Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Distinct spatio-temporal Ca(2+) signaling elicited by integrin alpha 2 beta 1 and glycoprotein VI under flow

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Mazzucato, M.
  • Cozzi, M. R.
  • Battiston, M.
  • Jandrot-Perrus, M.
  • Mongiat, M.
  • Marchese, P.
  • Kunicki, T. J.
  • Ruggeri, Zaverio
  • De Marco, Luigi

publication date

  • September 2009

journal

  • Blood  Journal

abstract

  • We studied how integrin alpha2beta1 and glycoprotein VI (GPVI) contribute to collagen-induced platelet activation under flow conditions by evaluating stable adhesion and intracellular Ca(2+) concentration ([Ca(2+)](i)) of FLUO 3-AM-labeled platelets perfused over acid-soluble type I or microfibrillar type VI collagen. Adhering platelets displayed 2 kinds of [Ca(2+)](i) oscillations. Rapid alpha-like peaks were unaffected by the membrane-impermeable Ca(2+) chelator ethyleneglycoltetraacetic acid but abolished by membrane-permeable BAPTA-AM. Longer-lasting gamma-like peaks were always preceded by at least one alpha-like peak and abolished by intracellular or extracellular Ca(2+) chelation. Inhibition of phosphatidylinositol 3-kinase or phospholipase C and modulation of cyclic nucleotides, but not blockage of adenosine diphosphate receptors, prevented both Ca(2+) responses. Human or mouse platelets lacking GPVI function exhibited alpha-like but not gamma-like Ca(2+) peaks, whereas those lacking alpha2beta1 showed markedly reduced to absent alpha-like and no gamma-like Ca(2+) peaks. Specific alpha2beta1 ligation induced alpha-like but not gamma-like peaks. Thus, alpha2beta1 may generate Ca(2+) signals that are reinforced by GPVI and required for subsequent longer-lasting Ca(2+) oscillation mediated by GPVI through transmembrane ion flux. Our results delineate a GPVI-independent signaling role of alpha2beta1 in response to collagen stimulation.

subject areas

  • Animals
  • Blood Circulation
  • Blood Platelets
  • Calcium Signaling
  • Cells, Cultured
  • Chromones
  • Collagen Type I
  • Enzyme Inhibitors
  • Humans
  • Integrin alpha2beta1
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Morpholines
  • Phosphatidylinositol 3-Kinases
  • Platelet Adhesiveness
  • Platelet Membrane Glycoproteins
  • Time Factors
scroll to property group menus

Identity

PubMed Central ID

  • PMC2756134

International Standard Serial Number (ISSN)

  • 0006-4971

Digital Object Identifier (DOI)

  • 10.1182/blood-2008-12-193490

PubMed ID

  • 19622836
scroll to property group menus

Additional Document Info

start page

  • 2793

end page

  • 2801

volume

  • 114

issue

  • 13

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support