Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0851184 (thinning)
 11,252 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phenothiazines (chlorpromazine, trifluoperazine, prochlorperazine, and fluphenazine) showed dose-dependent inhibition of phagocytosis of latex particles by cultured chick retinal pigment epithelial cells at concentrations of 10(-5)-10(-14) mol/l. Calmodulin antagonists (W-5, W-7, W-12, and W-13) showed similar effects as phenothiazines at concentrations of 10(-5)-10(-14) mol/l. These reactions were partially reversible at a concentration of 10(-9) mol/l. Cells cultured for 3 days in the presence of 10(-5) mol/l chlorpromazine or 10(-5) mol/l W-7 demonstrated morphologic alterations in their microvilli which were similar to those seen after cytochalasin B treatment, i.e., thinning and elongation of the microvilli with honeycomb-like changes.
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PMID:Effects of phenothiazines on cultured retinal pigment epithelial cells. 286 64

Some metal ions, e.g. Hg2+, Cd2+ and Al3+, can have the effects as ecotoxicological agents, of causing eggshell thinning and breakage in birds. In a homogenate of the Ca2+-secreting part of the eggshell gland mucosa, a study was made of the influence of Hg2+, Cd2+, Cu2+, Pb2+, methyl-Hg+, Zn2+, V3+, Al3+ and Ni2+ in different concentrations on the rate of ATP-dependent 10(-4) M Ca2+ binding. All compounds had an inhibitory action. The most potent metal (Hg2+) produced 50% inhibition (IC50) at 1.1 X 10(-6) M, whereas this value for the least potent compound (Ni2+) was 9 X 10(-4) M. The specific Ca2+-Mg2+-ATPase activity was also inhibited by the tested metal ions. In all cases except methyl-Hg+ the IC50 for this activity was lower than that for Ca2+ binding. The most potent ion in this respect was Cd2+, with an IC50 of 8 X 10(-8) M, and the least potent was methyl-Hg+, with an IC50 of 1.4 X 10(-3) M. Pb2+ and Cd2+ in a concentration range of 10(-5)-10(-4) stimulated the Mg2+-ATPase activity, however, to almost the same extent as 10(-4) M Ca2+. A possible explanation for this effect is that these ions may have an affinity for sites of Ca2+ binding of the polypeptide calmodulin and thereby influence the Ca2+ metabolism of the shell gland mucosa.
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PMID:Effect of some metal compounds on the Ca2+ binding and Ca2+-Mg2+-ATPase activity of eggshell gland mucosa homogenate from the domestic fowl. 294 86