𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Estrogen stimulates protein tyrosine phosphorylation and Src kinase activity in avian osteoclasts

✍ Scribed by Kristen D. Brubaker; Carol V. Gay

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
331 KB
Volume
76
Category
Article
ISSN
0730-2312

No coin nor oath required. For personal study only.

✦ Synopsis

The estrogen, 17␤-estradiol, stimulated a profound increase in phosphotyrosine immunostaining of proteins that localized along the site of attachment in avian osteoclasts within 1 min of treatment. By 10 min, this rapidly occurring event had returned to basal levels. Pretreatment with 1 µM herbimycin A, a tyrosine kinase inhibitor, prevented the response. Immunoblotting revealed that Src kinase was one of the phosphorylated intermediates. Src kinase also appeared to translocate to the periphery of the cells during the 1 min 17␤-estradiol treatment and became dispersed by 10 min. Src kinase activity measurements indicated an increase in phosphotransferase activity after the 1 min estradiol treatment; this effect diminished with longer exposures to estrogen. Pretreatment of osteoclasts with 1 µg/ml cytochalasin B, an inhibitor of actin polymerization, delayed the appearance of increased phosphotyrosine immunostaining at attachment sites, possibly through inhibition of Src kinase translocation. These findings demonstrate that estrogen stimulates rapid tyrosine phosphorylation in osteoclasts, a process that involves activation and translocation of Src kinase to the plasma membrane.

📜 SIMILAR VOLUMES

Src protein and tyrosine-phosphorylated
Src protein and tyrosine-phosphorylated protein profiles in marrow stroma during osteogenic stimulation
✍ Benjamin Y. Klein; Rubina Levitzki; Hannah Ben-Bassat 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 250 KB

Src protein is essential for the regulation of bone turnover primarily via bone resorption because it is required in osteoclast differentiation and function. We followed temporal changes of Src protein abundance in marrow stromal cells induced to mineralize by dexamethasone (DEX), growth in cold tem

Activation of Src kinase by protein–tyro
Activation of Src kinase by protein–tyrosine phosphatase–PEST in osteoclasts: Comparative analysis of the effects of bisphosphonate and protein–tyrosine phosphatase inhibitor on Src activation in vitro
✍ Meenakshi A. Chellaiah; Michael D. Schaller 📂 Article 📅 2009 🏛 John Wiley and Sons 🌐 English ⚖ 403 KB 👁 2 views

## Abstract PTP–PEST is involved in the regulation of sealing ring formation in osteoclasts. In this article, we have shown a regulatory role for PTP–PEST on dephosphorylation of c‐Src at Y527 and phosphorylation at Y418 in the catalytic site. Activation of Src in osteoclasts by over‐expression of

Mitogen-activated protein kinase activat
Mitogen-activated protein kinase activation in hepatocyte growth factor–stimulated rat hepatocytes: Involvement of protein tyrosine kinase and protein kinase C
✍ T Adachi; S Nakashima; S Saji; T Nakamura; Y Nozawa 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 422 KB 👁 1 views

nases. These results suggest that PTK, Ras, and PKC Hepatocyte growth factor (HGF) stimulated mitogenplay roles in MAP kinase activation induced by HGF and activated protein (MAP) kinases and MAP kinase kinase that MAP kinase activation resulting in AA release is in primary cultured rat hepatocytes.

Variable effects of tyrosine kinase inhi
Variable effects of tyrosine kinase inhibitors on avian osteoclastic activity and reduction of bone loss in ovariectomized rats
✍ Harry C. Blair; S. Elizabeth Jordan; T. Greg Peterson; Stephen Barnes 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 836 KB

We compared the effects of the tyrosine kinase inhibitor genistein, a naturally occurring isoflavone, to those of tyrphostin A25, tyrphostin A47, and herbimycin on avian osteoclasts in vitro. Inactive analogs daidzein and tyrphostin A1 were used to control for nonspecific effects. None of the tyrosi

Studies on the mechanism of rapid activa
Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A
✍ Olga Mazina; Sujin Park; Hiromi Sano; Patrick Wong; Fumio Matsumura 📂 Article 📅 2005 🏛 John Wiley and Sons 🌐 English ⚖ 235 KB 👁 2 views

While the process of the Ah receptor activation leading to cytochrome P450 induction has been well studied, the mechanism and the process through which the Ah receptor activates tyrosine kinases, within a few minutes of its ligand binding, is not known. Previously, it was reported by Tannheimer et a

Protein tyrosine kinase inhibitors incre
Protein tyrosine kinase inhibitors increase cytosolic calcium and inhibit actin organization as resorbing activity in rat osteoclasts
✍ Hiroshi Kajiya; Koji Okabe; Fujio Okamoto; Takashi Tsuzuki; Hiroyuki Soeda 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 270 KB

Although there is evidence that protein tyrosine kinase inhibitors (PTKIs) suppress bone resorption activity, the mechanism of action of these compounds on osteoclastic bone resorption remains obscure. In the present study, we investigated the effect of PTKIs on cytosolic Ca(2+) concentration ([Ca(2