Literature DB >> 8748144

Neutrophil proteinases and matrix degradation. The cell biology of pericellular proteolysis.

C A Owen1, E J Campbell.   

Abstract

Neutrophil proteinases have the capacity to degrade almost every component of the extracellular matrix. In marked contrast to the wealth of available data about the structure and activity of these proteinases when they are free in solution, there has been relatively little information about the mechanisms by which neutrophils use and control their proteolytic enzymes in an extracellular milieu that is replete with proteinase inhibitors. However, recent data have provided insights into several mechanisms that permit these enzymes to evade inhibition: (1) compartmentalization; (2) localized inactivation of proteinase inhibitors; (3) tight binding of enzymes to substrates; and (4) binding of proteinases to the neutrophil's cell surface.

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Year:  1995        PMID: 8748144     DOI: 10.1016/s1043-4682(05)80007-8

Source DB:  PubMed          Journal:  Semin Cell Biol        ISSN: 1043-4682


  13 in total

1.  Sequence-specific binding of normal serum immunoglobulin M to exposed protein C-termini.

Authors:  Alex V Sokoloff; Marissa Puckett; James J Ludtke; Bryan Fetterly
Journal:  Immunology       Date:  2004-06       Impact factor: 7.397

Review 2.  Neutrophil serine proteases fine-tune the inflammatory response.

Authors:  Christine T N Pham
Journal:  Int J Biochem Cell Biol       Date:  2007-11-29       Impact factor: 5.085

3.  Cleavage of native type I collagen by human neutrophil elastase.

Authors:  W Kafienah; D J Buttle; D Burnett; A P Hollander
Journal:  Biochem J       Date:  1998-03-01       Impact factor: 3.857

4.  The 1.8 A crystal structure of human cathepsin G in complex with Suc-Val-Pro-PheP-(OPh)2: a Janus-faced proteinase with two opposite specificities.

Authors:  P Hof; I Mayr; R Huber; E Korzus; J Potempa; J Travis; J C Powers; W Bode
Journal:  EMBO J       Date:  1996-10-15       Impact factor: 11.598

5.  Effect of plant neutrophil elastase inhibitor on leucocyte migration, adhesion and cytokine release in inflammatory conditions.

Authors:  C Oliveira; R A Navarro-Xavier; E A Anjos-Vallota; J O Martins; V L F Silveira; L R C Gonçalves; M S Araújo; G Motta; P Sannomiya; M L V Oliva
Journal:  Br J Pharmacol       Date:  2010-10       Impact factor: 8.739

6.  Converting enzyme-independent release of tumor necrosis factor alpha and IL-1beta from a stimulated human monocytic cell line in the presence of activated neutrophils or purified proteinase 3.

Authors:  C Coeshott; C Ohnemus; A Pilyavskaya; S Ross; M Wieczorek; H Kroona; A H Leimer; J Cheronis
Journal:  Proc Natl Acad Sci U S A       Date:  1999-05-25       Impact factor: 11.205

7.  A BODIPY-Tagged Phosphono Peptide as Activity-Based Probe for Human Leukocyte Elastase.

Authors:  Anna-Christina Schulz-Fincke; Michael Blaut; Annett Braune; Michael Gütschow
Journal:  ACS Med Chem Lett       Date:  2018-03-04       Impact factor: 4.345

Review 8.  Research Progress on the Immunogenicity and Regeneration of Acellular Adipose Matrix: A Mini Review.

Authors:  Kaiyang Liu; Yunfan He; Feng Lu
Journal:  Front Bioeng Biotechnol       Date:  2022-06-06

9.  Venular basement membranes ubiquitously express matrix protein low-expression regions: characterization in multiple tissues and remodeling during inflammation.

Authors:  Mathieu-Benoît Voisin; Doris Pröbstl; Sussan Nourshargh
Journal:  Am J Pathol       Date:  2009-12-11       Impact factor: 4.307

10.  A critical 'threshold' of beta 2-integrin engagement regulates augmentation of cytokine-mediated superoxide anion release.

Authors:  Trevor R Walker; Marie-Helene Ruchaud-Sparagano; Sarah R McMeekin; Ian Dransfield
Journal:  Br J Pharmacol       Date:  2004-03-08       Impact factor: 8.739

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