ADAMs and cell fusion

Huovila, Ari; Almeida, Eduardo; White, Judith M.

doi:10.1016/s0955-0674(96)80111-6

Cited by 132 publications

(76 citation statements)

References 43 publications

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“…The disintegrin domain might thus be considered as a structural feature rather than an integrin ligand. The carboxy-terminal end is composed of a cystein-rich domain involved in cell-cell fusion [18], an EGF-like domain, a transmembrane domain and a cytoplasmic tail containing phosphorylation sites and SH3 binding domains [19]. At least 40 ADAMs have been described, 25 of which are expressed in Homo Sapiens.…”

Section: Structural Features Of Adams and Adamtssmentioning

confidence: 99%

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

et al. 2008

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A disintegrin and metalloproteinases (ADAMs) are a recently discovered family of proteins that share the metalloproteinase domain with matrix metalloproteinases (MMPs). Among this family, structural features distinguish the membrane-anchored ADAMs and the secreted ADAMs with thrombospondin motifs referred to as ADAMTSs. By acting on a large panel of membrane-associated and extracellular substrates, they control several cell functions such as adhesion, fusion, migration and proliferation. The current review addresses the contribution of these proteinases in the positive and negative regulation of cancer progression as mainly mediated by the regulation of growth factor activities and integrin functions.

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Section: Structural Features Of Adams and Adamtssmentioning

confidence: 99%

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

et al. 2008

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“…Genetic screens and biochemical analyses have identified many proteins involved in muscle cell fusion located at the cell surface, in the cytoplasm, and in the nucleus (reviewed in Dworak and Sink, 2002;Taylor, 2002). The membrane proteins implicated in myotube formation in vertebrates include ␤1 integrin, ADAM12 (a member of a disintegrin and metalloproteinase family), NCAM, and M-cadherin (Rosen et al, 1992;Zeschnigk et al, 1995;Fazeli et al, 1996;Huovila et al, 1996;Charlton et al, 2000;Schwander et al, 2003). M-cadherin belongs to the cadherin family of calcium-dependent adhesion molecules.…”

Section: Introductionmentioning

confidence: 99%

RhoA GTPase Regulates M-Cadherin Activity and Myoblast Fusion

Charrasse

Comunale

Grumbach

et al. 2006

MBoC

121

131

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The Rho family of GTP-binding proteins plays critical roles during myogenesis induction. To elucidate their role later during myogenesis, we have analyzed RhoA function during myoblast fusion into myotubes. We find that RhoA activity is rapidly and transiently increased when cells are shifted into differentiation medium and then is decreased until myoblast fusion. RhoA activity must be down-regulated to allow fusion, because expression of a constitutively active form of RhoA (RhoAV14) inhibits this process. RhoAV14 perturbs the expression and localization of M-cadherin, a member of the Ca 2؉ -dependent cell-cell adhesion molecule family that has an essential role in skeletal muscle cell differentiation. This mutant does not affect N-cadherin and other proteins involved in myoblast fusion, ␤1-integrin and ADAM12. Active RhoA induces the entry of M-cadherin into a degradative pathway and thus decreases its stability in correlation with the monoubiquitination of M-cadherin. Moreover, p120 catenin association with M-cadherin is decreased in RhoAV14-expressing cells, which is partially reverted by the inhibition of the RhoA effector Rho-associated kinase ROCK. ROCK inhibition also restores M-cadherin accumulation at the cell-cell contact sites. We propose that the sustained activation of the RhoA pathway inhibits myoblast fusion through the regulation of p120 activity, which controls cadherin internalization and degradation.

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“…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).…”

mentioning

confidence: 99%

“…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 in most mammalian cell fusion processes, including ADAM1, 2, and 3 in fertilization (Blobel et al, 1992;Huovila et al, 1996;Wolfsberg and White, 1996;Hooft, 1998) and ADAM12 in osteoclast (Abe et al, 1999;Choi et al, 2001) and macrophage-derived multinucleated giant cell formation (Abe et al, 1999), in trophoblast syncytialization (Huovila et al, 1996;Gilpin et al, 1998;Shi et al, 2000), and in myogenesis (Yagami-Hiromasa et al, 1995).Several ADAMs are expressed by adult and developing skeletal muscles, including ADAM1, 4, 9, and 15 that are ubiquitous, and ADAM12, also called meltrin-␣, whose expression is less widespread (Yagami-Hiromasa et al, 1995;Loechel et al, 2000;Kratzschmar et al, 1996;Weskamp et al, 1996;Kurisaki et al, 1998). In rodents, constitutive muscle expression of ADAM12 starts at the embryonic stage when myotubes are formed (Kurisaki et al, 1998), persists at the neonatal stage (Yagami-Hiromasa et al, 1995;Borneman et al, 2000;Kronqvist et al, 2002), and ceases in adulthood (Borneman et al, 2000;Kronqvist et al, 2002).…”

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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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ADAMs and cell fusion

Cited by 132 publications

References 43 publications

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

RhoA GTPase Regulates M-Cadherin Activity and Myoblast Fusion

ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation

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ADAMs and cell fusion

Cited by 132 publications

References 43 publications

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

Emerging roles of ADAM and ADAMTS metalloproteinases in cancer

RhoA GTPase Regulates M-Cadherin Activity and Myoblast Fusion

ADAM12 and α9β1Integrin Are Instrumental in Human Myogenic Cell Differentiation

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ADAM12 and α₉β₁Integrin Are Instrumental in Human Myogenic Cell Differentiation