta 1, or stromal cell-derived factor 1. For PRG4, immunostaining showed good correlation with qRT-PCR results. This is the first study to show reductions in PRG4 in tendons and MTJs of old rats. Decreased PRG4 expression in tendons could result in increased tendon stiffness and may be associated with decreased activity in the elderly. The diminished collagen mRNA expression in combination with decreased PRG4 and Eln mRNA expression may be associated with increased risk of tendon injury with aging.

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Section: Discussionsupporting

confidence: 93%

“…Paxillin, talin, and collagen XXII also showed localization to the muscle side of the MTJs (arrows in Supplemental Fig. 1) consistent with previous reports (Turner et al 1991;Frenette and Tidball 1998;Koch et al 2004). …”

Section: Expression Levels Of Extracellular Matrix (Ecm) Proteins Consupporting

confidence: 90%

Age-related changes in structure and extracellular matrix protein expression levels in rat tendons

Kostrominova

Brooks

2013

AGE

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“…Focal adhesions are elongated in morphology and reside in both central and peripheral regions of the cell, and are generally found at the ends of actin filament bundles. Analogous adhesion structures have been observed in vivo in endothelial cells (Kano et al 1996), skeletal muscle myotendinous junctions (Turner et al 1991), and neuronal growth cones (Cypher and Letourneau 1991), and highly elongated adhesions have also been reported in vivo (Cukierman et al 2001).…”

Section: Focal Adhesionssupporting

confidence: 62%

Integrins in Cell Migration

Chan

Cortesio

Huttenlocher

2007

Methods in Enzymology

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Integrin-based adhesion has served as a model for studying the central role of adhesion in migration. In this article, we outline modes of migration, both integrin-dependent and -independent in vitro and in vivo. We next discuss the roles of adhesion contacts as signaling centers and linkages between the ECM and actin that allows adhesions to serve as traction sites. This includes signaling complexes that regulate migration and the interplay among adhesion, signaling, and pliability of the substratum. Finally, we address mechanisms of adhesion assembly and disassembly and the role of adhesion in cellular polarity.

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“…Indeed, both the structural and regulatory proteins including paxillin, FAK, vinculin, etc. are highly enriched in the dense plaques of smooth muscle tissue (280), the intercalated discs of cardiac muscle, and the myotendinous junctions of skeletal muscle (280).…”

Section: Integrin-actin Linkages and Muscle Contractionmentioning

confidence: 99%

Paxillin: Adapting to Change

Brown¹,

Turner²

2004

Physiological Reviews

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551

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Molecular scaffold or adaptor proteins facilitate precise spatiotemporal regulation and integration of multiple signaling pathways to effect the optimal cellular response to changes in the immediate environment. Paxillin is a multidomain adaptor that recruits both structural and signaling molecules to focal adhesions, sites of integrin engagement with the extracellular matrix, where it performs a critical role in transducing adhesion and growth factor signals to elicit changes in cell migration and gene expression.

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Localization of paxillin, a focal adhesion protein, to smooth muscle dense plaques, and the myotendinous and neuromuscular junctions of skeletal muscle

Cited by 97 publications

References 20 publications

Age-related changes in structure and extracellular matrix protein expression levels in rat tendons

Age-related changes in structure and extracellular matrix protein expression levels in rat tendons

Integrins in Cell Migration

Paxillin: Adapting to Change

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