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Effect of extracellular matrix proteins on vascular smooth muscle cell phenotype
Author(s) -
Hayward I. P.,
Bridle K. R.,
Campbell G. R.,
Underwood P. A.,
Campbell J. H.
Publication year - 1995
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1995.1019
Subject(s) - vitronectin , laminin , fibronectin , basal lamina , extracellular matrix , microbiology and biotechnology , cell adhesion , adhesion , myofilament , phenotype , cytoplasm , chemistry , vascular smooth muscle , matrix (chemical analysis) , biology , cell , anatomy , myocyte , biochemistry , ultrastructure , endocrinology , smooth muscle , organic chemistry , chromatography , gene
The effect on phenotypic expression of rabbit vascular smooth muscle cells (SMC) of the interstitial matrix proteins collagen I and fibronectin, the basal lamina proteins collagen IV and laminin, and the serum adhesion protein vitronectin was examined in culture. Experiments were performed in foetal calf serum stripped of fibronectin and vitronectin to eliminate their confounding effects. All the proteins promoted adhesion to the plastic culture dish (in a concentration dependent manner) of SMC freshly isolated from the artery wall. These cells had a high volume density of myofilaments (V v myo) in their cytoplasm. Laminin was best at maintaining SMC with a high V v myo (V v myo = 49.8%) followed by collagen IV (41.7%). Cells plated on vitronectin showed the lowest V v myo (31.3%). The results support the concept that the SMC basal lamina has a role in maintaining cells in the high V v myo phenotype.