Regular ArticleDisintegrin-like/Cysteine-Rich Region of ADAM 12 Is an Active Cell Adhesion Domain
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Cited by (52)
The puzzle of proteolytic effects in hemorrhage induced by Viperidae snake venom metalloproteinases
2021, Proteolytic Signaling in Health and DiseaseActing on identity: Myoblast fusion and the formation of the syncytial muscle fiber
2017, Seminars in Cell and Developmental BiologyA disintegrin and metalloproteinase-12 (ADAM12): Function, roles in disease progression, and clinical implications
2013, Biochimica et Biophysica Acta - General SubjectsCitation Excerpt :This binding to C2C12 myoblasts proceeds via the disintegrin-like and cysteine-rich domains of ADAM12. Although they share structural homology with the P-III class of snake venom metalloproteases (SVMPs) [23], they lack the commonly associated RGD integrin-binding motif responsible for binding to structures in the vasculature [24]. Iba et al., further observed that ADAM12 binds to primary murine osteoblasts, fibroblastic cells, osteoblastic cells, and myoblastic cells during the well plate assay in which these cells were seeded to the pre-attached rADAM12 [25].
Drosophila metalloproteases in development and differentiation: The role of ADAM proteins and their relatives
2011, European Journal of Cell BiologyCitation Excerpt :While the prodomain is considered to be involved in protein folding and in the regulation of activity (Suzuki et al., 1998), the intracellular domain is apparently required for proper trafficking of these proteins (Cao et al., 2002). The disintegrin-like domain, on the other hand, is known to interact with integrins, thereby mediating cell adhesion (Zolkiewska, 1999) and the ACR domain was reported to be involved in homo-oligomerization (Meyer et al., 2010). With respect to Kuzbanian, the zygotic loss of the active form of the protein results in a dramatic excess of cardiomyocytes in the Drosophila heart, which affects all subtypes of these cells, e.g., the tinman and the seven-up expressing cells.
The disintegrin and metalloprotease Meltrin from Drosophila forms oligomers via its protein binding domain and is regulated by the homeobox protein VND during embryonic development
2010, Insect Biochemistry and Molecular BiologyCitation Excerpt :The disintegrin-like, cysteine rich and EGF-like domains on the other hand are considered to be the site of protein-protein interaction. In this context especially the disintegrin-like domain is known to interact with integrins and thereby mediates cell adhesion (Zolkiewska, 1999). In mice, the ADAM protein Meltrin β was shown to be expressed in the peripheral nervous system, skeletal muscles, bones and in the embryonic heart (Kurisaki et al., 1998; Yagami-Hiromasa et al., 1995).
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Correspondence and reprint requests may be addressed to the author at Department of Biochemistry, Kansas State University, 104 Willard Hall, Manhattan, KS 66506. Fax: (785) 532-7278. E-mail: [email protected].