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Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair : Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades
Joint Authors
Wilkins-Port, Cynthia E.
Higgins, Craig E.
Higgins, Stephen P.
Higgins, Paul J.
Kobori-Hotchkiss, Issey
Source
Biochemistry Research International
Issue
Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-8, 8 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-02-20
Country of Publication
Egypt
No. of Pages
8
Main Subjects
Abstract EN
Spatial and temporal regulation of the pericellular proteolytic environment by local growth factors, such as EGF and TGF-β, initiates a wide repertoire of cellular responses coupled to a plasmin/matrix metalloproteinase (MMP) dependent stromal-remodeling axis.
Cell motility and invasion, tumor metastasis, wound healing, and organ fibrosis, for example, represent diverse events controlled by expression of a subset of genes that encode various classes of tissue remodeling proteins.
These include members of the serine protease and MMP families that functionally constitute a complex system of interacting protease cascades and titrated by their respective inhibitors.
Several structural components of the extracellular matrix are upregulated by TGF-β as are matrix-active proteases (e.g., urokinase (uPA), plasmin, MMP-1, -3, -9, -10, -11, -13, -14).
Stringent controls on serine protease/MMP expression and their topographic activity are essential for maintaining tissue homeostasis.
Targeting individual elements in this highly interactive network may lead to novel therapeutic approaches for the treatment of cancer, fibrotic diseases, and chronic wounds.
American Psychological Association (APA)
Wilkins-Port, Cynthia E.& Higgins, Stephen P.& Higgins, Craig E.& Kobori-Hotchkiss, Issey& Higgins, Paul J.. 2012. Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair : Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades. Biochemistry Research International،Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-472868
Modern Language Association (MLA)
Wilkins-Port, Cynthia E.…[et al.]. Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair : Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades. Biochemistry Research International No. 2012 (2012), pp.1-8.
https://search.emarefa.net/detail/BIM-472868
American Medical Association (AMA)
Wilkins-Port, Cynthia E.& Higgins, Stephen P.& Higgins, Craig E.& Kobori-Hotchkiss, Issey& Higgins, Paul J.. Complex Regulation of the Pericellular Proteolytic Microenvironment during Tumor Progression and Wound Repair : Functional Interactions between the Serine Protease and Matrix Metalloproteinase Cascades. Biochemistry Research International. 2012. Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-472868
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-472868