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J. Biol. Chem., Vol. 261, Issue 23, 10478-10481, Aug, 1986
CP Chiang and M Nilsen-Hamilton
Growth regulators such as epidermal growth factor (EGF) and type beta
transforming growth factor (TGF-beta) regulate the synthesis and secretion
of certain proteins by cells in culture. The secretion pattern of each cell
line and the effect of growth regulators on the secretion pattern are
unique. EGF increased the secreted and intracellular levels of
mitogen-regulated protein (MRP) and major excreted protein (MEP) by Swiss
3T3 cells. MRP is related by sequence to prolactin. MEP is a thiol protease
located intracellularly in the lysosomes. EGF also selectively induced a
52,000-dalton mitogen-induced protein (MIP 52) secreted by human
fibroblasts. Two types of TGF-betas were tested for their effects on the
expression of secreted proteins in mouse and human fibroblasts: TGF-beta
from human platelets and a growth inhibitor (GI/TGF-beta) secreted by BSC-1
cells. Each selectively decreased the levels of the two secreted proteins
induced by growth factors in mouse embryo 3T3 cells and one secreted
protein induced by growth factors in human fibroblasts. Platelet TGF-beta
and GI/TGF-beta also induced one 48,000-dalton protein secreted by human
fibroblasts. Synthesis of DNA and the incorporation of [35S]methionine into
total protein in Swiss 3T3 cells were not affected by platelet TGF-beta or
GI/TGF-beta. Thus, the inhibitory effect of platelet TGF-beta on the
synthesis and secretion of these three proteins is due to a specific effect
of platelet TGF-beta on the regulation of MRP and MEP that does not
interfere with the ability of EGF to stimulate DNA or protein synthesis.
Opposite and selective effects of epidermal growth factor and human platelet transforming growth factor-beta on the production of secreted proteins by murine 3T3 cells and human fibroblasts
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