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ADAMTS: Novel proteases expressed by activated mast cells

  • Gianni García-Faroldi EMAIL logo , Elin Rönnberg , Adolfo Orro , Gabriela Calounova , Bengt Guss , Anders Lundequist und Gunnar Pejler EMAIL logo
Veröffentlicht/Copyright: 8. Januar 2013
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 394 Heft 2

Abstract

Here we show that mast cells (MCs) express the metalloproteases of the Adisintegrin and metalloproteinase with thrombospondin motifs (ADAMTS) family, and that ADAMTS expression is influenced by MC activation. Co-culture of MCs with live Gram-positive bacteria caused a profound induction of ADAMTS-9 and -6, as well as down-regulated expression of ADAMTS-5. Similar patterns were also seen after MC activation with calcium ionophore and by immunoglobulin E receptor crosslinking. Moreover, ADAMTS-5, -6 and -9 were all induced by activation of terminally differentiated murine peritoneal MCs and in a human MC line. ADAMTS-9 up-regulation in response to immunoglobulin E receptor crosslinking was strongly dependent on Gö6976-sensitive protein kinase C and partly dependent on nuclear factor of activated T cells and nuclear factor kappa-light-chain-enhancer of activated B cells, respectively. The expression of ADAMTS-5, -6 and -9 was closely linked to MC maturation, as shown by their strong induction during the differentiation of bone marrow precursor cells into mature MCs. ADAMTS family members have been shown to possess aggrecanase activity. Accordingly, MCs were shown to express aggrecanase activity. Finally, ADAMTS-5 protein was detected in MCs by immunocytochemistry. Taken together, the present study reveals ADAMTS expression by MCs and that MC activation regulates the expression of these proteases, thus implicating the ADAMTS family of proteases in MC function.

Keywords: ADAMTS; aggrecanase; immunoglobulin E (IgE); mast cells; metalloproteases
Corresponding authors: Gianni García-Faroldi and Gunnar Pejler, Swedish University of Agricultural Sciences, Department of Anatomy, Physiology and Biochemistry, Uppsala, Sweden
Received: 2012-8-13
Accepted: 2012-11-8
Published Online: 2013-01-08
Published in Print: 2013-02-01

©2013 by Walter de Gruyter Berlin Boston

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  13. Melanoma resistance to photodynamic therapy: new insights
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  19. Cell Biology and Signaling
  20. Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
  21. Proteolysis
  22. ADAMTS: Novel proteases expressed by activated mast cells
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https://doi.org/10.1515/hsz-2012-0270
Schlagwörter für diesen Artikel
ADAMTS; aggrecanase; immunoglobulin E (IgE); mast cells; metalloproteases

Artikel in diesem Heft

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: The physiology and dynamics of cellular microcompartments
  5. Highlight: The Physiology and Dynamics of Cellular Microcompartments
  6. Cellular microcompartments constitute general suborganellar functional units in cells
  7. Dynamics of bioenergetic microcompartments
  8. Microcompartments within the yeast plasma membrane
  9. Plant cell microcompartments: a redox-signaling perspective
  10. Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
  11. Minireviews
  12. Beyond anemia: hepcidin, monocytes and inflammation
  13. Melanoma resistance to photodynamic therapy: new insights
  14. The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
  15. cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
  16. Research Articles/Short Communications
  17. Protein Structure and Function
  18. Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
  19. Cell Biology and Signaling
  20. Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
  21. Proteolysis
  22. ADAMTS: Novel proteases expressed by activated mast cells
  23. The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
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