Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy.

Vachon, Pierre H.; Xu, Hong; Liu, L; Loechel, Frosty; Hayashi, Yukiko; Arahata, Kiichi; Reed, John C.; Wewer, Ulla M.; Engvall, Eva

doi:10.1172/jci119716

Cited by 177 publications

(229 citation statements)

References 80 publications

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“…The role of integrins was also studied in Duchenne muscular dystrophy evidencing the detection of high levels of α7β1-integrin in order to compensate for the absence of dystrophin; these results reinforced the role played by integrins in the integrity and stability of skeletal muscle fibers (20).…”

Section: Introductionmentioning

confidence: 77%

Expression of muscle-specific integrins in masseter muscle fibers during malocclusion disease

Cutroneo

Piancino

Ramieri

et al. 2012

International Journal of Molecular Medicine

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Abstract.Integrins are heterodimeric cell surface membrane proteins linking the extracellular matrix to actin. α7B integrin is detected in proliferating and adult myofibers, whereas α7A plays a role in regenerating muscle fibers with a minor function in mature muscle fibers. The expression levels of β1A appear to be very low, whereas β1D appears to be the predominant integrin form in mature muscle. Considering the important features of masseter muscle we have studied integrin expression in masseter muscle specimens of surgical patients with posterior right crossbite and comparing them to left side masseter muscle specimens. Our results showed that the expression of integrins was significantly lower in the crossbite side muscle. Furthermore, the most important finding is that β1A is clearly detectable in adult masseter muscle. This behavior could be due to the particular composition of masseter, since it contains hybrid fibers showing the capacity to modify the contractile properties to optimize the energy efficiency or the action of the muscle during contraction. Moreover, masseter is characterized by a high turnover of muscle fibers producing a regeneration process. This may indicate a longer time to heal, justifying the loss of β1D and the consequential increase of β1A. Thus, our data provide the first suggestion that integrins in masseter muscle play a key role regulating the functional activity of muscle and allowing the optimization of contractile forces.

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Section: Introductionmentioning

confidence: 77%

Expression of muscle-specific integrins in masseter muscle fibers during malocclusion disease

Cutroneo

Piancino

Ramieri

et al. 2012

International Journal of Molecular Medicine

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“…Of these, the roles of the fibronectin receptor ␣5␤1 and the laminin receptor ␣7␤1 are the best studied. ␣5␤1 promotes proliferation and inhibits differentiation of myoblasts in vitro (Blaschuk and Holland, 1994;Boettiger et al, 1995;Sastry et al, 1996), whereas ␣7␤1 is thought to promote the maturation and survival of myotubes (Song et al, 1992;Vachon et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Integrins in the mouse myotome: Developmental changes and differences between the epaxial and hypaxial lineage

Bajanca

Luz

Duxson

et al. 2004

Developmental Dynamics

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Integrins are cellular adhesion receptors that mediate signaling and play key roles in the development of multicellular organisms. However, their role in the cellular events leading to myotome formation is completely unknown. Here, we describe the expression patterns of the ␣1, ␣4, ␣5, ␣6, and ␣7 integrin subunits in the mouse myotome and correlate them with the expression of several differentiation markers. Our results indicate that these integrin subunits may be differentially involved in the various phases of myogenic determination and differentiation. A detailed characterization of the myogenic cell types expressing the ␣4 and ␣6 subunits showed a regionalization of the myotome and dermomyotome based on cell-adhesion properties. We conclude that ␣6␤1 may be an early marker of epaxial myogenic progenitor cells. In contrast, ␣4␤1 is up-regulated in the intercalated myotome after myocyte differentiation. Furthermore, ␣4␤1 is expressed in the hypaxial dermomyotome and is maintained by early hypaxial myogenic progenitor cells colonizing the myotome. Developmental Dynamics 231:402-415, 2004.

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“…The distribution of ␣ 2 ␤ 1 was mainly restricted to the crypt while ␣ 3 ␤ 1 was found predominantly in the villus (35,36). More recently, ␣ 7 B␤ 1 , a spe-cific laminin receptor largely involved in muscle development in response to laminin (37) has been identified in the intestinal epithelium. It was found to be located at the crypt-villus junction in the intact intestine while its expression was transiently up-regulated in differentiating enterocytes (38).…”

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confidence: 99%

Expression of Functionally Distinct Variants of the β4A Integrin Subunit in Relation to the Differentiation State in Human Intestinal Cells

Basora¹,

Herring-Gillam

Boudreau³

et al. 1999

Journal of Biological Chemistry

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Integrins are important mediators of cell-laminin interactions. In the small intestinal epithelium, which consists of spatially separated proliferative and differentiated cell populations located, respectively, in the crypt and on the villus, laminins and laminin-binding integrins are differentially expressed along the cryptvillus axis. One exception to this is the integrin ␣ 6 ␤ 4 , which is thought to be ubiquitously expressed by intestinal cells. However, in this study, a re-evaluation of the ␤ 4 subunit expression with different antibodies revealed that two forms of ␤ 4 exist in the human intestinal epithelium. Furthermore, we show that differentiated enterocytes express a full-length 205-kDa ␤ 4 A subunit, whereas undifferentiated crypt cells express a novel ␤ 4 A subunit that does not contain the COOH-terminal segment of the cytoplasmic domain (␤ 4 A ctd؊ ). This new form was not found to arise from alternative ␤ 4 mRNA splicing. Moreover, we found that these two ␤ 4 A forms can associate into ␣ 6 ␤ 4 A complexes; however, the ␤ 4 A ctd؊ integrin expressed by the undifferentiated crypt cells is not functional for adhesion to laminin-5. Hence, these studies identify a novel ␣ 6 ␤ 4 A ctd؊ integrin expressed in undifferentiated intestinal crypt cells that is functionally distinct.

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Integrins (alpha7beta1) in muscle function and survival. Disrupted expression in merosin-deficient congenital muscular dystrophy.

Cited by 177 publications

References 80 publications

Expression of muscle-specific integrins in masseter muscle fibers during malocclusion disease

Expression of muscle-specific integrins in masseter muscle fibers during malocclusion disease

Integrins in the mouse myotome: Developmental changes and differences between the epaxial and hypaxial lineage

Expression of Functionally Distinct Variants of the β4A Integrin Subunit in Relation to the Differentiation State in Human Intestinal Cells

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