Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin.

B. R. Troen, Susannah Gal, M. M. Gottesman

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

The major excreted protein (MEP) of malignantly transformed mouse fibroblasts is a secreted thiol proteinase. Sequencing of the MEP cDNA shows the coding region for the protein to be identical with the sequence for a mouse cysteine proteinase isolated from macrophages, but the MEP cDNA is polyadenylated at a different site in the 3' non-coding region. Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. We have placed the MEP cDNA in a eukaryotic expression vector and demonstrated the production of the 39 kDa polypeptide form of mouse MEP in monkey CV-1 cells.

Original languageEnglish (US)
Pages (from-to)731-735
Number of pages5
JournalThe Biochemical journal
Volume246
Issue number3
DOIs
StatePublished - Jan 1 1987

Fingerprint

Cathepsins
Complementary DNA
Proteins
Cathepsin L
Peptides
Cysteine Proteases
Protein Sequence Analysis
Sulfhydryl Compounds
Amino Acids
Open Reading Frames
Haplorhini
Macrophages
Peptide Hydrolases
Fibroblasts

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{e1c42124a8064285b06e07d7aa47ec33,
title = "Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin.",
abstract = "The major excreted protein (MEP) of malignantly transformed mouse fibroblasts is a secreted thiol proteinase. Sequencing of the MEP cDNA shows the coding region for the protein to be identical with the sequence for a mouse cysteine proteinase isolated from macrophages, but the MEP cDNA is polyadenylated at a different site in the 3' non-coding region. Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. We have placed the MEP cDNA in a eukaryotic expression vector and demonstrated the production of the 39 kDa polypeptide form of mouse MEP in monkey CV-1 cells.",
author = "Troen, {B. R.} and Susannah Gal and Gottesman, {M. M.}",
year = "1987",
month = "1",
day = "1",
doi = "10.1042/bj2460731",
language = "English (US)",
volume = "246",
pages = "731--735",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin. / Troen, B. R.; Gal, Susannah; Gottesman, M. M.

In: The Biochemical journal, Vol. 246, No. 3, 01.01.1987, p. 731-735.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Sequence and expression of the cDNA for MEP (major excreted protein), a transformation-regulated secreted cathepsin.

AU - Troen, B. R.

AU - Gal, Susannah

AU - Gottesman, M. M.

PY - 1987/1/1

Y1 - 1987/1/1

N2 - The major excreted protein (MEP) of malignantly transformed mouse fibroblasts is a secreted thiol proteinase. Sequencing of the MEP cDNA shows the coding region for the protein to be identical with the sequence for a mouse cysteine proteinase isolated from macrophages, but the MEP cDNA is polyadenylated at a different site in the 3' non-coding region. Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. We have placed the MEP cDNA in a eukaryotic expression vector and demonstrated the production of the 39 kDa polypeptide form of mouse MEP in monkey CV-1 cells.

AB - The major excreted protein (MEP) of malignantly transformed mouse fibroblasts is a secreted thiol proteinase. Sequencing of the MEP cDNA shows the coding region for the protein to be identical with the sequence for a mouse cysteine proteinase isolated from macrophages, but the MEP cDNA is polyadenylated at a different site in the 3' non-coding region. Strong homology of MEP with human cathepsin L suggests that MEP is the mouse analogue of cathepsin L. Amino acid sequencing of the N-terminus of the secreted form of MEP indicates that, during secretion, the polypeptide is cleaved between amino acids 17 and 18. We have placed the MEP cDNA in a eukaryotic expression vector and demonstrated the production of the 39 kDa polypeptide form of mouse MEP in monkey CV-1 cells.

UR - http://www.scopus.com/inward/record.url?scp=0023656232&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023656232&partnerID=8YFLogxK

U2 - 10.1042/bj2460731

DO - 10.1042/bj2460731

M3 - Article

C2 - 3689328

AN - SCOPUS:0023656232

VL - 246

SP - 731

EP - 735

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -