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Editorial

ADAMTS7: a promising new therapeutic target in coronary heart disease

, MD MRCP & , MD PhD FRCPath
Pages 863-867 | Published online: 06 Jul 2013

Figures & data

Figure 1. Schematic representation of the ADAMTS7 protein (see text). The terminal TS motif domain is the site for cartilage oligomeric matrix protein (COMP) and granulin-epithelin precursor (GEP) binding.

Figure 1. Schematic representation of the ADAMTS7 protein (see text). The terminal TS motif domain is the site for cartilage oligomeric matrix protein (COMP) and granulin-epithelin precursor (GEP) binding.

Figure 2. Proposed mechanism of ADAMTS7 mediates vascular smooth muscle cell (VSMC) migration. Activated ADAMTS7 cleaves cartilage oligomeric matrix protein (COMP), thereby removing its inhibitory effect on VSMC. Sites of pathway regulation are displayed in red text.

Figure 2. Proposed mechanism of ADAMTS7 mediates vascular smooth muscle cell (VSMC) migration. Activated ADAMTS7 cleaves cartilage oligomeric matrix protein (COMP), thereby removing its inhibitory effect on VSMC. Sites of pathway regulation are displayed in red text.

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