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Title: Expression of recombinant human Met-ase-1: a NK cell-specific granzyme.
Austin Authors: Smyth, Mark J;O'Connor, M D;Kelly, J M;Ganesvaran, P;Thia, K Y;Trapani, Joseph A
Affiliation: Cellular Cytotoxicity Laboratory, Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australia
Issue Date: 14-Dec-1995
Publication information: Biochemical and Biophysical Research Communications; 217(2): 675-83
Abstract: Human Met-ase-1 is a member of a family of cytotoxic lymphocyte serine proteases (granzymes), but is expressed specifically in CD3- large granular lymphocytes with natural killer cell activity. We have devised a polymerase chain reaction strategy to delete the predicted hexapropeptide of human Met-ase-1 (Ser-6 to Gln-1), to enable its expression and activation in mammalian COS cells. In addition, using peptide immunization we have derived a unique and specific monoclonal antibody detecting human Met-ase-1. Western blot analysis and protease assays of transfected COS cell lysates against a panel of thiobenzyl ester substrates formally demonstrated that the human Met-ase-1 gene encodes a serine proteinase that specifically hydrolyzes substrates containing a methionine (Met-) side chain at P1. The expression of active human Met-ase-1 and the generation of a specific anti-human Met-ase-1 monoclonal antibody will now enable a detailed structure/function analysis of key amino acids that confer this unusual serine protease specificity.
Gov't Doc #: 7503751
Journal: Biochemical and biophysical research communications
Type: Journal Article
Subjects: Animals
Antibodies, Monoclonal.immunology
Base Sequence
Cell Line
Cercopithecus aethiops
DNA Primers.chemistry
Killer Cells, Natural.enzymology
Molecular Sequence Data
Protein Processing, Post-Translational
Recombinant Proteins
Serine Endopeptidases.genetics.immunology.metabolism
Substrate Specificity
Appears in Collections:Journal articles

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