2001
DOI: 10.1006/excr.2000.5069
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MMP-2 Colocalizes with Caveolae on the Surface of Endothelial Cells

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Cited by 164 publications
(125 citation statements)
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“…39 Among these interactions, the binding between MMP-7 and CD44HSPG is different from other combinations in that MMP-7 interacts with sulfated glycosaminoglycan chains of CD44HSPG but not with its core protein, 16 whereas other MMPs associate with their binding molecules through a protein-protein interaction. [36][37][38][39] Thus, our data in Promatrilysin-1 activation through interaction with CD151 T Shiomi et al the present study demonstrate for the first time that proMMP-7 also binds to CD151 through a proteinprotein interaction. ProMMP-7 is composed of PP and catalytic domains, 3 and CD151 comprises four transmembrane domains, two extracellular and one intracellular loops, and NH 2 -and COOH-terminal intracytoplasmic domains.…”
Section: Discussionsupporting
confidence: 61%
“…39 Among these interactions, the binding between MMP-7 and CD44HSPG is different from other combinations in that MMP-7 interacts with sulfated glycosaminoglycan chains of CD44HSPG but not with its core protein, 16 whereas other MMPs associate with their binding molecules through a protein-protein interaction. [36][37][38][39] Thus, our data in Promatrilysin-1 activation through interaction with CD151 T Shiomi et al the present study demonstrate for the first time that proMMP-7 also binds to CD151 through a proteinprotein interaction. ProMMP-7 is composed of PP and catalytic domains, 3 and CD151 comprises four transmembrane domains, two extracellular and one intracellular loops, and NH 2 -and COOH-terminal intracytoplasmic domains.…”
Section: Discussionsupporting
confidence: 61%
“…However, from what is currently known from other studies, caveolin-1 may serve as an important intercellular signalling molecule that is capable of potentiating the progression, invasiveness and vascularisation of renal tumours. In support of this hypothesis, caveolin-1 is shown to interact and potentiate the activity of metalloproteinases (Puyraimond et al, 2001) and the urokinase receptor (Stahl and Mueller, 1995;Wei et al, 1999) in a variety of cell types, leading to activation of cell surface plasminogen, and generation of plasmin, which in turn leads to the overall degradation of extracellular matrices. Recently, Lisanti and co-workers (Liu et al, 2002) have shown that, within an in vitro model of angiogenesis, the direct delivery of caveolin-1-derived peptides to the cytoplasm of endothelial cells is sufficient to induce capillary tubule formation.…”
Section: Discussionmentioning
confidence: 87%
“…For example, within caveolae the annexin II tetramer (AIIt) forms a putative tumor-cell membrane receptor for procatB at the cell surface (Mai et al, 2000;Sloane et al, 2005). Moreover, other proteases, such as urokinase plasminogen activator (uPA) and its receptor uPAR and the matrix metalloproteases MMP-2 and MT1-MMP (Annabi et al, 2001;Puyraimond et al, 2001), have been localized to caveolae at the level of the tumor cell surface. Sloane et al (2005) have hypothesized that interactions of procatB with the annexin II tetramer, through direct binding to p11, facilitate activation of procatB and in turn tumor progression by initiating a proteolytic cascade involving remodeling proteases.…”
Section: Discussionmentioning
confidence: 99%