The role of mechanical stretching in the activation and localization of adhesion proteins and related intracellular molecules

Boccafoschi, Francesca; Mosca, C.; Bosetti, Michela; Cannas, M.

doi:10.1002/jcb.23056

Cited by 18 publications

(15 citation statements)

References 28 publications

(26 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Transmitted via intracellular signaling cascades including MAPK26, PI3K/Akt27, GTPases28, Wnt29 and calcium30 pathways, the signals modulate osteoblastic differentiation by up-regulation of genes such as Runx2, Alp , and Ocn 31. RUNX2 is a master control transcription factor of osteoblastic differentiation and function.…”

Section: Discussionmentioning

confidence: 99%

Magnitude-dependent response of osteoblasts regulated by compressive stress

Shen

Geng

Liu

et al. 2017

Sci Rep

View full text Add to dashboard Cite

The present study aimed to investigate the role of magnitude in adaptive response of osteoblasts exposed to compressive stress. Murine primary osteoblasts and MC3T3-E1 cells were exposed to compressive stress (0, 1, 2, 3, 4, and 5 g/cm2) in 3D culture. Cell viability was evaluated, and expression levels of Runx2, Alp, Ocn, Rankl, and Opg were examined. ALP activity in osteoblasts and TRAP activity in RAW264.7 cells co-cultured with MC3T3-E1 cells were assayed. Results showed that compressive stress within 5.0 g/cm2 did not influence cell viability. Both osteoblastic and osteoblast-regulated osteoclastic differentiation were enhanced at 2 g/cm2. An increase in stress above 2 g/cm2 did not enhance osteoblastic differentiation further but significantly inhibited osteoblast-regualted osteoclastic differentiation. This study suggested that compressive stress regulates osteoblastic and osteoclastic differentiation through osteoblasts in a magnitude-dependent manner.

show abstract

Section: Discussionmentioning

confidence: 99%

Magnitude-dependent response of osteoblasts regulated by compressive stress

Shen

Geng

Liu

et al. 2017

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Tyrosine phosphorylation at different sites within FAK is catalyzed in distinct ways and affects various cellular functions. Previous studies regarding the FAK activation state in a variety of non-chondrocytic cell types under mechanical stress have mainly concentrated on the autophosphorylation site [25,26,27]. In a study on fibroblasts, Tyr 576/577 residues of FAK were shown to be required for the mechanical stress-induced cellular response [13,28].…”

Section: Discussionmentioning

confidence: 99%

Periodic Mechanical Stress Stimulates the FAK Mitogenic Signal in Rat Chondrocytes Through ERK1/2 Activity

Liang

Ren

Liu

et al. 2013

Cell Physiol Biochem

View full text Add to dashboard Cite

Background/Aims: The biological effects of periodic mechanical stress on chondrocytes have been studied extensively over the past few years. However, the mechanisms underlying chondrocyte mechanosensing and signaling in response to periodic mechanical stress remain to be determined. In the current study, we examined the effects of focal adhesion kinase (FAK) signaling on periodic mechanical stress-induced chondrocyte proliferation and matrix synthesis. Methods and Results: Periodic mechanical stress significantly induced sustained phosphorylation of FAK at Tyr³⁹⁷ and Tyr^576/577. Reduction of FAK with targeted shRNA via transfection of NH₂-terminal tyrosine phosphorylation-deficient FAK mutant Y397F or Y576F-Y577F abolished periodic mechanical stress-induced chondrocyte proliferation and matrix synthesis, accompanied by attenuated ERK1/2 phosphorylation. However, activation of Src, PLCγ1 and Rac1 was not prevented upon FAK suppression. Furthermore, pretreatment with the Src-selective inhibitor, PP2, and shRNA targeted to Src or suppression of Rac1 with its selective inhibitor, NSC23766, blocked FAK phosphorylation at Tyr,^576/577 but not Tyr,³⁹⁷ under periodic mechanical stress. Interestingly, FAK phosphorylation neither at Tyr³⁹⁷ nor at Tyr^576/577 was affected by PLCγ1 depletion when periodic mechanical stress was applied. In addition, Tyr³⁹⁷ and Tyr^576/577 phosphorylation levels were reduced upon pretreatment with a blocking antibody against integrin β1 under conditions of periodic mechanical stress. Conclusion: Our findings collectively suggest that periodic mechanical stress promotes chondrocyte proliferation and matrix synthesis through at least two pathways, integrin β1-Src-Rac1-FAK(Tyr^576/577)-ERK1/2 and integrin β1-FAK (Tyr³⁹⁷)-ERK1/2.

show abstract

“…In addition its ability to sense external forces, vinculin has been reported to regulate how applied mechanical stress alters adhesion composition in order to induce cell morphological changes. [37][38][39] Recent evidence indicates that vinculin is crucial for transmission of mechanical forces resulting from either actomyosin or cell-generated forces, since the recruitment of vinculin to FAs corresponds to the amount of force applied to the extracellular matrix (ECM). 40,41 Furthermore, the F-actin/vinculin interaction may be required for these forces since, without Vt, vinculin does not follow the retrograde flow of actin.…”

Section: -36mentioning

confidence: 99%