Article (Scientific journals)
Spatiotemporal segregation of endothelial cell integrin and nonintegrin extracellular matrix-binding proteins during adhesion events.
Basson, C. T.; Knowles, W. J.; Bell, L. et al.
1990In Journal of Cell Biology, 110 (3), p. 789-801
Peer Reviewed verified by ORBi
 

Files


Full Text
(1990) BASSON J CELL BIOL .pdf
Publisher postprint (5.08 MB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Acid Phosphatase/metabolism; Amino Acid Sequence; Animals; Aorta; Cattle; Cell Adhesion/drug effects; Cell Movement; Cells, Cultured; Endothelium, Vascular/physiology; Extracellular Matrix/physiology; Fibrinogen/physiology; Fibronectins/physiology; Fluorescent Antibody Technique; Integrins/physiology; Laminin/physiology; Molecular Sequence Data; Oligopeptides/chemical synthesis/metabolism/pharmacology
Abstract :
[en] Bovine aortic endothelial cell (BAEC) attachments to laminin, fibronectin, and fibrinogen are inhibited by soluble arginine-glycine-aspartate (RGD)-containing peptides, and YGRGDSP activity is responsive to titration of either soluble peptide or matrix protein. To assess the presence of RGD-dependent receptors, immunoprecipitation and immunoblotting studies were conducted and demonstrated integrin beta 1, beta 3, and associated alpha subunits as well as a beta 1 precursor. Immunofluorescence of BAECs plated on laminin, fibronectin, and fibrinogen reveals different matrix-binding specificities of each of these integrin subclasses. By 1 h after plating, organization of beta 1 integrin into fibrillar streaks is influenced by laminin and fibronectin, whereas beta 3 integrin punctate organization is influenced by fibrinogen and the integrin spatial distribution changes with time in culture. In contrast, the nonintegrin laminin-binding protein LB69 only organizes after cell-substrate contact is well established several hours after plating. Migration of BAECs is also mediated by both integrin and nonintegrin matrix-binding proteins. Specifically, BAEC migration on laminin is remarkably sensitive to RGD peptide inhibition, and, in its presence, beta 1 integrin organization dissipates and reorganizes into perinuclear vesicles. However, RGD peptides do not alter LB69 linear organization during migration. Similarly, agents that block LB69--e.g., antibodies to LB69 as well as YIGSR-NH2 peptide--do not inhibit attachment of nonmotile BAECs to laminin. However, both anti-LB69 and YIGSR-NH2 inhibit late adhesive events such as spreading. Accordingly, we propose that integrin and nonintegrin extracellular matrix-binding protein organizations in BAECs are both temporally and spatially segregated during attachment processes. High affinity nonintegrin interaction with matrix may create necessary stable contacts for longterm attachment, while lower affinity integrins may be important for initial cell adhesion as well as for transient contacts of motile BAECs.
Disciplines :
Oncology
Biochemistry, biophysics & molecular biology
Author, co-author :
Basson, C. T.
Knowles, W. J.
Bell, L.
Albelda, S. M.
Castronovo, Vincenzo ;  Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biologie générale et cellulaire - GIGA-R : Labo de recherche sur les métastases
Liotta, L. A.
Madri, J. A.
Language :
English
Title :
Spatiotemporal segregation of endothelial cell integrin and nonintegrin extracellular matrix-binding proteins during adhesion events.
Publication date :
1990
Journal title :
Journal of Cell Biology
ISSN :
0021-9525
eISSN :
1540-8140
Publisher :
Rockefeller University Press, New York, United States - New York
Volume :
110
Issue :
3
Pages :
789-801
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 25 May 2010

Statistics


Number of views
57 (7 by ULiège)
Number of downloads
83 (1 by ULiège)

Scopus citations®
 
95
Scopus citations®
without self-citations
71
OpenCitations
 
68

Bibliography


Similar publications



Contact ORBi