Literature DB >> 30580156

Role of meprin metalloproteinases in cytokine processing and inflammation.

Christian Herzog1, Randy S Haun2, Gur P Kaushal3.   

Abstract

Meprin metalloendopeptidases, comprising α and β isoforms, are widely expressed in mammalian cells and organs including kidney, intestines, lungs, skin, and bladder, and in a variety of immune cells and cancer cells. Meprins proteolytically process many inflammatory mediators, including cytokines, chemokines, and other bioactive proteins and peptides that control the function of immune cells. The knowledge of meprin-mediated processing of inflammatory mediators and other target substrates provides a pathophysiologic link for the involvement of meprins in the pathogenesis of many inflammatory disorders. Meprins are now known to play important roles in inflammatory diseases including acute kidney injury, sepsis, urinary tract infections, bladder inflammation, and inflammatory bowel disease. The proteolysis of epithelial and endothelial barriers including cell junctional proteins by meprins promotes leukocyte influx into areas of tissue damage to result in inflammation. Meprins degrade extracellular matrix proteins; this ability of meprins is implicated in the cell migration of leukocytes and the invasion of tumor cells that express meprins. Proteolytic processing and maturation of procollagens provides evidence that meprins are involved in collagen maturation and deposition in the fibrotic processes involved in the formation of keloids and hypertrophic scars and lung fibrosis. This review highlights recent progress in understanding the role of meprins in inflammatory disorders in both human and mouse models.
Copyright © 2018 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  CCL2; IL-18; IL-1β; IL-6; IL-6R; Inflammation; Meprin A; Meprin α; Meprin β; Metalloproteinase

Year:  2018        PMID: 30580156      PMCID: PMC6414266          DOI: 10.1016/j.cyto.2018.11.032

Source DB:  PubMed          Journal:  Cytokine        ISSN: 1043-4666            Impact factor:   3.861


  88 in total

1.  Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity.

Authors:  G P Bertenshaw; B E Turk; S J Hubbard; G L Matters; J E Bylander; J M Crisman; L C Cantley; J S Bond
Journal:  J Biol Chem       Date:  2001-01-22       Impact factor: 5.157

Review 2.  Hypertrophic scarring and keloids: pathomechanisms and current and emerging treatment strategies.

Authors:  Gerd G Gauglitz; Hans C Korting; Tatiana Pavicic; Thomas Ruzicka; Marc G Jeschke
Journal:  Mol Med       Date:  2010-10-05       Impact factor: 6.354

3.  Actinonin, a meprin A inhibitor, protects the renal microcirculation during sepsis.

Authors:  Zhen Wang; Christian Herzog; Gur P Kaushal; Neriman Gokden; Philip R Mayeux
Journal:  Shock       Date:  2011-02       Impact factor: 3.454

4.  Nonpolarized secretion of human meprin alpha in colorectal cancer generates an increased proteolytic potential in the stroma.

Authors:  D Lottaz; C A Maurer; D Hahn; M W Büchler; E E Sterchi
Journal:  Cancer Res       Date:  1999-03-01       Impact factor: 12.701

5.  Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney.

Authors:  P E Butler; M J McKay; J S Bond
Journal:  Biochem J       Date:  1987-01-01       Impact factor: 3.857

Review 6.  Meprins, membrane-bound and secreted astacin metalloproteinases.

Authors:  Erwin E Sterchi; Walter Stöcker; Judith S Bond
Journal:  Mol Aspects Med       Date:  2008-08-22

7.  Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation.

Authors:  Sanjita Banerjee; Judith S Bond
Journal:  J Biol Chem       Date:  2008-09-11       Impact factor: 5.157

8.  Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1beta.

Authors:  Christian Herzog; Randy S Haun; Varsha Kaushal; Philip R Mayeux; Sudhir V Shah; Gur P Kaushal
Journal:  Biochem Biophys Res Commun       Date:  2009-01-07       Impact factor: 3.575

Review 9.  Interleukin 1 and interleukin 18 as mediators of inflammation and the aging process.

Authors:  Charles A Dinarello
Journal:  Am J Clin Nutr       Date:  2006-02       Impact factor: 7.045

10.  Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers.

Authors:  Greg P Bertenshaw; Mona T Norcum; Judith S Bond
Journal:  J Biol Chem       Date:  2002-10-23       Impact factor: 5.157

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  4 in total

1.  Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor.

Authors:  Charles Bayly-Jones; Christopher J Lupton; Claudia Fritz; Hariprasad Venugopal; Daniel Ramsbeck; Michael Wermann; Christian Jäger; Alex de Marco; Stephan Schilling; Dagmar Schlenzig; James C Whisstock
Journal:  Nat Commun       Date:  2022-10-19       Impact factor: 17.694

2.  Identification of MMP1 as a potential gene conferring erlotinib resistance in non-small cell lung cancer based on bioinformatics analyses.

Authors:  Huyue Zhou; Qiumei Xiang; Changpeng Hu; Jing Zhang; Qian Zhang; Rong Zhang
Journal:  Hereditas       Date:  2020-07-23       Impact factor: 3.271

3.  Differences in Shedding of the Interleukin-11 Receptor by the Proteases ADAM9, ADAM10, ADAM17, Meprin α, Meprin β and MT1-MMP.

Authors:  Martin Sammel; Florian Peters; Juliane Lokau; Franka Scharfenberg; Ludwig Werny; Stefan Linder; Christoph Garbers; Stefan Rose-John; Christoph Becker-Pauly
Journal:  Int J Mol Sci       Date:  2019-07-26       Impact factor: 5.923

4.  Meprin β expression modulates the interleukin-6 mediated JAK2-STAT3 signaling pathway in ischemia/reperfusion-induced kidney injury.

Authors:  Shaymaa Abousaad; Faihaa Ahmed; Ayman Abouzeid; Elimelda Moige Ongeri
Journal:  Physiol Rep       Date:  2022-09
  4 in total

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