de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Shear stress mediates tyrosylprotein sulfotransferase isoform shift in human endothelial cells

MPS-Authors

Goettsch,  Sandra
Max Planck Institute of Molecular Physiology, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons98678

Bayer,  Peter
Sonstige Wissenschaftliche Organisationseinheiten, Max Planck Institute of Molecular Physiology, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Goettsch, S., Goettsch, W., Morawietz, H., & Bayer, P. (2002). Shear stress mediates tyrosylprotein sulfotransferase isoform shift in human endothelial cells. Biochemical and Biophysical Research Communications, 294(3): 1, pp. 541-546. Retrieved from http://dx.doi.org/10.1016/S0006-291X(02)00511-9.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-0E5C-F
Abstract
In this study, we examined expression of tyrosylprotein sulfotransferase (TPST) isoforms TPST1 and TPST2 in primary cultures of human umbilical vein endothelial cells. For the first time coexpression. of both isoforms is shown in primary human cells. Application of physiological levels of shear stress regulates expression of TPST isoforms in a time- and dose-dependent manner. Sustained application of arterial laminar shear stress causes downregulation of TPST1 mRNA and protein expression, while TPST2 is upregulated. This TPST isoform shift is mediated by different signaling pathways. Shear stress-dependent downregulation of TPST1 involves protein kinase C, while upregulation of TPST2 is mediated by a tyrosine kinase-dependent pathway. (C) 2002 Elsevier Science (USA). All rights reserve