Molecular cloning of human cathepsin G: structural similarity to mast cell and cytotoxic T lymphocyte proteinases
Human cathepsin G is a serine proteinase with chymotrypsin-like specificity found in both polymorphonuclear leukocytes (neutrophils) and the U937 leukemic cell line. Utilizing RNA from the latter, the authors have constructed a cDNA library in lambdagt11 and isolated a clone which apparently codes for the complete amino acid sequence of this enzyme. Analysis of the sequence reveals homology with rat mast cell proteinase II (47%) but a greater degree of identity (56%) with a product of activated mouse cytotoxic T lymphocytes. The close relationship between the three proteins indicates similarities in substrate specificity and in biosynthesis which they predict involves removal of a two amino acid activation peptide during or just before packaging to their respective storage granules.
- Research Organization:
- Univ. of Georgia, Athens
- OSTI ID:
- 5639672
- Journal Information:
- Biochemistry; (United States), Vol. 26:8
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CATHEPSIN
DNA-CLONING
AMINO ACID SEQUENCE
DNA POLYMERASES
GENES
LYMPHOCYTES
MAN
MESSENGER-RNA
MICE
RECOMBINANT DNA
SH-PROTEINASES
TRITIUM COMPOUNDS
ANIMAL CELLS
ANIMALS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CLONING
CONNECTIVE TISSUE CELLS
DNA
ENZYMES
HYDROLASES
LABELLED COMPOUNDS
LEUKOCYTES
MAMMALS
MATERIALS
MOLECULAR STRUCTURE
NUCLEIC ACIDS
NUCLEOTIDYLTRANSFERASES
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PHOSPHORUS-GROUP TRANSFERASES
POLYMERASES
PRIMATES
RNA
RODENTS
SOMATIC CELLS
TRANSFERASES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques