cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components.
By Alain Colige, Shi-wu Li, Aleksander L. Sieron, Betty Nusgens, D. J. Prockop, C. LaPierre. 1997
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- M. Bekhouche
- Zena Werb
- A. Colige
- A. Forlino
- Frédéric Kesteloot
- W. A. Cabral
- C. Deroanne
- Aileen M. Barnes
Citations in the corpus
- Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans (2007, background): “…and in the pericellular space, and mature collagen molecules self-assemble into heterotypic fibrils with other matrix proteins [Ayad et al., 1998; Chakravarti et al., 1998; Colige et al., 1997; Font et al., 1998; Kyriakides et al., 1998; Prockop et al., 1993; Scott, 1988; Svensson et al., 1999].”
- Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases. (2000, background): “To see whether papilin interacts with a papilin cassette-containing metalloproteinase we chose procollagen N-proteinase, the only available purified ADAMTS metalloproteinase with specific, known substrate: procollagen I (Colige et al., 1997; Leung et al., 1979; Prockop et al., 1998).”
- ADAMTS-2 functions as anti-angiogenic and anti-tumoral molecule independently of its catalytic activity (2010, background): “Among the other members of the ADAMTS family, ADAMTS-2 is one of the best characterized [17, 18].”
- The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology. (2015, background): “High expression of ADAMTS2 is detected in all type I collagen-rich tissues from fetal calf such as skin, bones, tendons and aorta, which supports its importance for type I collagen maturation [7].”
- A Disintegrin and Metalloproteinase with Thrombospondin Motifs 18 Deficiency Leads to Visceral Adiposity and Associated Metabolic Syndrome in Mice. (2017, background): “…and ovulation (ADAMTS1) 16 ; angiogenesis inhibition (ADAMTSs 1, 8, and 9) 17,18 ; degradation of cartilage oligomeric matrix protein (ADAMTSs 7 and 12) 19 ; cleavage of the matrix proteoglycan aggrecan, versican, and brevican (ADAMTSs 1, 4, 5, 8, 9, and 15) 20 e 23 ; and cleavage of ultralarge e…”
- How matrix metalloproteinases regulate cell behavior. (2001, background): “…et al. 1999); ADAMTS-2, which is a procollagen amino-propeptidase that is required for the proper assembly of fibrillar collagens I and II (Colige et al. 1997); and ADAMTS-4 and ADAMTS-5/11 (aggrecanases 1 and 2, respectively), which can degrade the cartilage proteoglycan aggrecan…”