Close relationship of the major excreted protein of transformed murine fibroblasts to thiol-dependent cathepsins


Publication Type:

Journal Article


Cancer research, Volume 46, Number 9, p.4590-3 (1986)


0008-5472 (Print)<br/>0008-5472 (Linking)

Accession Number:



Amino Acid Sequence, Animals, Cathepsins/genetics, Cell Cycle, Cell Transformation, Neoplastic/*enzymology, Cloning, Molecular, DNA/genetics, Mice, Molecular Weight, Neoplasm Proteins/*genetics, Proteins/genetics, RNA, Messenger/genetics


<p>Complementary DNA clones corresponding to 638 nucleotides of the messenger RNA encoding the major portion of murine major excreted protein have been isolated and sequenced. The amino acid sequence of a part of the murine major excreted protein deduced from the DNA sequence reveals substantial and significant homology with the cysteine proteases actinidin, rat cathepsin H, and papain. Since the amount of murine major excreted protein secreted by cultured cells is often enhanced by transformation, it is implicated in oncogenic phenomena and may play a role in the metastatic process by virtue of its proteolytic activity.</p>


Denhardt, D T<br/>Hamilton, R T<br/>Parfett, C L<br/>Edwards, D R<br/>St Pierre, R<br/>Waterhouse, P<br/>Nilsen-Hamilton, M<br/>CA39256/CA/NCI NIH HHS/<br/>Cancer Res. 1986 Sep;46(9):4590-3.