Serine/threonine phosphatases in osteoclastogenesis and bone resorption.

Autor: Karkache IY; Department of Orthopedic Surgery, University of Minnesota, Minneapolis, MN 55455, United States., Damodaran JR; Department of Orthopedic Surgery, University of Minnesota, Minneapolis, MN 55455, United States., Molstad DHH; Department of Orthopedic Surgery, University of Minnesota, Minneapolis, MN 55455, United States., Bradley EW; Department of Orthopedic Surgery, University of Minnesota, Minneapolis, MN 55455, United States; Stem Cell Institute, University of Minnesota, Minneapolis, MN 55455, United States. Electronic address: ebradle1@umn.edu.
Jazyk: angličtina
Zdroj: Gene [Gene] 2021 Mar 01; Vol. 771, pp. 145362. Date of Electronic Publication: 2020 Dec 16.
DOI: 10.1016/j.gene.2020.145362
Abstrakt: Maintenance of optimal bone mass is controlled through the concerted functions of several cell types, including bone resorbing osteoclasts. Osteoclasts function to remove calcified tissue during developmental bone modeling, and degrade bone at sites of damage during bone remodeling. Changes to bone homeostasis can arise with alterations in osteoclastogenesis and/or catabolic activity that are not offset by anabolic activity; thus, factors that regulate osteoclastogenesis and bone resorption are of interest to further our understanding of basic bone biology, and as potential targets for therapeutic intervention. Several key cytokines, including RANKL and M-CSF, as well as co-stimulatory factors elicit kinase signaling cascades that promote osteoclastogenesis. These kinase cascades are offset by the action of protein phosphatases, including members of the serine/threonine phosphatase family. Here we review the functions of serine/threonine phosphatases and their control of osteoclast differentiation and function, while highlighting deficiencies in our understanding of this understudied class of proteins within the field.
(Copyright © 2020 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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