Integrins: Redundant or Important Players in Skeletal Muscle?

Mayer, Ulrike

doi:10.1074/jbc.r200022200

Cited by 168 publications

(148 citation statements)

References 80 publications

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“…In vertebrates, it is α7β1D that is required for the maintenance of adult muscles. The α7β1 integrin is a laminin receptor and loss of either the α7 subunit or its ligand laminin 2/4 leads to congenital muscular dystrophy in human patients as well as in mice [96][97][98][99].…”

Section: Skeletal Musclementioning

confidence: 99%

Integrins in regulation of tissue development and function

Danen¹,

Sonnenberg²

2003

The Journal of Pathology

229

173

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Cell adhesion is indispensable for embryonic development and for proper tissue function. In metazoans, integrins are the major adhesion receptors that connect cells to components of the extracellular matrix. Integrins are implicated in assembly of extracellular matrices, cell adhesion and migration on extracellular matrices, and in vertebrates (in which the integrin family has expanded) they can also mediate cell-cell adhesion. Furthermore, integrinmediated adhesion can modulate many different signal transduction cascades and support cell survival, proliferation, and influence the expression of differentiation-related genes. In this review we briefly explain how integrins can affect so many different aspects of cell behavior and discuss evidence for roles of integrins in tissue development, function, and disease.

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Section: Skeletal Musclementioning

confidence: 99%

Integrins in regulation of tissue development and function

Danen¹,

Sonnenberg²

2003

The Journal of Pathology

229

173

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“…Laminin-2 forms polymers through the short arm regions, and this laminin network adheres to the plasma membrane through the laminin globular domain in the a2-chain (Colognato and Yurchenco 2000). DG and integrin are well-characterized receptors of laminin-2 Mayer 2003). A major class of congenital muscular dystrophy (MDC1A) is caused by mutations in the LAMA2 gene that encodes the laminin a2-chain (Helbling- Leclerc et al 1995).…”

Section: Extracellular Matrix Proteins and Receptorsmentioning

confidence: 99%

The genetic and molecular basis of muscular dystrophy: roles of cell–matrix linkage in the pathogenesis

2006

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Muscular dystrophies are a heterogeneous group of genetic disorders. In addition to genetic information, a combination of various approaches such as the use of genetic animal models, muscle cell biology, and biochemistry has contributed to improving the understanding of the molecular basis of muscular dystrophy's etiology. Several lines of evidence confirm that the structural linkage between the muscle extracellular matrix and the cytoskeleton is crucial to prevent the progression of muscular dystrophy. The dystrophin-glycoprotein complex links the extracellular matrix to the cytoskeleton, and mutations in the component of this complex cause Duchenne-type or limb-girdle-type muscular dystrophy. Mutations in laminin or collagen VI, muscle matrix proteins, are known to cause a congenital type of muscular dystrophy. Moreover, it is not only the primary genetic defects in the structural or matrix proteins, but also the primary mutations of enzymes involved in the protein glycosylation pathway that are now recognized to disrupt the matrix-cell interaction in a certain group of muscular dystrophies. This group of diseases is caused by the secondary functional defects of dystroglycan, a transmembrane matrix receptor. This review considers recent advances in understanding the molecular pathogenesis of muscular dystrophies that can be caused by the disruption of the cell-matrix linkage.

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“…Unlike ␣ 4 ␤ 1 , an integrin closely related to ␣ 9 ␤ 1 and expressed by differentiating myogenic cells (Rosen et al, 1992), the role of ␣ 9 ␤ 1 in postnatal myogenesis has not been investigated (Mayer, 2003) despite previous mention of its expression at onset of myotube formation in the mouse embryo (Wang et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

