@entity14172 ( @entity14172 ) is an important trophic factor for controlling the actions of @entity442 in @entity1 dermal fibroblasts and porcine aortic smooth muscle cells. When @entity14172 is associated with extracellular matrix, it acts to enhance the cell growth response to @entity442 . The amount of @entity14172 within the extracellular matrix is related in part to the amount that is present in conditioned medium, which is related to its rate of synthesis and degradation. A @entity563 protease that degrades @entity14172 is present in the conditioned medium of both of these cell types. Because the @entity14172 protease activity that is secreted by fibroblasts has been shown to be due to the complement components @entity6649 and C1s, these studies were undertaken to determine whether smooth muscle cells also secreted these proteases and to identify some of the factors that regulate their secretion by both cell types. Both smooth muscle cells and @entity1 fibroblasts were shown to release @entity6746 s into conditioned medium. Both @entity6649 and C1s were detected as activated forms, as determined by @entity214 -PAGE using reducing conditions. The addition of increasing concentrations of either @entity1356 or @entity310 resulted in increased synthesis of C1s by fibroblasts and smooth muscle cells, and they each increased @entity6649 release. @entity310 (50 ng/ml) and @entity1356 (20 ng/ml) resulted in maximum stimulation of release of both proteases. In contrast @entity619 (10(-7) M) had no effect on C1s release and stimulated @entity6649 release only by smooth muscle cells. To determine the physiological significance of this increase in @entity6649 and C1s, the amount of @entity14172 protease activity that was present in conditioned medium was determined before and after exposure to @entity310 , IL-beta, and @entity619 . All three compounds resulted in an increase in the amount of @entity14172 proteolytic activity. @entity619 inhibited the release of C(1) inhibitor from fibroblasts, and this contributed to the net increase in proteolytic activity. @entity310 inhibited the smooth muscle cell DNA synthesis response to @entity442 , but the effect of @entity442 was partially restored by the addition of C1 inhibitor. In conclusion, both @entity6649 and C1s are released by cultured fibroblasts, and the release of each into fibroblast or porcine smooth muscle cells medium is stimulated by @entity310 and @entity1356 . This increase results in a net increase in @entity14172 proteolysis, which has the potential to modify @entity442 and @entity14172 actions.

Control of insulin-like growth factor binding protein-5 protease synthesis and secretion by XXXX fibroblasts and porcine aortic smooth muscle cells.

@entity1 :: ('9606', 'Species') :: ['human'] @entity6746 :: ('3183', 'Gene') :: ['C1r and C1'] @entity1356 :: ('3553', 'Gene') :: ['IL-1beta'] @entity310 :: ('7124', 'Gene') :: ['TNFalpha'] @entity442 :: ('3479', 'Gene') :: ['IGF-I'] @entity6649 :: ('715', 'Gene') :: ['C1r'] @entity619 :: ('MESH:D003907', 'Chemical') :: ['Dexamethasone', 'dexamethasone'] @entity563 :: ('CHEBI:17822', 'Chemical') :: ['serine'] @entity14172 :: ('3488', 'Gene') :: ['IGF binding protein-5', 'IGFBP-5'] @entity214 :: ('CHEBI:8984', 'Chemical') :: ['SDS']
@entity1 :: (9606,Species) :: ['human']
