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As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website.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

Monoclonal-antibodies to a particulate superoxide-forming system stimulate a respiratory burst in intact guinea-pig neutrophils

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

Overview

authors

  • Berton, G.
  • Rosen, Hugh
  • Ezekowitz, R. A. B.
  • Bellavite, P.
  • Serra, M. C.
  • Rossi, F.
  • Gordon, S.

publication date

  • June 1986

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • Monoclonal rat antibodies were produced against a subcellular preparation of phorbol 12-myristate 13-acetate (PMA)-stimulated guinea pig neutrophils that retains NADPH-oxidase activity. Two antibodies, 1A10.4 and IG4, were isolated that bind to a surface antigen restricted to guinea pig neutrophils from bone marrow and peritoneal exudate and to macrophages and that trigger a respiratory burst in neutrophils in the presence of cytochalasin B. Intact antibody 1A10.4, subclass IgG2c, can trigger superoxide anion release directly; F(ab')2 fragments of 1A10.4 and intact IG4 require further cross-linking by F(ab')2 fragments of anti-rat immunoglobulin antibody. Both antibodies recognize the same antigen, a proteolipid of apparent molecular mass 10 kDa. Immunoprecipitation of solubilized oxidase activity with 1A10.4 brings down this activity as part of a macromolecular complex. Surface expression of the antigen is increased on treatment of cells with both PMA and cytochalasin B. 1A10.4 also triggers release of the granule enzyme beta-glucuronidase. Triggering of a respiratory burst by the antibodies appears distinct from the PMA and fMet-Leu-Phe signalling systems. These studies indicate that the antigen defined by antibodies 1A10.4 and IG4 becomes associated with the superoxide anion-generating system of neutrophils but may play a more general role in signal transduction in phagocytic cells.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Cell Membrane
  • Cytochalasin B
  • Flow Cytometry
  • Glucuronidase
  • Guinea Pigs
  • Molecular Weight
  • Multienzyme Complexes
  • NADH, NADPH Oxidoreductases
  • Neutrophils
  • Oxygen Consumption
  • Proteolipids
  • Superoxides
  • Tetradecanoylphorbol Acetate
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.83.11.4002

PubMed ID

  • 3012541
scroll to property group menus

Additional Document Info

start page

  • 4002

end page

  • 4006

volume

  • 83

issue

  • 11

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

  • About
  • Contact Us
  • Support