Search PubMed⌕ Search

Biomedical subjects

G Till

Publications and source records attributed to G Till.

25 records · Page 2Linked to original sources

Enhancement of the PGE1 response of macrophages by concanavalin A and colchicine.

The effect of concanavalin A (Con A) and colchicine on the prostaglandin E1 (PGE1)-mediated cyclic AMP generation in rat peritoneal macrophages have been studied. Although Con A and colchicine by themselves did not affect cyclic AMP levels, they greatly enhanced cyclic AMP production induced by PGE1. There was not only augmentation of cyclic AMP levels at maximally active concentrations of PGE1, but also an increased sensitivity to low (inactive) concentrations of PGE1. Except for lentil lectin, none of the other lectins affected PGE1 sensitivity whereas lumicolchicine was as effective as colchicine. In addition, both Con A and colchicine raised the sensitivity to isoproterenol and choleraenterotoxin. Although details of the mechanisms by which Con A or colchicine influenced the membrane-bound adenyl cyclase and PGE1 receptors remain unclear, these observations suggest that certain alterations of the cell membrane may render macrophages more susceptible to the regulating effects of prostaglandins.

Adenylyl Cyclases↗

Release of cyclic AMP from macrophages by stimulation with prostaglandins.

The effect of various prostaglandins (PG)on the generation of cyclic AMP in rat peritoneal macrophages has been studied in vitro. PGE1 produced a rapid intracellular accumulation of cyclic AMP which was followed by its release into the extracellular space. More cyclic AMP was released with prostaglandins of the E-type than with A- and F-types. It is suggested that release of cyclic AMP from macrophages may participate in the modulation of leukocyte function.

Animals↗

Two distinct chemotactic factor inactivators in human serum.

The chemotactic factor inactivator (CFI) has been isolated from whole human serum by a combination of techniques including salt precipitation, anionic exchange, and gel filtration chromatography. Two inactivators have been obtained, a beta-globulin with a sedimentation velocity of approximately 7S and an alpha-globulin with a sedimentation velocity of approximately 4S. The former has a specificity for inactivation of the chemotactic activity associated with the C3 fragments, whereas the C5 chemotactic fragment is specifically inactivated by the alpha-globulin CFI. CFI in crude fractions of human serum is heat labile, time and temperature dependent for its activity, and pH dependent, expressing optimal activity at a pH range of 7.2 to 7.4.

Alpha-Globulins↗