The α7β1 Integrin Mediates Adhesion and Migration of Skeletal Myoblasts on Laminin

Crawley, Suzanne C.; Farrell, Eleanor M.; Wang, Weigwang; Gu, M.; Huang, Hui‐Yu; Huynh, Vu; Hodges, Bradley L.; Cooper, Douglas N.W.; Kaufman, Stephen J.

doi:10.1006/excr.1997.3671

Cited by 64 publications

(58 citation statements)

References 62 publications

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“…In mouse, ADAM12 positively modulates expression of integrin ␣ 7 (Cao et al, 2003;Moghadaszadeh et al, 2003), which has functions in skeletal muscle development and disease (Burkin and Kaufman, 1999). ␣ 7 ␤ 1 integrin is mainly involved in mpc adhesion and migration on the matrix component laminin (Yao et al, 1996;Crawley et al, 1997;Blanco-Bose and Blau, 2001) and in myotendinous junction formation (Nawrotzki et al, 2003). Murine ␣ 7 ␤ 1 integrin can bind ADAM12 disintegrin and cysteinerich domain and induce cell adhesion (Zhao et al, 2004).…”

Section: Discussionmentioning

confidence: 99%

“…Recombinant full-length human ADAM12 (10 g/ml in coating buffer [6.22 g/l NaHCO 3 , 1.70 g/l Na 2 CO 3 , and H 2 O, pH 9.5]) and then saturated with 1% bovine serum albumin in PBS (37°C; 60 min). mpc were seeded (0.6 ϫ 10 6 cells/ml) and allowed to attach 60 min at 37°C in presence of Y9A2, mAb to ␣ 9 ␤ 1 (20 g/ml in Ham's-F12) or O26, monoclonal blocking antibody to ␣ 7 (20 g/ml; generous gift from S. J. Kaufman, University of Illinois, Urbana, IL) (Crawley et al, 1997). Controls were ensured by replacement of Y9A2 and O26 by normal IgG fraction (20 g/ml in Ham's-F12).…”

Section: Cell Adhesion Assaysmentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

Section: Cell Adhesion Assaysmentioning

confidence: 99%

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Lafuste

Sonnet

Chazaud

et al. 2005

MBoC

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“…Since migration of C2C12 cells was stimulated by induction of an activated form of R-Ras (Figure 4), R-Ras may stimulate fusion of myoblasts through increased motility by raising the frequency of cell ± cell adhesion and/or the eciency of cell alignment. Indeed, it has been reported that myotube formation can be inhibited by loss of integrin function, which is indispensable for myoblast migration (Menko and Boettinger, 1987;Rosen et al, 1992;Yao et al, 1996;Crawley et al, 1997;Rohwedel et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Positive regulation of skeletal myogenesis by R-Ras

2000

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Most of the proteins in the Ras-family proteins, including Ras, Rap and TC21, have been reported to be strong inhibitors of skeletal myogenesis. Here we show that R-Ras, another member of this family, promotes terminal dierentiation of C2C12 skeletal myoblasts. In contrast to Ras, which induced a markedly transformed phenotype of C2C12 cells, an activated mutant of R-Ras (R-Ras Q87L ) did not exhibit any inhibitory eect on the dierentiation of C2C12 cells, but enhanced the formation of multinucleated myotubes. Although R-Ras Q87L showed little eect on induction of two muscle-speci®c proteins, creatine kinase and myogenin, it prevented cell death during myoblast dierentiation, probably through Akt activation and Bcl-x L induction. Motility of C2C12 cells, which may be involved in fusion of myoblasts, was also stimulated by R-Ras Q87L. Furthermore, we observed a transient activation of endogenous R-Ras during dierentiation of C2C12 cells. The ectopic expression of R-Ras GAP inhibited the dierentiation. These results suggest that R-Ras has a positive eect on the terminal dierentiation of myoblasts and may be involved in the program of skeletal myogenesis.

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“…The laminin-binding ␣7␤1 integrin, expressed in mouse skeletal muscle as early as E10.5 d of development, mediates myoblast motility on laminin substrates (Kaufman et al, 1980;Kaufman et al, 1991;Yao et al, 1996a,b;Crawley et al, 1997;von der Mark et al, 2002). In mature skeletal muscle, the ␣7 receptor is associated with costameres and the myotendinous and neuromuscular junctions (Bao et al, 1993;Belkin et al, 1996;Martin et al, 1996;van der Flier et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

The β1 Cytoplasmic Domain Regulates the Laminin-binding Specificity of the α7X1 Integrin

Yeh

Ziober

Liu

et al. 2003

MBoC

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During muscle development, the laminin-specific ␣7 integrin is alternatively spliced in the putative ligand-binding domain to yield either the ␣7X1 or the ␣7X2 variant. The relative level of ␣7X1 and ␣7X2 is developmentally regulated. Similarly, the partner ␤1 integrin cytoplasmic domain is converted from the ␤1A to the ␤1D splice variant. To determine whether ␤1D modulates the activity of the ␣7 receptor, cells were transfected with ␣7X1 and ␤1D cDNA. ␣7X1 coupled with ␤1A failed to adhere to laminin-1, whereas cotransfectants expressing ␣7X1 and ␤1D showed strong adhesion. Interestingly, ␣7X1 complexed with ␤1A and ␤1D displayed the same level of poor adhesion to laminin-2/4 or strong adhesion to laminin-10/11. These findings indicate that ␣7 function is regulated not only by X1/X2 in its extracellular domain but also by ␤1 cytoplasmic splice variants. It is likely that expression of ␤1D alters ␣7X1 binding to laminin isoforms by a process related to ligand affinity modulation. Functional regulation of ␣7␤1 by developmentally regulated splicing events may be important during myogenic differentiation and repair because the integrin mediates adhesion, motility, and cell survival.

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The α7β1 Integrin Mediates Adhesion and Migration of Skeletal Myoblasts on Laminin

Cited by 64 publications

References 62 publications

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

Positive regulation of skeletal myogenesis by R-Ras

The β1 Cytoplasmic Domain Regulates the Laminin-binding Specificity of the α7X1 Integrin

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The α7β1 Integrin Mediates Adhesion and Migration of Skeletal Myoblasts on Laminin

Cited by 64 publications

References 62 publications

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

Positive regulation of skeletal myogenesis by R-Ras

The β1 Cytoplasmic Domain Regulates the Laminin-binding Specificity of the α7X1 Integrin

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation