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Isolation and characterization of a cDNA for human MEP/Cathepsin L

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6081090
The major excreted acid protease from malignantly transformed mouse cells (MEP) has similar enzymatic properties to Cathepsin L. They have cloned and sequenced the mouse cDNA for this protein. In this work they report the isolation and characterization of a cDNA for human MEP. A 1.6 kb cDNA from an Okayama-Berg library made from mRNA from SV-40 transformed human fibroblasts was isolated by cross-hybridization at low stringency to the mouse cDNA. Sequence analysis shows that the cloned DNA is more than 70% homologous to the mouse DNA within the protein coding region, non-coding 3' and 5' regions being less homologous than this. The deduced amino acid sequence from the single open reading frame is 98% homologous with the partial protein sequence published for human Cathepsin L and 70% homologous to mouse MEP. Northern blots show that mouse and human cells make a similar size message, about 1.8 kb. A Northern blot of human tissues shows the highest levels of MEP/Cathepsin L mRNA in liver, stomach, ovary and small bowel, with lower levels in other tissues. The isolation of this human clone for MEP/Cathepsin L will allow them to determine whether expression of this protease is correlated with tumorigenicity in human cells as it is in the mouse system.
Research Organization:
National Institute of Health, Bethesda, MD
OSTI ID:
6081090
Report Number(s):
CONF-870644-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 46:6
Country of Publication:
United States
Language:
English