Literature DB >> 8939664

Focalized proteolysis: spatial and temporal regulation of extracellular matrix degradation at the cell surface.

C B Basbaum1, Z Werb.   

Abstract

Cells respond to changes in their microenvironment by altering their cell surface and extracellular matrix proteins. Rapid and irreversible changes in these proteins are possible through their degradation or activation by proteolysis. By focalizing the proteolytic events at or near the cell surface, these processes can be effective even in the presence of high concentrations of inhibitors. Evidence is emerging that secreted and transmembrane matrix metalloproteinases, metalloproteinases of the adamalysin and astacin (tolloid) families, and serine proteinases are crucial in development, differentiation, cell motility and invasion, and cell-extracellular decisions.

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Year:  1996        PMID: 8939664     DOI: 10.1016/s0955-0674(96)80116-5

Source DB:  PubMed          Journal:  Curr Opin Cell Biol        ISSN: 0955-0674            Impact factor:   8.382


  66 in total

1.  Spatiotemporal expression patterns of metalloproteinases and their inhibitors in the postnatal developing rat cerebellum.

Authors:  C Vaillant; M Didier-Bazès; A Hutter; M F Belin; N Thomasset
Journal:  J Neurosci       Date:  1999-06-15       Impact factor: 6.167

Review 2.  Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules.

Authors:  G E Davis; K J Bayless; M J Davis; G A Meininger
Journal:  Am J Pathol       Date:  2000-05       Impact factor: 4.307

3.  Oscillatory behavior of a simple kinetic model for proteolysis during cell invasion.

Authors:  H Berry; V Larreta-Garde
Journal:  Biophys J       Date:  1999-08       Impact factor: 4.033

4.  Type VIII collagen stimulates smooth muscle cell migration and matrix metalloproteinase synthesis after arterial injury.

Authors:  G Hou; D Mulholland; M A Gronska; M P Bendeck
Journal:  Am J Pathol       Date:  2000-02       Impact factor: 4.307

5.  TGF-beta3-induced palatogenesis requires matrix metalloproteinases.

Authors:  L Blavier; A Lazaryev; J Groffen; N Heisterkamp; Y A DeClerck; V Kaartinen
Journal:  Mol Biol Cell       Date:  2001-05       Impact factor: 4.138

6.  Enzyme-catalyzed gel proteolysis: an anomalous diffusion-controlled mechanism.

Authors:  G C Fadda; D Lairez; B Arrio; J-P Carton; V Larreta-Garde
Journal:  Biophys J       Date:  2003-11       Impact factor: 4.033

7.  Fibronectin-alpha4beta1 integrin interactions regulate metalloproteinase-9 expression in steatotic liver ischemia and reperfusion injury.

Authors:  Carolina Moore; Xiu-Da Shen; Feng Gao; Ronald W Busuttil; Ana J Coito
Journal:  Am J Pathol       Date:  2007-02       Impact factor: 4.307

8.  Alpha4beta1 integrin/ligand interaction inhibits alpha5beta1-induced stress fibers and focal adhesions via down-regulation of RhoA and induces melanoma cell migration.

Authors:  Jose V Moyano; Alfredo Maqueda; Benito Casanova; Angeles Garcia-Pardo
Journal:  Mol Biol Cell       Date:  2003-05-18       Impact factor: 4.138

9.  Release of matrix metalloproteinase-8 during physiological trafficking and induced mobilization of human hematopoietic stem cells.

Authors:  Carolin Steinl; Mike Essl; Thomas D Schreiber; Konstanze Geiger; Lea Prokop; Stefan Stevanović; Oliver Pötz; Harald Abele; Johannes T Wessels; Wilhelm K Aicher; Gerd Klein
Journal:  Stem Cells Dev       Date:  2013-02-12       Impact factor: 3.272

10.  Fibronectin fragmentation is a feature of periodontal disease sites and diabetic foot and leg wounds and modifies cell behavior.

Authors:  Corey M Stanley; Yao Wang; Sanjay Pal; Robert J Klebe; Lawrence B Harkless; Xiaoping Xu; Zhihua Chen; Bjorn Steffensen
Journal:  J Periodontol       Date:  2008-05       Impact factor: 6.993

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