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The RhoA-Rok-myosin II pathway is involved in extracellular matrix-mediated regulation of prolactin signaling in mammary epithelial cells.

Du JY, Chen MC, Hsu TC, Wang JH, Brackenbury L, Lin TH, Wu YY, Yang Z, Streuli CH, Lee YJ - J. Cell. Physiol. (2012)

Bottom Line: Under these culture conditions, the RhoA pathway is activated, leading to downregulation of prolactin receptor expression and reduced prolactin signaling.In addition, inhibition of myosin II ATPase activity by blebbistatin also exerts a beneficial effect on prolactin receptor expression and prolactin signaling, suggesting that tension exerted by the collagen substratum, in collaboration with the RhoA-Rok-myosin II pathway, contributes to the failure of prolactin signaling.They display high levels of RhoA activity and are inefficient in prolactin signaling, stressing the importance of matrix stiffness in signal transduction.

View Article: PubMed Central - PubMed

Affiliation: Institute of Microbiology and Immunology, Chung Shan Medical University, Taichung, Taiwan, ROC.

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Related in: MedlinePlus

MECs cultured on plastic and collagen I exhibit higher RhoA activity than those cultured on BM. MECs were cultured on plastic (PL), collagen I (CI) or BM. Cell lysates were incubated with GST-Rhotekin Rho binding domain bound to glutathione-agarose beads to precipitate GTP-bound Rho. Total lysates and precipitates were then analyzed by immunoblotting using antibody to RhoA.
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fig01: MECs cultured on plastic and collagen I exhibit higher RhoA activity than those cultured on BM. MECs were cultured on plastic (PL), collagen I (CI) or BM. Cell lysates were incubated with GST-Rhotekin Rho binding domain bound to glutathione-agarose beads to precipitate GTP-bound Rho. Total lysates and precipitates were then analyzed by immunoblotting using antibody to RhoA.

Mentions: Initially, we examined RhoA activity in MECs cultured on plastic, collagen I, and BM. Our results showed that cells cultured on plastic and collagen I exhibited comparable levels of RhoA activity, which were much greater than those in cells cultured on BM (Fig. 1). This result indicates that ECM differentially regulates RhoA activity in MECs.


The RhoA-Rok-myosin II pathway is involved in extracellular matrix-mediated regulation of prolactin signaling in mammary epithelial cells.

Du JY, Chen MC, Hsu TC, Wang JH, Brackenbury L, Lin TH, Wu YY, Yang Z, Streuli CH, Lee YJ - J. Cell. Physiol. (2012)

MECs cultured on plastic and collagen I exhibit higher RhoA activity than those cultured on BM. MECs were cultured on plastic (PL), collagen I (CI) or BM. Cell lysates were incubated with GST-Rhotekin Rho binding domain bound to glutathione-agarose beads to precipitate GTP-bound Rho. Total lysates and precipitates were then analyzed by immunoblotting using antibody to RhoA.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3675639&req=5

fig01: MECs cultured on plastic and collagen I exhibit higher RhoA activity than those cultured on BM. MECs were cultured on plastic (PL), collagen I (CI) or BM. Cell lysates were incubated with GST-Rhotekin Rho binding domain bound to glutathione-agarose beads to precipitate GTP-bound Rho. Total lysates and precipitates were then analyzed by immunoblotting using antibody to RhoA.
Mentions: Initially, we examined RhoA activity in MECs cultured on plastic, collagen I, and BM. Our results showed that cells cultured on plastic and collagen I exhibited comparable levels of RhoA activity, which were much greater than those in cells cultured on BM (Fig. 1). This result indicates that ECM differentially regulates RhoA activity in MECs.

Bottom Line: Under these culture conditions, the RhoA pathway is activated, leading to downregulation of prolactin receptor expression and reduced prolactin signaling.In addition, inhibition of myosin II ATPase activity by blebbistatin also exerts a beneficial effect on prolactin receptor expression and prolactin signaling, suggesting that tension exerted by the collagen substratum, in collaboration with the RhoA-Rok-myosin II pathway, contributes to the failure of prolactin signaling.They display high levels of RhoA activity and are inefficient in prolactin signaling, stressing the importance of matrix stiffness in signal transduction.

View Article: PubMed Central - PubMed

Affiliation: Institute of Microbiology and Immunology, Chung Shan Medical University, Taichung, Taiwan, ROC.

Show MeSH
Related in: MedlinePlus