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(Pro)collagenase (matrix metalloproteinase-1) is present in rodent osteoclasts and in the underlying bone-resorbing compartment.
- J. Delaisse, Y. Eeckhout, +5 authors R. Baron
- Biology, Medicine
- Journal of cell science
- 1 December 1993
It is proposed that osteoclastic collagenase is secreted in the resorbing compartment where it may cooperate with the lysosomal cysteine proteinases in the degradation of the collagen component of the matrix during the resOrption of bone. Expand
Differential effects of the 3',5'-cyclic adenosine monophosphate and protein kinase C pathways on the response of isolated rat osteoclasts to calcitonin.
It is concluded that, in osteoclasts, CT receptors are coupled to both the cAMP-dependent protein kinase and the PKC pathways, and although these two second messengers can have additive inhibitory effects on bone resorption, only activation of thePKC pathway induces rapid cell retraction. Expand
Evidence for the presence of (pro)collagenase in osteoclasts
The strontium salt S12911 inhibits bone resorption in mouse calvaria and isolated rat osteoclasts cultures
Ion transport and the molecular mechanisms of bone resorption
9. Ion transport and the molecular mechanisms of bone resorption