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Rouille Y, Duguay SJ, Lund K, Furuta M, Gong Q, Lipkind G, Oliva AA Jr, Chan SJ, Steiner DF: Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Frontiers Neuroendocrinol 1995, 16:322-361.
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The glycosylation of human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) is important for the efficient intracellular transport of the envelope precursor gp160
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Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg Gl: Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 1995, 270:5331-5338.
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Atkinson SJ, Crabbe T, Cowell S, Ward RV, Butler MJ, Sato H, Seiki M, Reynolds JJ, Murphy G: Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes. J Biol Chem 1995, 270:30479-30485. This study shows that MT-MMP-1 is inhibited far less efficiently by TIMP-1 than it is by TIMP-2. As TIMP-2 is expressed constitutively, whereas the expression of TIMP-1 is regulated, the finding of differential inhibition implies that MT-MMP-1 may be active in cell surface proteolysis even in the presence of high concentrations of TIMP-1.
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Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinoma
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Okada A, Bellocq J-P, Rouyer N, Chenard M-P, Rio M-C, Chambon P, Basset P: Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinoma. Proc Natl Acad Sei USA 1996, 92:2730-2734.
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Kessler E, Takahara K, Biniaminov L, Brusel M, Greenspan DS: Bone morphogenetic protein-1 : the type I procollagen C-proteinase. Science 1996, 271:360-362. This study shows that the carboxy-terminal propeptide of procollagen is a substrate for mammalian BMP-1 /tolloid, a protein necessary for development in Drosophila. The data, therefore, link ECM regulation with development via this astacin family metalloproteinase.
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Ac, S.1
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VDIPEN, a metalloproteinase-generated neoepitope, is induced and immunolocalized in articular cartilage during inflammatory arthritis
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Science
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Wei, Y.1
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Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and -dependent pathways
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Lund LR, Romer J, Thomasset N, Solberg H, Pike C, Bissell MJ, Dano K, Werb Z: Two distinct phases of apoptosis in mammary gland involution: proteinase-independent and -dependent pathways. Development 1996, 122:181-193. This study shows that proteinases produced by stromal cells degrade the basement membrane underlying mammary epithelial cells, inducing the apoptotic death of the epithelial cells during involution. Thus, this proteolytic process is a specialized mesenchymal-epithelial interaction that regulates cell differentiation, function and viability.
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Development
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Lund, L.R.1
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Upregulation of the 72-kDa type IV collagenase in epithelial and stromal cells during rat tracheal gland morphogenesis
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Lim M, EKman F, Dohrman A, Cunha G, Basbaum C: Upregulation of the 72-kDa type IV collagenase in epithelial and stromal cells during rat tracheal gland morphogenesis. Dev Biol 1995, 171:521-530. This paper shows that the cells at the leading edge of invading tracheal gland epithelia express gelatinase A. Therefore, even in an environment in which the stromal cells express large quantities of this proteinase, local proteolysis by the growing tip of the epithelium may be important.
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Lim, M.1
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Impaired wound healing in mice with a disrupted plasminogen gene
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Romer J, Bugge TH, Pike C, Lund LR, Flick MJ, Degen JL, Dano K: Impaired wound healing in mice with a disrupted plasminogen gene. Nat Med 1996, 2:287-292. This study shows that plasminogen-null mice display a profound defect in wound healing. In the absence of this proteinase, keratinocytes fail to migrate and proliferate to cover the area of injury. Although the mechanism underlying the defective keratinocyte function has not been elucidated, the data suggest that proteolysis of the provisional fibrin matrix is required. These data point to a critical role for plasminogen, and, by inference, plasminogen activators, in wound repair.
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Nat Med
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Romer, J.1
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Pike, C.3
Lund, L.R.4
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Extracellular matrixdependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction
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Roskelley CD, Desprez PY, Bissell MJ: Extracellular matrixdependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction. Proc Natl Acad Sei USA 1994, 91:12378-12382.
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Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression
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Sympson CJ, Talhouk RS, Alexander CM, Chin JR, Clift SM, Bissell MJ, Werb Z; Targeted expression of stromelysin-1 in mammary gland provides evidence for a role of proteinases in branching morphogenesis and the requirement for an intact basement membrane for tissue-specific gene expression. J CellBiol 1994, 125:681-693.
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J CellBiol
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Boudreau N, Sympson CJ, Werb Z, Bissell MJ: Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix Science 1995, 267:891-893.
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Science
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0029896682
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Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
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Alexander CM, Hansell EJ, Behrendtsen O, Rannery ML, Kishnani NS, Hawkes SP, Werb Z: Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 1996, 122:1723-1736. This study shows that regulation of TIMP-3 underlies the programmed cell death of maternal decidua during implantation. The authors also used TIMP-1 transgenic mice to demonstrate the requirement for MMPs in decidua for growth and angiogenesis at the maternal-fetal interface. These data give the first direct insight into MMP action during a normal invasive event.
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Development
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Alexander, C.M.1
Hansell, E.J.2
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