Importance of mast cell Prss31/transmembrane tryptase/tryptase-γ in lung function and experimental chronic obstructive pulmonary disease and colitis.
Hansbro, PM
Hamilton, MJ
Fricker, M
Gellatly, SL
Jarnicki, AG
Zheng, D
Frei, SM
Wong, GW
Hamadi, S
Zhou, S
Foster, PS
Krilis, SA
Stevens, RL
- Publisher:
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Publication Type:
- Journal Article
- Citation:
- The Journal of biological chemistry, 2014, 289, (26), pp. 18214-18227
- Issue Date:
- 2014-06
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Importance of mast cell Prss31 Transmembrane tryptase -tryptase in lung function and experimental COPD and Colitis.pdf | Published version | 3.5 MB | Adobe PDF |
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Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Hansbro, PM | |
dc.contributor.author | Hamilton, MJ | |
dc.contributor.author | Fricker, M | |
dc.contributor.author | Gellatly, SL | |
dc.contributor.author | Jarnicki, AG | |
dc.contributor.author | Zheng, D | |
dc.contributor.author | Frei, SM | |
dc.contributor.author | Wong, GW | |
dc.contributor.author | Hamadi, S | |
dc.contributor.author | Zhou, S | |
dc.contributor.author | Foster, PS | |
dc.contributor.author | Krilis, SA | |
dc.contributor.author | Stevens, RL | |
dc.date.accessioned | 2021-03-04T01:01:40Z | |
dc.date.available | 2021-03-04T01:01:40Z | |
dc.date.issued | 2014-06 | |
dc.identifier.citation | The Journal of biological chemistry, 2014, 289, (26), pp. 18214-18227 | |
dc.identifier.issn | 0021-9258 | |
dc.identifier.issn | 1083-351X | |
dc.identifier.uri | http://hdl.handle.net/10453/146748 | |
dc.description.abstract | Protease serine member S31 (Prss31)/transmembrane tryptase/tryptase-γ is a mast cell (MC)-restricted protease of unknown function that is retained on the outer leaflet of the plasma membrane when MCs are activated. We determined the nucleotide sequences of the Prss31 gene in different mouse strains and then used a Cre/loxP homologous recombination approach to create a novel Prss31(-/-) C57BL/6 mouse line. The resulting animals exhibited no obvious developmental abnormality, contained normal numbers of granulated MCs in their tissues, and did not compensate for their loss of the membrane tryptase by increasing their expression of other granule proteases. When Prss31-null MCs were activated with a calcium ionophore or by their high affinity IgE receptors, they degranulated in a pattern similar to that of WT MCs. Prss31-null mice had increased baseline airway reactivity to methacholine but markedly reduced experimental chronic obstructive pulmonary disease and colitis, thereby indicating both beneficial and adverse functional roles for the tryptase. In a cigarette smoke-induced model of chronic obstructive pulmonary disease, WT mice had more pulmonary macrophages, higher histopathology scores, and more fibrosis in their small airways than similarly treated Prss31-null mice. In a dextran sodium sulfate-induced acute colitis model, WT mice lost more weight, had higher histopathology scores, and contained more Cxcl-2 and IL-6 mRNA in their colons than similarly treated Prss31-null mice. The accumulated data raise the possibility that inhibitors of this membrane tryptase may provide additional therapeutic benefit in the treatment of humans with these MC-dependent inflammatory diseases. | |
dc.format | Print-Electronic | |
dc.language | eng | |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
dc.relation.ispartof | The Journal of biological chemistry | |
dc.relation.isbasedon | 10.1074/jbc.m114.548594 | |
dc.rights | info:eu-repo/semantics/closedAccess | |
dc.subject | 03 Chemical Sciences, 06 Biological Sciences, 11 Medical and Health Sciences | |
dc.subject.classification | Biochemistry & Molecular Biology | |
dc.subject.mesh | Lung | |
dc.subject.mesh | Mast Cells | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Mice, Inbred BALB C | |
dc.subject.mesh | Mice, Inbred C3H | |
dc.subject.mesh | Mice, Inbred C57BL | |
dc.subject.mesh | Mice, Inbred CBA | |
dc.subject.mesh | Mice, Knockout | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Colitis | |
dc.subject.mesh | Pulmonary Disease, Chronic Obstructive | |
dc.subject.mesh | Disease Models, Animal | |
dc.subject.mesh | Membrane Proteins | |
dc.subject.mesh | Male | |
dc.subject.mesh | Tryptases | |
dc.subject.mesh | Animals | |
dc.subject.mesh | Colitis | |
dc.subject.mesh | Disease Models, Animal | |
dc.subject.mesh | Humans | |
dc.subject.mesh | Lung | |
dc.subject.mesh | Male | |
dc.subject.mesh | Mast Cells | |
dc.subject.mesh | Membrane Proteins | |
dc.subject.mesh | Mice, Inbred BALB C | |
dc.subject.mesh | Mice, Inbred C3H | |
dc.subject.mesh | Mice, Inbred C57BL | |
dc.subject.mesh | Mice, Inbred CBA | |
dc.subject.mesh | Mice, Knockout | |
dc.subject.mesh | Pulmonary Disease, Chronic Obstructive | |
dc.subject.mesh | Tryptases | |
dc.title | Importance of mast cell Prss31/transmembrane tryptase/tryptase-γ in lung function and experimental chronic obstructive pulmonary disease and colitis. | |
dc.type | Journal Article | |
utslib.citation.volume | 289 | |
utslib.location.activity | United States | |
utslib.for | 03 Chemical Sciences | |
utslib.for | 06 Biological Sciences | |
utslib.for | 11 Medical and Health Sciences | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney | |
utslib.copyright.status | closed_access | * |
dc.date.updated | 2021-03-04T01:01:38Z | |
pubs.issue | 26 | |
pubs.publication-status | Published | |
pubs.volume | 289 | |
utslib.citation.issue | 26 |
Abstract:
Protease serine member S31 (Prss31)/transmembrane tryptase/tryptase-γ is a mast cell (MC)-restricted protease of unknown function that is retained on the outer leaflet of the plasma membrane when MCs are activated. We determined the nucleotide sequences of the Prss31 gene in different mouse strains and then used a Cre/loxP homologous recombination approach to create a novel Prss31(-/-) C57BL/6 mouse line. The resulting animals exhibited no obvious developmental abnormality, contained normal numbers of granulated MCs in their tissues, and did not compensate for their loss of the membrane tryptase by increasing their expression of other granule proteases. When Prss31-null MCs were activated with a calcium ionophore or by their high affinity IgE receptors, they degranulated in a pattern similar to that of WT MCs. Prss31-null mice had increased baseline airway reactivity to methacholine but markedly reduced experimental chronic obstructive pulmonary disease and colitis, thereby indicating both beneficial and adverse functional roles for the tryptase. In a cigarette smoke-induced model of chronic obstructive pulmonary disease, WT mice had more pulmonary macrophages, higher histopathology scores, and more fibrosis in their small airways than similarly treated Prss31-null mice. In a dextran sodium sulfate-induced acute colitis model, WT mice lost more weight, had higher histopathology scores, and contained more Cxcl-2 and IL-6 mRNA in their colons than similarly treated Prss31-null mice. The accumulated data raise the possibility that inhibitors of this membrane tryptase may provide additional therapeutic benefit in the treatment of humans with these MC-dependent inflammatory diseases.
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