The tyrosine phosphatase inhibitor vanadate protects osteoblasts from growth inhibition by glucocorticoids.

The tyrosine phosphatase inhibitor vanadate protects osteoblasts from growth inhibition by glucocorticoids.

Detalhes bibliográficos
Main Authors:	Hulley, P, Conradie, R, Titus, C, Hough, F
Formato:	Journal article
Publicado em:	1999

Registos relacionados

Vanadate protects osteoblasts in vitro and in vivo from glucocorticoid impairment of proliferation
Por: Hulley, P, et al.
Publicado em: (2002)

Pathogenesis of glucocorticoid osteoporosis: Role of tyrosine phosphatases
Por: Hulley, P, et al.
Publicado em: (2001)

Vanadate prevents glucocorticoid-induced apoptosis of osteoblasts in vitro and osteocytes in vivo.
Por: Conradie, M, et al.
Publicado em: (2007)

Glucocorticoid-induced osteoporosis in the rat is prevented by the tyrosine phosphatase inhibitor, sodium orthovanadate.
Por: Hulley, P, et al.
Publicado em: (2002)

Mitogen-activated protein kinase phosphatase 1/dual specificity phosphatase 1 mediates glucocorticoid inhibition of osteoblast proliferation.
Por: Horsch, K, et al.
Publicado em: (2007)

Glucocorticoids inhibit osteoblast proliferation via transcriptional upregulation of MKP-1: A prime target for the development of novel osteo-anabolic agents
Por: Hulley, P, et al.
Publicado em: (2003)

Inhibition of mitogen-activated protein kinase activity and proliferation of an early osteoblast cell line (MBA 15.4) by dexamethasone: role of protein phosphatases.
Por: Hulley, P, et al.
Publicado em: (1998)

Glucocorticoids induce rapid up-regulation of mitogen-activated protein kinase phosphatase-1 and dephosphorylation of extracellular signal-regulated kinase and impair proliferation in human and mouse osteoblast cell lines.
Por: Engelbrecht, Y, et al.
Publicado em: (2003)

Regulation of bim in glucocorticoid-mediated osteoblast apoptosis.
Por: Espina, B, et al.
Publicado em: (2008)

BIM is a novel regulator of glucocorticoid-induced apoptosis in osteoblasts
Por: Espina, B, et al.
Publicado em: (2006)

MECHANISMS OF OSTEOBLAST INHIBITION BY STEROIDS
Por: Hulley, P
Publicado em: (2004)

Rapid inhibitory effects of glucocorticoids on ERK activity and osteoblast proliferation occur via transcriptional upregulation of MKP-1
Por: Horsch, K, et al.
Publicado em: (2004)

Regulation of tyrosine phosphorylation cascades by phosphatases: What the actions of vanadium teach us
Por: Hulley, P, et al.
Publicado em: (2003)

Rapid inhibitory effects of glucocorticoids on ERK activity and osteoblast proliferation occur via transcriptional upregulation of MKP-1
Por: Horsch, K, et al.
Publicado em: (2004)

Alternative insulin signalling pathways in osteoblasts
Por: Langeveldt, C, et al.
Publicado em: (2002)

Bim as a potential target in osteoblast survival
Por: Espina, B, et al.
Publicado em: (2005)

Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases
Por: Wiljan Hendriks, et al.
Publicado em: (2018-02-01)

Alternative insulin signalling pathways in osteoblast cell lines
Por: Langeveldt, C, et al.
Publicado em: (2002)

The BH3-only protein BIM is upregulated in osteoblasts in response to dexamethasone treatment, growth factor deprivation and anoikis
Por: Espina, B, et al.
Publicado em: (2005)

Vanadate sensitive ATPase and phosphatase-activity in guard-cell protoplasts of Commelina
Por: Fricker, M, et al.
Publicado em: (1987)

Vanadate sensitive ATPase and phosphatase activity in guard cell protoplasts of Commelina
Por: Fricker, M, et al.
Publicado em: (1987)

Sodium Vanadate Treatment as a Shortcut Following Alkaline Phosphatase Cleavage
Por: Yu-Yuan Peter Wo, et al.
Publicado em: (1998-09-01)

Manzamenones Inhibit T-Cell Protein Tyrosine Phosphatase
Por: Jun'ichi Kobayashi, et al.
Publicado em: (2006-02-01)

Protein Tyrosine Phosphatase Biochemical Inhibition Assays
Por: Marek Baranowski, et al.
Publicado em: (2022-09-01)

The identification of transcriptional targets associated with osteoblast apoptosis signaling in response to growth factor withdrawal
Por: Liang, M, et al.
Publicado em: (2006)

The Role of MKP-1 in the Anti-Proliferative Effects of Glucocorticoids in Primary Rat Pre-Osteoblasts.
Por: Micheline Sanderson, et al.
Publicado em: (2015-01-01)

Lactoferrin protects osteoblasts and osteocytes from apoptosis
Por: Locklin, R, et al.
Publicado em: (2009)

Identification of Phomoxanthone A and B as Protein Tyrosine Phosphatase Inhibitors
Por: Runlei Yang, et al.
Publicado em: (2020-09-01)

Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies
Por: Zhendong Song, et al.
Publicado em: (2021-01-01)

The EYA tyrosine phosphatase activity is pro-angiogenic and is inhibited by benzbromarone.
Por: Emmanuel Tadjuidje, et al.
Publicado em: (2012-01-01)

The mechanism of allosteric inhibition of protein tyrosine phosphatase 1B.
Por: Shuai Li, et al.
Publicado em: (2014-01-01)

Inhibition of receptor tyrosine kinase signalling by small molecule agonist of T-cell protein tyrosine phosphatase
Por: Tähtinen Siri, et al.
Publicado em: (2010-01-01)

Activation of Ceramidase and Ceramide Kinase by Vanadate via a Tyrosine Kinase–Mediated Pathway
Por: Eiko Tada, et al.
Publicado em: (2010-01-01)

Osteoblast Differentiation on Collagen Scaffold with Immobilized Alkaline Phosphatase
Por: F Jafary, et al.
Publicado em: (2017-10-01)

The mode of action of the Protein tyrosine phosphatase 1B inhibitor Ertiprotafib.
Por: Ganesan Senthil Kumar, et al.
Publicado em: (2020-01-01)

Crystal structure of the vanadate-inhibited Ca(2+)-ATPase
Por: Clausen, J, et al.
Publicado em: (2016)

Chemical inhibition of bacterial protein tyrosine phosphatase suppresses capsule production.
Por: Alistair J Standish, et al.
Publicado em: (2012-01-01)

Glucocorticoid transiently upregulates mitochondrial biogenesis in the osteoblast
Por: Chien-Ning Hsu, et al.
Publicado em: (2020-01-01)

Protein Tyrosine Phosphatase 1B Inhibitors from the Stems of Akebia quinata
Por: Jin-Pyo An, et al.
Publicado em: (2016-08-01)

Role of receptor protein tyrosine phosphatase alpha (RPTPalpha) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels.
Por: Imbrici, P, et al.
Publicado em: (2000)