“…The integrin ␣ 9 subunit forms a single heterodimer ␣ 9 ␤ 1 (Palmer et al, 1993). Thus, this integrin constitutes a choice candidate as a privileged partner of ADAM12 during postnatal mpc fusion process (White, 2003).Unlike ␣ 4 ␤ 1 , an integrin closely related to ␣ 9 ␤ 1 and expressed by differentiating myogenic cells (Rosen et al, 1992), the role of ␣ 9 ␤ 1 in postnatal myogenesis has not been investigated (Mayer, 2003) despite previous mention of its expression at onset of myotube formation in the mouse embryo (Wang et al, 1995).In the present article, we show that both ADAM12 and ␣ 9 integrin are constitutively expressed during human myogenic cell differentiation and mediate a cell-cell interaction selectively involved in fusion of mononucleated myoblasts to preformed myotubes. …”

mentioning

confidence: 99%

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Lafuste

Sonnet

Chazaud

et al. 2005

MBoC

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Knowledge on molecular systems involved in myogenic precursor cell (mpc) fusion into myotubes is fragmentary. Previous studies have implicated the a disintegrin and metalloproteinase (ADAM) family in most mammalian cell fusion processes. ADAM12 is likely involved in fusion of murine mpc and human rhabdomyosarcoma cells, but it requires yet unknown molecular partners to launch myogenic cell fusion. ADAM12 was shown able to mediate cell-to-cell attachment through binding ␣ 9 ␤ 1 integrin. We report that normal human mpc express both ADAM12 and ␣ 9 ␤ 1 integrin during their differentiation. Expression of ␣ 9 parallels that of ADAM12 and culminates at time of fusion. ␣ 9 and ADAM12 coimmunoprecipitate and participate to mpc adhesion. Inhibition of ADAM12/␣ 9 ␤ 1 integrin interplay, by either ADAM12 antisense oligonucleotides or blocking antibody to ␣ 9 ␤ 1 , inhibited overall mpc fusion by 47-48%, with combination of both strategies increasing inhibition up to 62%. By contrast with blockade of vascular cell adhesion molecule-1/␣ 4 ␤ 1 , which also reduced fusion, exposure to ADAM12 antisense oligonucleotides or anti-␣ 9 ␤ 1 antibody did not induce detachment of mpc from extracellular matrix, suggesting specific involvement of ADAM12-␣ 9 ␤ 1 interaction in the fusion process. Evaluation of the fusion rate with regard to the size of myotubes showed that both ADAM12 antisense oligonucleotides and ␣ 9 ␤ 1 blockade inhibited more importantly formation of large (>5 nuclei) myotubes than that of small (2-4 nuclei) myotubes. We conclude that both ADAM12 and ␣ 9 ␤ 1 integrin are expressed during postnatal human myogenic differentiation and that their interaction is mainly operative in nascent myotube growth. INTRODUCTIONAdult skeletal muscle regeneration after injury results from activation, proliferation, and fusion of mononucleated myogenic precursor cells (mpc) (Hawke and Garry, 2001). The mpc fusion results from an ordered sequence of events, including clustering and alignment of cells, establishment of close cell-to-cell contacts, and plasma membrane merging (Doberstein et al., 1997;Taylor, 2003). Various membrane proteins have been implicated in myotube formation, including N-and M-cadherins, neural cell adhesion molecule (NCAM), and vascular cell adhesion molecule (VCAM), ␣ 4 ␤ 1 and other integrins, and a disintegrin and metalloproteinases (ADAMs) (Abmayr et al., 2003). ADAMs form a family of Ͼ30 transmembrane glycoproteins with a unique domain organization, including a prodomain, a proteolytic domain (metalloprotease), an adhesion integrin-binding site formed by both disintegrin and cysteine-rich domains, an epidermal growth factor-like domain, a transmembrane domain, and a signaling cytoplasmic tail (Huovila et al., 1996;Primakoff and Myles, 2002;White, 2003). In addition, some ADAMs contain a hydrophobic sequence in a cysteine-rich region that may represent a fusion peptide, suggesting that this subclass of ADAMs might participate to plasma membrane merging (Huovila et al., 1996). Some ADAMs have been implicated i...

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Integrins: Redundant or Important Players in Skeletal Muscle?

Cited by 168 publications

References 80 publications

Integrins in regulation of tissue development and function

Integrins in regulation of tissue development and function

The genetic and molecular basis of muscular dystrophy: roles of cell–matrix linkage in the pathogenesis

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

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Integrins: Redundant or Important Players in Skeletal Muscle?

Cited by 168 publications

References 80 publications

Integrins in regulation of tissue development and function

Integrins in regulation of tissue development and function

The genetic and molecular basis of muscular dystrophy: roles of cell–matrix linkage in the pathogenesis

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation