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As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website.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

Limited cleavage of cellular fibronectin by plasminogen activator purified from transformed cells

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

Overview

authors

  • Quigley, James
  • Gold, L. I.
  • Schwimmer, R.
  • Sullivan, L. M.

publication date

  • May 1987

journal

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

abstract

  • The substrate specificity and direct catalytic activity of plasminogen activator (PA) was examined under conditions where its natural substrate, plasminogen, was missing or inhibited. PA, purified from cultures of transformed chicken fibroblasts, was incubated with purified preparations of potential substrates. The adhesive glycoprotein fibronectin, isolated from normal chicken fibroblast extracellular matrix, underwent limited but specific cleavage by PA in the absence of plasminogen. Analysis of the cleavage products by polyacrylamide gels under both reducing and nonreducing conditions indicated that PA-mediated cleavage occurred near the carboxyl terminus of fibronectin but on the amino-terminal side of the interchain disulfide bridge, thus disrupting the native dimeric fibronectin molecule. Under the identical conditions, chicken ovalbumin was not cleaved while the established substrate, chicken plasminogen, was extensively converted to plasmin. A monoclonal antibody, directed against avian PA and shown to inhibit plasminogen-free, cell-mediated matrix degradation, specifically inhibited the fibronectin cleavage. A human PA, urokinase, also cleaved fibronectin under plasminogen-free conditions yielding a limited number of high molecular weight cleavage products.

subject areas

  • Animals
  • Avian Sarcoma Viruses
  • Cell Transformation, Neoplastic
  • Chick Embryo
  • Fibroblasts
  • Fibronectins
  • Humans
  • Plasminogen Activators
  • Substrate Specificity
  • Thrombin
  • Urokinase-Type Plasminogen Activator
scroll to property group menus

Identity

PubMed Central ID

  • PMC304741

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.84.9.2776

PubMed ID

  • 3033662
scroll to property group menus

Additional Document Info

start page

  • 2776

end page

  • 2780

volume

  • 84

issue

  • 9

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

  • About
  • Contact Us
  • Support