您要找的是不是:
n. 次磷酸盐
$firstVoiceSent
- 来自原声例句
请问您想要如何调整此模块？
感谢您的反馈，我们会尽快进行适当修改！
请问您想要如何调整此模块？
感谢您的反馈，我们会尽快进行适当修改！细胞库/细胞培养
ELISA试剂盒
实验室仪器/设备
原辅料包材
体外检测试剂
&&Anti-Hypophosphorylated Neurofilament H antibody [NF-200]
Anti-Hypophosphorylated Neurofilament H antibody [NF-200]
&丁香通采购保障计划，让您的采购更放心。
供应商信息
商家诚信度：
成立时间：2013年
入驻丁香通年限：4年
商家等级：金牌客户
产品信息完整度：54%
联系人：闵经理
若您通过QQ未能联系到商家，您可以给商家发送站内信，与其取得联系。
扫一扫微信联系商家
地址：南京市建邺区云锦路58号
该商家已通过实名认证
数据正在加载，请稍候...
扫一扫微信联系商家
联系人: 闵经理
（联系我时请说在丁香通看到的）
30秒填写信息，方便商家与您及时沟通
您正在向&&发送关于产品&&的询问
登录丁香园账号即可使用多地址管理，
*&电话和Email请至少填写一项
给商家留言
我对您在丁香通发布的“Anti-Hypophosphorylated Neurofilament H antibody [NF-200]” 非常感兴趣。请联系我并提供报价。
点击“立即发送”后，商家将在1个工作日内与您取得联系。
让更多商家看到我的询价
丁香通采购热线：400-
Copyright (C)
DXY All Rights Reserved.Hypophosphorylated and inactive Pyk2 associates with paxillin at the microtubule organizing... - Abstract - Europe PMC
Europe PMC requires Javascript to function effectively.
Either your web browser doesn't support Javascript or it is currently turned off. In the latter case, please
turn on Javascript support in your web browser and reload this page.
Search worldwide, life-sciences literature
Jo?lle St-Pierre
Tara L Lysechko
Hanne L Ostergaard
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada.
[):718-730]
Journal Article, Research Support, Non-U.S. Gov't
10.1016/j.cellsig.
Pyk2 is a non-receptor tyrosine kinase that regulates cellular adhesion. We generated antibodies to a peptide corresponding to the N-terminus (NT) of Pyk2 and another to a portion of the C-terminal (CT) domain. Only the CT antiserum recovered paxillin-associated Pyk2. These antibodies recognized overlapping but biochemically distinct molecular species of Pyk2 since the CT antiserum recovered Pyk2 after NT antibody immunodepletion. Furthermore, the CT antibody could not immunoblot NT antibody-captured Pyk2. Phosphorylation partially accounts for the differential binding of these antibodies as dephosphorylation of Pyk2 recovered with the NT antibodies allows for recognition by the CT antibody. Additionally, Pyk2 recovered with the NT antibody displays increased serine/threonine phosphorylation. We suggest that the NT epitope is inaccessible to the antibody because Pyk2 is in a closed confirmation in association with paxillin. Upon induction of serine and/or threonine phosphorylation of Pyk2, it opens to a confirmation that allows for antibody binding to the NT epitope but at the same time no longer binds paxillin or the CT antiserum. These antibodies also display differential staining of Pyk2 in both T cells and macrophages. Pyk2 recognized by the CT antibody, but not the NT antibody, colocalized with paxillin at the microtubule-organizing center (MTOC). The MTOC-bound Pyk2 was not tyrosine phosphorylated upon T cell activation. We hypothesize that a reservoir of primarily inactive Pyk2 associates with paxillin at the MTOC, which may allow for rapid delivery of Pyk2 to specific sites of adhesion.
