Source:http://linkedlifedata.com/resource/pubmed/id/15358180
Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
2004-9-13
|
| pubmed:databankReference | |
| pubmed:abstractText |
Trypsin-like serine proteases are involved in diverse biological processes such as complement activation, tissue remodeling, cellular migration, tumor invasion, and metastasis. Here we report a novel human C1r-like serine protease analog, CLSPa, derived from dendritic cells (DC). The 487-residue CLSPa protein contains a CUB domain and a serine protease domain, possessing characteristic catalytic triad but lacking typical activation/cleavage sequence. It shares great homology with complement C1r/C1s and mannose-associated serine proteases. CLSPa mRNA is widely expressed, especially abundant in placenta, liver, kidney, pancreas, and myeloid cells, which are a major resources of serine proteases. Upon stimulation by agonistic anti-CD40 Ab, TNF-alpha, or LPS, CLSPa mRNA expression was significantly up-regulated in monocytic cells and monocyte-derived immature DC. When overexpressed in 293T cells, CLSPa protein was synthesized into the culture supernatants as a secretory protein, which had an inhibitory effect on complement-mediated cytotoxicity to antibody-sensitized erythrocytes. However, CLSPa itself possesses little protease activity, but it plays an inhibitory role in other active protease catalytic processes. The identification of human CLSPa as a novel Clr-like protein might facilitate future investigation of the regulatory mechanism of CLSPa in complement pathways during inflammation.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement C1r,
http://linkedlifedata.com/resource/pubmed/chemical/Complement System Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin Inhibitors
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0006-291X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
321
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
329-36
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:15358180-Amino Acid Sequence,
pubmed-meshheading:15358180-Base Sequence,
pubmed-meshheading:15358180-Cell Line,
pubmed-meshheading:15358180-Chromosomes, Human, Pair 12,
pubmed-meshheading:15358180-Cloning, Molecular,
pubmed-meshheading:15358180-Complement C1r,
pubmed-meshheading:15358180-Complement System Proteins,
pubmed-meshheading:15358180-Cytotoxicity, Immunologic,
pubmed-meshheading:15358180-Dendritic Cells,
pubmed-meshheading:15358180-Gene Expression Regulation,
pubmed-meshheading:15358180-Hemolysis,
pubmed-meshheading:15358180-Humans,
pubmed-meshheading:15358180-Molecular Sequence Data,
pubmed-meshheading:15358180-Monocytes,
pubmed-meshheading:15358180-RNA, Messenger,
pubmed-meshheading:15358180-Sequence Alignment,
pubmed-meshheading:15358180-Serine Endopeptidases,
pubmed-meshheading:15358180-Trypsin Inhibitors
|
| pubmed:year |
2004
|
| pubmed:articleTitle |
A novel human dendritic cell-derived C1r-like serine protease analog inhibits complement-mediated cytotoxicity.
|
| pubmed:affiliation |
Institute of Immunology, Zhejiang University, 353 Yan'an Road, Hangzhou 310031, PR China.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|