Relative roles of collagenase and lysosomal cysteine-proteinases in bone resorption
- PMID: 1480065
Relative roles of collagenase and lysosomal cysteine-proteinases in bone resorption
Abstract
Both lysosomal cysteine-proteinases and collagenase appear to be necessary for the resorption of actively growing, immature woven bone, but their relative roles are not yet clearly elucidated. The present evidence indicates that, during bone resorption, the osteoclast first solubilizes the mineral by a secretion of acid and then removes the exposed demineralized collagen by the action of secreted lysosomal collagenolytic cysteine-proteinases. Collagenase in bone seems to be mainly a product of osteoblasts and related cells, not osteoclasts. Its role could be limited in the removal of any non-mineralized collagen layers which could be covering mineralized bone surfaces and which seem to prevent the activation of osteoclasts and thus their action; such a "shield" of unmineralized osteoid is well-established at the surface of actively growing woven bone, although not on the resorbing surfaces of mature lamellar bone. Moreover, some osteoblast-derived procollagenase is stored in the mineralized bone matrix from which it can be released by demineralization. It is therefore possible that it may also contribute to the degradation of demineralized bone collagen once it has been released and activated by lysosomal cysteine-proteinases under the osteoclast.
Similar articles
-
The role of collagenase in bone resorption. An overview.Pathol Biol (Paris). 1988 Nov;36(9):1139-46. Pathol Biol (Paris). 1988. PMID: 2851768 Review.
-
Cellular biology and biochemical mechanism of bone resorption. A review of recent developments on the formation, activation, and mode of action of osteoclasts.Clin Orthop Relat Res. 1988 Jun;(231):239-71. Clin Orthop Relat Res. 1988. PMID: 3286076 Review.
-
Bone-resorbing agents affect the production and distribution of procollagenase as well as the activity of collagenase in bone tissue.Endocrinology. 1988 Jul;123(1):264-76. doi: 10.1210/endo-123-1-264. Endocrinology. 1988. PMID: 2838255
-
Degradation of collagen in the bone-resorbing compartment underlying the osteoclast involves both cysteine-proteinases and matrix metalloproteinases.J Cell Physiol. 1992 Feb;150(2):221-31. doi: 10.1002/jcp.1041500202. J Cell Physiol. 1992. PMID: 1734028
-
Plasminogen activators are involved in the degradation of bone by osteoclasts.Bone. 2008 Nov;43(5):915-20. doi: 10.1016/j.bone.2008.07.004. Epub 2008 Jul 21. Bone. 2008. PMID: 18691680
Cited by
-
Widespread expression of tartrate-resistant acid phosphatase (Acp 5) in the mouse embryo.J Anat. 2000 Apr;196 ( Pt 3)(Pt 3):433-41. doi: 10.1046/j.1469-7580.2000.19630433.x. J Anat. 2000. PMID: 10853965 Free PMC article.
-
Inhibition of cartilage and bone destruction in adjuvant arthritis in the rat by a matrix metalloproteinase inhibitor.J Exp Med. 1995 Aug 1;182(2):449-57. doi: 10.1084/jem.182.2.449. J Exp Med. 1995. PMID: 7629505 Free PMC article.
-
Spatio-temporal simulations of bone remodelling using a bone cell population model based on cell availability.Front Bioeng Biotechnol. 2023 Mar 7;11:1060158. doi: 10.3389/fbioe.2023.1060158. eCollection 2023. Front Bioeng Biotechnol. 2023. PMID: 36959906 Free PMC article.
-
Chloroquine increases osteoclast activity in vitro but does not improve the osteopetrotic bone phenotype of ADO2 mice.Bone. 2021 Dec;153:116160. doi: 10.1016/j.bone.2021.116160. Epub 2021 Aug 28. Bone. 2021. PMID: 34464779 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Other Literature Sources