)- subscription required
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
Show all items
CitePeer Related ArticlesVolume 47, Issue 13
ARVO Annual Meeting Abstract Oxidative Stress Induces Secretion of Hypophosphorylated Soluble CD44 by Trabecular Meshwork Cells in Culture
Author Affiliations & Notes
M.J. Nolan
Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, IL
B.Y. J. T. Yue
Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, IL
J.R. Samples
Ophthalmology, Casey Eye Institute, Portland, OR
P.A. Knepper
Ophthalmology and Visual Sciences, University of Illinois at Chicago, Chicago, IL Ophthalmology, Northwestern University, Chicago, IL
M.J. Nolan, N B.Y.J.T. Yue, N J.R. Samples, N P.A. Knepper, None.
Illinois Society for the Prevention of Blindness, Midwest Eye Banks, Katherine Connelly and Rosemary O'Meara Research Funds, NIH EY05628 (Yue), NIH EY01792 (UIC Core)
Investigative Ophthalmology & Visual Science May 2006, Vol.47, 1840. doi:
User Alerts
You are adding an alert for:
Oxidative Stress Induces Secretion of Hypophosphorylated Soluble CD44 by Trabecular Meshwork Cells in Culture
You will receive an email whenever this article is corrected, updated, or cited in the literature. You can manage this and all other alerts in
The alert will be sent to:
This feature is available to Subscribers Only
M.J. Nolan, B.Y. J. T. Yue, J.R. Samples, P.A. K
Oxidative Stress Induces Secretion of Hypophosphorylated Soluble CD44 by Trabecular Meshwork Cells in Culture . Invest. Ophthalmol. Vis. Sci. ):1840.
Download citation file:
© 2017 Association for Research in Vision and Ophthalmology.
Purpose: :
Protein phosphorylation is a regulatory feature of several neurodegenerative diseases. Recently, we reported that a 32–kDa ectodomain fragment of CD44, i.e., soluble CD44 (sCD44), is hypo–phosphorylated in primary open angle glaucoma (POAG) aqueous humor and is cytotoxic to trabecular meshwork (TM) and retinal ganglion cells in cell culture. This study examined whether metabolic stress of TM cells results in hypophosphorylation of the ectodomain of sCD44.
Methods: :
Human TM cells were grown in Eagles mimimum essential medium (MEM) containing 10% fetal calf serum (FCS) until confluent. The cells were washed twice with PBS and incubated in MEM containing 0.1% FCS with 1, 10 mM lactate or PBS. The media was aspirated and replenished with fresh media containing 1, 10 mM lactate or PBS at selected time points ––3, 6, 12, 24, 36 and 48 hours. The concentration of sCD44 in the media at each time point was determined by ELISA. Aliquots of the media at each time point were immunoprecipitated, electrophoresed, and subjected to western blot analysis using anti–CD44 and phospho–specific serine/threonine antibodies. The blots were analyzed by densitometry to determine the ratio of phosphorylation to sCD44 protein.
Results: :
Lactate treatment resulted in a time– and dose–dependent release of sCD44 into the media. sCD44 concentration in the media increased with 1 mM or 10 mM lactate after 3 hours of treatment (P&0.04) and the sCD44 concentration remained elevated in the 10 mM lactate treated cells. Western blot analysis of the 32–kDa sCD44 phosphorylation status in the 10 mM lactate treated media showed a progressive decrease in serine/threonine phosphorylation after 6 hours of lactate treatment. Densitometry indicated that the control media showed an increased in phosphorylation of sCD44 whereas 10 mM lactate treated cell media showed a three–fold decrease in phosphorylation after 12, 24, 36, and 48 hours.
Conclusions: :
Metabolic stress, as exemplified by lactate treatment of TM cells, caused the release of sCD44 and decreased the phosphorylation of sCD44. Lactate treatment of TM cells is a useful cell model of cell stress and may be applicable to cell stress responses in POAG.
Keywords: stress response o outflow: trabecular meshwork o protein modifications-post translational
Advertisement
To View More...
Purchase this article with an account.
This PDF is available to Subscribers Only
You must be signed into an individual account to use this feature.