Premium
Modulation of synthesis of specific proteins in endothelial cells by copper, cadmium, and disulfiram: An early response to an angiogenic inducer of cell migration
Author(s) -
Hannan G. N.,
McAuslan B. R.
Publication year - 1982
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041110213
Subject(s) - fibronectin , disulfiram , endothelial stem cell , chemistry , angiogenesis , inducer , stimulation , cell culture , cell , copper , biochemistry , protein biosynthesis , microbiology and biotechnology , biology , in vitro , endocrinology , cancer research , genetics , gene , organic chemistry
Copper, cadmium, and disulfiram (an ionophore for copper) modulate the synthesis of several polypeptides in two clonal lines of bovine aortal endothelial cells. After treatment of type 1 endothelial cells with 10 −3 M CuSO 4 or 10 −5 M CdCl 2 four cell‐associated polypeptides (M r = 28,000, 32,000, 73,000, and 83,000 daltons) were induced. In contrast, in Type 2 endothelial cells, which have cultural characteristics distinct from Type 1, only one new cell‐associated protein (M r = 32,000 and 40,000 daltons) was induced. Other differences are revealed by analyses of proteins secreted into the growth medium. In particular low levels of only CuSO 4 (10 −6 M) enhanced the synthesis in Type 2 cells of a protein (M r = 220,000 daltons) identified as fibronectin. Since only copper ions induced fibronectin, we propose that the mechanism of induction of fibronectin synthesis, in contrast to the induction of cell−associated polypeptides, does not involve a sulphydryl−containing receptor molecule. It is suggested that the specific enhancement of fibronectin synthesis by copper ions may be a controlling event in the stimulation by copper ions of endothelial cell migration and angiogenesis.