Document Detail


Characterization of cDNA clones encoding mouse proteinase 3 (myeloblastine) and cathepsin G.
MedLine Citation:
PMID:  9211743     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Serine proteases are the most abundant granule constituents of several major hematopoietic cell lineages. Due to their high abundance and their strict tissue specificity they have become important phenotypic cell markers used for studies of various aspects of hematopietic cell development. Using a polymerase chain reaction (PCR)-based strategy for the isolation of trypsin-related serine proteases, we were able to isolate cDNAs for two of the major neutrophil and monocyte serine proteases in the mouse, cathepsin G and mouse protease 3 (myeloblastin). The internal PCR fragments were used as probes to screen a mouse mast cell cDNA library and a cDNA library originating from a mouse monocytic cell line (WEHI-274.1). Full-length cDNAs for mouse cathepsin G and proteinase 3 were isolated and their complete sequences were determined. Northern blot analysis revealed expression of cathepsin G in immature cells of the monocyte macrophage lineage but also in the connective tissue mast cell line MTC. Proteinase 3 was expressed in several cell lines of myelo-monocytic origin and in one B-cell line, but not in any of the other cell lines tested. The isolation of cDNAs for mouse cathepsin G and mouse proteinase 3, together with the previous characterization of the gene for mouse N-elastase, and the entire or partial amino acid sequences for porcine azurocidine, equine N-elastase and proteinase 3, rat, dog, and rabbit cathepsin Gs in evolutionary relatively distantly related mammalian species, indicates that these four members of the serine protease family have been maintained for more than 100 million years of mammalian evolution. This latter finding indicates a strong evolutionary pressure to maintain specific immune functions associated with these neutrophil and monocyte proteases. All amino acid positions of major importance for the cleavage site selection have also been fully conserved between mouse and human proteinase 3 and a few minor changes have occurred between mouse and human cathepsin G.
Authors:
M Aveskogh; C Lützelschwab; M R Huang; L Hellman
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Immunogenetics     Volume:  46     ISSN:  0093-7711     ISO Abbreviation:  Immunogenetics     Publication Date:  1997  
Date Detail:
Created Date:  1997-08-13     Completed Date:  1997-08-13     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  0420404     Medline TA:  Immunogenetics     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  181-91     Citation Subset:  IM    
Affiliation:
Department of Medical Immunology and Microbiology, University of Uppsala, Biomedical Center, Box 582, S-751 23 Uppsala, Sweden.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/U43525;  X78544
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Cathepsin G
Cathepsins / genetics*
Cloning, Molecular
DNA, Complementary / genetics
Dogs
Gene Expression
Humans
Mice
Mice, Inbred BALB C
Molecular Sequence Data
Myeloblastin
Phylogeny
RNA, Messenger / genetics
Rabbits
Rats
Sequence Alignment
Sequence Homology, Nucleic Acid
Serine Endopeptidases / genetics*
Tissue Distribution
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/RNA, Messenger; EC 3.4.-/Cathepsins; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.20/CTSG protein, human; EC 3.4.21.20/Cathepsin G; EC 3.4.21.20/Ctsg protein, mouse; EC 3.4.21.20/Ctsg protein, rat; EC 3.4.21.76/Myeloblastin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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