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Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes.
Two cDNA clones corresponding to genes that are induced at least 10-fold in peripheral human blood leukocytes by staphylococcal enterotoxin A were isolated and sequenced. Clone 1-3E encodes a 247-residue protein that comprises a putative signal sequence, and resembles a serine protease; the cognate mRNA is expressed in T lymphocyte clones but in none of the other human cell lines tested. The deduced protein sequence is most closely related (68% homology) to that of the postulated protease CCPI from activated murine cytotoxic T lymphocytes and to that of rat mast cell protease II (47% homology). The other cDNA, 3-10C, encodes a protein of 99 residues that resembles human beta-thromboglobulin (42% homology); the cognate mRNA was also found in SEA-stimulated U937 cells, a histiocytic lymphoma-derived cell line.
PMID: 2953813 [PubMed - indexed for MEDLINE]
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Cited by 48 PubMed Central articles
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NMR structure and dynamics of monomeric neutrophil-activating peptide 2.
Young H, Roongta V, Daly TJ, Mayo KH.
Biochem J. 1999 Mar 15; 338 ( Pt 3):591-8.
[Biochem J. 1999]
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Sheep mast-cell proteinases-1 and -3: cDNA cloning, primary structure and molecular modelling of the enzymes and further studies on substrate specificity.
McAleese SM, Pemberton AD, McGrath ME, Huntley JF, Miller HR.
Biochem J. 1998 Aug 1; 333 ( Pt 3):801-9.
[Biochem J. 1998]
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A recipe for designing water-soluble, beta-sheet-forming peptides.
Mayo KH, Ilyina E, Park H.
Protein Sci. 1996 Jul; 5(7):1301-15.
[Protein Sci. 1996]
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