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Mechanical strain and estrogen activate estrogen receptor alpha in bone cells.
J Bone Miner Res. 2001 Jun; 16(6):1045-55.JB

Abstract

Bone cells' early responses to estrogen and mechanical strain were investigated in the ROS 17/2.8 cell line. Immunoblotting with antiphosphorylated estrogen receptor a (ER-alpha) antibody showed that when these cells were exposed for 10 minutes to estrogen (10(-8) M) or a single period of cyclic dynamic strain (peak 3400 microepsilon, 1 Hz, 600 cycles), there was an increase in the intensity of a 66-kDa band, indicating phosphorylation of ser122 in the amino terminus of ER-alpha. Increased phosphorylation was detected within 5 minutes of exposure to estrogen and 5 minutes after the end of the period of strain. Estrogen and strain also activated the mitogen-activated protein kinase (MAPK) family member extracellular regulated kinase-1 (ERK-1). Increases in ERK activation coincided with increased ER-alpha phosphorylation. Activation of ERK-1 and the phosphorylation of ER-alpha, by both estrogen and strain, were prevented by the MAP kinase kinase (MEK) inhibitor U0126 and the protein kinase A (PKA) inhibitor (PKI). These data support previous suggestions that resident bone cells' early responses to strain and estrogen share a common pathway, which involves ER-alpha. This pathway also appears to involve PKA and ERK-mediated phosphorylation of ser122 within the amino terminus of ER-alpha. Reduced availability of this pathway when estrogen levels are reduced could explain diminished effectiveness of mechanically related control of bone architecture after the menopause.

Authors+Show Affiliations

Department of Veterinary Basic Sciences, The Royal Veterinary College, London, United Kingdom.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11393781

Citation

Jessop, H L., et al. "Mechanical Strain and Estrogen Activate Estrogen Receptor Alpha in Bone Cells." Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, vol. 16, no. 6, 2001, pp. 1045-55.
Jessop HL, Sjöberg M, Cheng MZ, et al. Mechanical strain and estrogen activate estrogen receptor alpha in bone cells. J Bone Miner Res. 2001;16(6):1045-55.
Jessop, H. L., Sjöberg, M., Cheng, M. Z., Zaman, G., Wheeler-Jones, C. P., & Lanyon, L. E. (2001). Mechanical strain and estrogen activate estrogen receptor alpha in bone cells. Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research, 16(6), 1045-55.
Jessop HL, et al. Mechanical Strain and Estrogen Activate Estrogen Receptor Alpha in Bone Cells. J Bone Miner Res. 2001;16(6):1045-55. PubMed PMID: 11393781.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mechanical strain and estrogen activate estrogen receptor alpha in bone cells. AU - Jessop,H L, AU - Sjöberg,M, AU - Cheng,M Z, AU - Zaman,G, AU - Wheeler-Jones,C P, AU - Lanyon,L E, PY - 2001/6/8/pubmed PY - 2002/1/5/medline PY - 2001/6/8/entrez SP - 1045 EP - 55 JF - Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research JO - J Bone Miner Res VL - 16 IS - 6 N2 - Bone cells' early responses to estrogen and mechanical strain were investigated in the ROS 17/2.8 cell line. Immunoblotting with antiphosphorylated estrogen receptor a (ER-alpha) antibody showed that when these cells were exposed for 10 minutes to estrogen (10(-8) M) or a single period of cyclic dynamic strain (peak 3400 microepsilon, 1 Hz, 600 cycles), there was an increase in the intensity of a 66-kDa band, indicating phosphorylation of ser122 in the amino terminus of ER-alpha. Increased phosphorylation was detected within 5 minutes of exposure to estrogen and 5 minutes after the end of the period of strain. Estrogen and strain also activated the mitogen-activated protein kinase (MAPK) family member extracellular regulated kinase-1 (ERK-1). Increases in ERK activation coincided with increased ER-alpha phosphorylation. Activation of ERK-1 and the phosphorylation of ER-alpha, by both estrogen and strain, were prevented by the MAP kinase kinase (MEK) inhibitor U0126 and the protein kinase A (PKA) inhibitor (PKI). These data support previous suggestions that resident bone cells' early responses to strain and estrogen share a common pathway, which involves ER-alpha. This pathway also appears to involve PKA and ERK-mediated phosphorylation of ser122 within the amino terminus of ER-alpha. Reduced availability of this pathway when estrogen levels are reduced could explain diminished effectiveness of mechanically related control of bone architecture after the menopause. SN - 0884-0431 UR - https://www.unboundmedicine.com/medline/citation/11393781/Mechanical_strain_and_estrogen_activate_estrogen_receptor_alpha_in_bone_cells_ L2 - https://doi.org/10.1359/jbmr.2001.16.6.1045 DB - PRIME DP - Unbound Medicine ER -