Molecular Characteristics of a Multicorn, a New Large Proteolytic Assembly and Potential Anti-Cancer Drug Target, in Human Breast Cancer Cells
Abstract
Proper regulation of cell division and differentiation are major factors preventing neoplastic growth, and proteolysis is one of controlling mechanism of these processes. We have discovered a new giant proteolytic complex ubiquitous among Eukaryotes. The enzyme named multicorn apparently takes part in cell cycle regulation and is involved in partial overcoming the physiological effects of inhibitors targeting a well- known drug target, proteasome . The multicorn may constitute an attractive target for anti-cancer drugs, a marker for neoplastic transformation and may influence success of drugs targeting proteasome. The studies conducted lead toward understanding biological role of this enzyme. Our findings up to date: (i) the multicorn, which was first found in the cytosol, is present in the nucleus of mitotic cells. Importantly, it is detectable only in nucleus of the control MCF-10A breast cells, and not in the MCF-7 cancerous cells. (ii) The human multicorn is built from a single subunit. The oligomerization and activity of multicorn apparently is regulated by phosphorylation of this subunit in several distinct sites. (iii) The pattern of phosphorylation is specific for the particular cellular fraction, and differs between nonsynchronous, mitotic and overconfluent cells, and between control and cancerous cells.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 01, 2002
- Accession Number
- ADA407389
Entities
People
- Maria E. Gaczynaka
Organizations
- University of Texas Health Science Center at San Antonio