Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature, and nervous system

Velling, Teet; Collo, Ginetta; Sorokin, Lydia; Durbeej, Madeleine; Zhang, Hongyan; Gullberg, Donald

doi:10.1002/(sici)1097-0177(199612)207:4<355::aid-aja1>3.0.co;2-g

Cited by 68 publications

(44 citation statements)

References 53 publications

(35 reference statements)

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“…Neither ␣1 nor ␣7 were detected in the embryo at this stage (not shown). The ␣1 expression pattern has not been described previously for these stages in the mouse, but the absence of ␣7 agrees with the detailed study of Velling et al (1996) who found ␣7 mRNA expression starting at E10.0/E10.5.…”

Section: Early (Primary) Myotome Formationsupporting

confidence: 90%

“…At approximately E10.5, expression of the ␣1 integrin subunit is clearly detected in the myotome (Fig. 1V,W), at a time that ␣7 is also up-regulated (not shown; Velling et al, 1996). This up-regulation of two new laminin receptors and the down-regulation of the early ␣6-containing laminin-receptor suggest that the myotomes are entering a new myogenic phase.…”

Section: Myotomal Growthmentioning

confidence: 91%

“…␣7 is not present in the mouse myotome when myogenin starts being expressed (see above), but its up-regulation coincides in time with the appearance of MyoD (Velling et al, 1996). Thus, we used double IHC for MyoD and the ␣7 subunit to determine whether these are expressed by the same cells in vivo.…”

Section: Myod-positive Cells Express Different Laminin Receptorsmentioning

confidence: 99%

“…Although the expression of the ␤1 (Pow and Hendrickx, 1995), ␣1 (Duband et al, 1992), ␣4 (Stepp et al, 1994), ␣6 (Bronner-Fraser et al, 1992Thorsteinsdó ttir et al, 1995;Pow and Hendrickx, 1995), and ␣7 (Velling et al, 1996) integrin subunits have been described in the myotome, it is not clear whether their expression patterns vary with the differentiation state of the myotomal cells and/or among the different regions of the myotome.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Early (Primary) Myotome Formationsupporting

confidence: 90%

Section: Myotomal Growthmentioning

confidence: 91%

Section: Myod-positive Cells Express Different Laminin Receptorsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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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“…Integrin ␣ 7 is mainly expressed in skeletal, smooth, and cardiac muscle (32), but also in some glioblastoma and melanoma cells (30,31) and in nervous tissue (32,33). The extracellular and the intracellular domains of integrin ␣ 7 undergo developmentally regulated splicing (34 -36); myoblasts express the cytoplasmic splice variant B and the extracellular splice variants X1 and…”

mentioning

confidence: 99%

The Integrin α7 Cytoplasmic Domain Regulates Cell Migration, Lamellipodia Formation, and p130CAS/Crk Coupling

Mielenz¹,

Hapke

Pöschl

et al. 2001

Journal of Biological Chemistry

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The integrin ␣ 7 ␤ 1 is the major laminin-binding integrin in skeletal, heart, and smooth muscle and is a receptor for laminin-1 and -2. It mediates myoblast migration on laminin-1 and -2 and thus might be involved in muscle development and repair. Previously we have shown that ␣ 7 B as well as the ␣ 7 A and -C splice variants induce cell motility on laminin when transfected into nonmotile HEK293 cells. In this study we have investigated the role of the cytoplasmic domain of ␣ 7 in the laminin-induced signal transduction of ␣ 7 ␤ 1 integrin regulating cell adhesion and migration. Deletion of the cytoplasmic domain did not affect assembly of the mutated ␣ 7 ⌬cyt/␤ 1 heterodimer on the cell surface or adhesion of ␣ 7 ⌬cyt-transfected cells to laminin. The motility of these cells on the laminin-1/E8 fragment, however, was significantly reduced to the level of mock-transfected cells; lamellipodia formation and polarization of the cells were also impaired. Adhesion to the laminin-1/E8 fragment induced tyrosine phosphorylation of the focal adhesion kinase, paxillin, and p130 CAS as well as the formation of a p130 CAS -Crk complex in wild-type ␣ 7 B-transfected cells. In ␣ 7 B⌬cyt cells, however, the extent of p130 CAS tyrosine formation was reduced and formation of the p130 CAS -Crk complex was impaired, with unaltered levels of p130 CAS and Crk protein levels. These findings indicate adhesion-dependent regulation of p130 CAS /Crk complex formation by the cytoplasmic domain of ␣ 7 B integrin after cell adhesion to laminin-1/E8 and imply ␣ 7 B-controlled lamellipodia formation and cell migration through the p130 CAS /Crk protein complex.During muscle repair, undifferentiated muscle precursor cells, so-called satellite cells, are activated and migrate to sites of damaged muscle along the basement membranes of preexisting muscle fibers to close the wound by proliferating and fusing (1, 2). In vitro, skeletal myoblasts have been shown to migrate on laminin (LN) 1 1 (3), the laminin-1-E8 fragment that is derived from laminin-1 by elastase digestion (4), and on laminin-2 (5), but not on fibronectin (4). The major component of muscle basement membranes supporting muscle cell migration is laminin-2 (6). The migration of fibroblast-like cells in culture involves polarization of cells, formation of filopodia, lamellipodia, stress fibers, and myosin-based contractility (7). Filopodia, lamellipodia and stress fiber formation are mediated by Cdc42, Rac, and Rho, respectively, which are members of the Rho family of small GTPases (8). Cdc42, Rac, and Rho can either be activated by soluble factors like growth factors, bioactive peptides, and hormones (8) or by integrins (9, 10), which can transduce signals from the extracellular matrix after clustering and ligand-induced conformational changes (11) in a hierarchical fashion (12). Several proteins become tyrosine-phosphorylated after integrin-mediated cell attachment. Those are, among others, the focal adhesion kinase (FAK) (13), the adaptor protein p130 CAS (Crk-associated Src substr...

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Spatial and temporal expression of the β1D integrin during mouse development

et al. 1997

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Distinct α7Aβ1 and α7Bβ1 integrin expression patterns during mouse development: α7A is restricted to skeletal muscle but α7B is expressed in striated muscle, vasculature, and nervous system

Cited by 68 publications

References 53 publications

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

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

The Integrin α7 Cytoplasmic Domain Regulates Cell Migration, Lamellipodia Formation, and p130CAS/Crk Coupling

Spatial and temporal expression of the β1D integrin during mouse development

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