uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Extended cleavage specificities of mast cell proteases 1 and 2 from golden hamster: Classical chymase and an elastolytic protease comparable to rat and mouse MCP-5
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology.ORCID iD: 0000-0002-4771-0080
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Microbiology.
Show others and affiliations
2018 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 13, no 12, article id e0207826Article in journal (Refereed) Published
Abstract [en]

Serine proteases constitute the major protein content of mast cell secretory granules. Here we present the extended cleavage specificity of two such proteases from the golden hamster, Mesocricetus auratus. Analysis by phage display technique showed that one of them (HAM1) is a classical chymase with a specificity similar to the human mast cell chymase. However, in contrast to the human chymase, it does not seem to have a particular preference for any of the three aromatic amino acids, Phe, Tyr and Trp, in the P1 position of substrates. HAM1 also efficiently cleaved after Leu similarly to human and many other mast cell chymases. We observed only a 3-fold lower cleavage activity on Leu compared to substrates with P1 aromatic amino acids. Chymotryptic enzymes seem to be characteristic for connective tissue mast cells in mammalian species from opossums to humans, which indicates a very central role of these enzymes in mast cell biology. HAM1 also seems to have the strongest preference for negatively charged amino acids in the P2 position of all mast cell chymases so far characterized. The second hamster chymase, HAM2, is an elastolytic in its activity, similarly to the alpha-chymases in rats and mice (rMCP-5 and mMCP-5, respectively). The presence of an alpha-chymase that developed elastase activity thereby seems to be a relatively early modification of the alpha-chymase within the rodent branch of the mammalian evolutionary tree.

Place, publisher, year, edition, pages
PUBLIC LIBRARY SCIENCE , 2018. Vol. 13, no 12, article id e0207826
National Category
Immunology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-373000DOI: 10.1371/journal.pone.0207826ISI: 000452307600021PubMedID: 30521603OAI: oai:DiVA.org:uu-373000DiVA, id: diva2:1278233
Funder
Swedish Research Council, 621-2011-5007Available from: 2019-01-14 Created: 2019-01-14 Last updated: 2019-01-14Bibliographically approved

Open Access in DiVA

fulltext(6973 kB)63 downloads
File information
File name FULLTEXT01.pdfFile size 6973 kBChecksum SHA-512
24fa33288e87e6689acaa33bd227849294025bfc988784c3d512750cccfe9af2b764988148d6e5d2fbf958dcb4f028569201901f8db891ba6f01de9f23ab8415
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Authority records BETA

Thorpe, MichaelFu, ZhirongAkula, SrinivasHellman, Lars

Search in DiVA

By author/editor
Thorpe, MichaelFu, ZhirongAkula, SrinivasHellman, Lars
By organisation
MicrobiologyDepartment of Cell and Molecular Biology
In the same journal
PLoS ONE
ImmunologyBiochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
Total: 63 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 62 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf