There is good reason to believe that the known human cysteine protease repertoire is currently incomplete. Recently, two peptide sequences (i.e. CTLA-2alpha and CTLA-2beta) have been identified in the mouse T-lymphocyte. These peptides have been shown to be similar to the propeptide of human cathepsin L. In this project, computer based searches for human homologues to these mouse peptide sequences has been made. One entry from the TIGR express sequence tag database has been identified. As part of this project, the tag was isolated from the human Jurkat cell mRNA, a cell line compatible with the source of RNA used to identify the original sequence tag. / Several novel members of the papain proteases superfamilly have been discovered and characterized in the last couple of years. Of particular note is cathepsin K, which is primarily an osteoclast component that has been shown to be the main mediator of organic matrix degradation during bone resorption. Since many of these proteases demonstrate relevant extracellular matrix degradation in connective tissue, they are of significant interest in the study of joint health and diseases. In this project, qualitative cathepsins mRNA expression analyses in representative human joint-related cells have been assessed by RT-PCR. (Abstract shortened by UMI.)
Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.31533 |
Date | January 2000 |
Creators | Roy, Nicholas, 1973- |
Contributors | Mort, John S. (advisor) |
Publisher | McGill University |
Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
Language | English |
Detected Language | English |
Type | Electronic Thesis or Dissertation |
Format | application/pdf |
Coverage | Master of Science (Division of Surgical Research.) |
Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
Relation | alephsysno: 001804686, proquestno: MQ70496, Theses scanned by UMI/ProQuest. |
Page generated in 0.0016 seconds