Transcription regulation of cathepsin K controlled by bone resorption related cytokines
Date
1999
DOI
Authors
Kamolmatyakul, Suttatip
Version
OA Version
Citation
Abstract
Osteoclasts function as bone and cartilage-resorbing cells to modulate bone
formation and metabolism. They posses a highly specialized proton generating
mechanism for the rapid dissolution of bone mineral and secrete collagenases,
cathepsin K and other hydrolyses active in the degradation of bone matrix
proteins. To date, several cytokines have been implicated in osteoclast formation
and activity. Some cytokines, including IL-1a, induce bone resorption whereas
the others, such as IFN-y, inhibit bone resorption. It is possible that cytokines
may control physiological and pathological bone resorption through the regulation
of osteoclast gene expression including cathepsin K. Cathepsin K is abundantly
and selectively expressed in osteoclast, and is a key protease responsible for
matrix protein degradation in normal bone remodeling as well as in pathological
processes, such as periodontal disease and osteoporosis. lnterferon-y (IFN-y) is
a glycoprotein produced by activated lymphocyte and natural killer cells and has
multiple biologic effects, including antiviral, antitumor, and cell growth inhibitory
activities. Like many other cytokines, IFN-y also functions in bone metabolism.
IFN-y inhibits osteoclastic bone resorption, but the mechanism responsible for
this inhibition is unknown. IL-1a is pluripotent cytokine produced by
monocytes/macrophages that has various effects on a wide variety of cells
including osteoclast. I L-1 a is the most potent osteoclast-activating factor that ... [TRUNCATED]
Description
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Thesis (D.Sc.D.)--Boston University, Henry M. Goldman School of Dental Medicine, 1999 (Pediatric Dentistry).
Includes bibliographical references (leaves 68-79).
Thesis (D.Sc.D.)--Boston University, Henry M. Goldman School of Dental Medicine, 1999 (Pediatric Dentistry).
Includes bibliographical references (leaves 68-79).
License
This work is protected by copyright. Downloading is restricted to the BU community. If you are the author of this work and would like to make it publicly available, please contact open-help@bu.edu.