期刊
BONE
卷 41, 期 1, 页码 39-51出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.bone.2007.01.024
关键词
osteoblasts; focal adhesion kinase (FAK); skeletal regeneration; osteoclasts; Pyk2
资金
- NCRR NIH HHS [C06 RR016490, C06-RR16490] Funding Source: Medline
- NIAMS NIH HHS [R01 AR045989-02, R01 AR45989, R01 AR045989, R01 AR045989-07, R01 AR045989-09, R01 AR045989-06S1, R01 AR045989-08, R01 AR045989-04, R01 AR045989-01A1, R01 AR045989-05, R01 AR045989-03] Funding Source: Medline
- NIDCR NIH HHS [P60 DE013058, P60 DE013058-020002, P60 DE013058-019002, P60 DE013058-01S19002, R01 DE 012462, R01 DE024000, P60 DE013058-010002, P60 DE13058, P60 DE013058-01S10002, R01 DE012462] Funding Source: Medline
Integrins link the inside of a cell with its outside environment and in doing so regulate a wide variety of cell behaviors. Integrins are well known for their roles in angiogenesis and cell migration but their functions in bone formation are less clear. The majority of integrin signaling proceeds through focal adhesion kinase (FAK), an essential component of the focal adhesion complex. We generated transgenic mice in which FAK was deleted in osteoblasts and uncovered a previously unknown role in osteoblast differentiation associated with bone healing. FAK mutant cells migrated to the site of skeletal injury and angiogenesis was unaffected yet the transgenic mice still exhibited numerous defects in reparative bone formation. Osteoblast differentiation itself was unperturbed by the loss of FAK, whereas the attachment of osteoclasts to the bone matrix was disrupted in vivo. We postulate that defective bi-directional integrin signaling affects the organization of the collagen matrix. Finally, we present a compensatory candidate molecule, Pyk2, which localized to the focal adhesions in osteoblasts that were lacking FAK. (c) 2007 Elsevier Inc. All rights reserved.
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