Biomedical subjects

C P Setton

Publications and source records attributed to C P Setton.

4 recordsLinked to original sources

PubMed1995

Biochemical and morphological changes in the developing kidney.

We have studied microsomal phospholipid, cholesterol and protein concentration in rat renal papilla, medulla and cortex during postnatal development, and the relationship between these membranes biochemical parameters and morphological changes. We also determined DNA concentration in each kidney zone. No changes were observed either in papillary microsomal phospholipids, proteins and cholesterol or in DNA concentration from 10-to 70-day-old rats. Medullary microsomal proteins and cholesterol did not change but a significant increase was observed in the microsomal phospholipid concentration during development; in this case, medullary DNA was significantly lower at 70 than at 10 days. In contrast, all biochemical parameters in renal cortex were significantly higher during development except for DNA concentration which suffered a great decrease. These biochemical findings demonstrate that the developmental pattern is different in each zone of the kidney and confirm the fact that the papilla, in newborn rats, is almost fully developed whereas the renal cortex and medulla are immature.

Aging↗

PubMed1992

Compartmental study of rat renal phospholipid metabolism.

Phospholipid content and metabolism were studied in rat renal papillary, medullary and cortical slices. The highest concentration of phospholipids was found in cortex and the lowest in papilla samples (ratio cortex/medulla, 1.3; cortex/papilla, 3.7). The profile of the various phospholipids was different depending on the zone. The most important difference was the relative concentrations of sphingomyelin (CerPCho) and phosphatidylinositol (PtdIns) with ratios for PtdIns/CerPCho of 5.0, 3.3 and 2.5 in papilla, medulla, and cortex, respectively. In the three zones, PtdIns showed the highest specific activity for [2-14C]glycerol and [1-14C]arachidonic acid incorporation. By contrast, a higher amount of [1-14C]palmitic acid was incorporated into phosphatidylcholine than into any other phospholipid. The various radioactive precursors were only poorly incorporated into phosphatidylethanolamine. No radioactivity was associated with phosphatidylserine. The papilla possesses the most active phospholipid metabolism of all the pathways studied.

Animals↗

PubMed1989

Increase of phosphatidylinositol arachidonic acid incorporation induced by mepacrine.

In view of the fact that mepacrine (Mp) is usually used as an inhibitor of the endogenous phospholipase A2, and since this enzyme produces the release of arachidonic acid (AA) from membrane phospholipids, we studied the effect of different concentrations of Mp on the mobilization of [1-14C]AA in rat renomedullary phospholipids. During the acylation period, 0.1 mM Mp did not produce any significant change in the incorporation of [1-14C]AA into phosphatidylcholine (PC) and phosphatidylethanolamine (PE), and only a slight increase in phosphatidylinositol (PI). Higher concentrations of Mp (0.5 to 1.0 mM) produced a decrease of radioactivity in PE and PC with an increase in PI. Using prelabeled slices, a dose-dependent decrease in the 14C-radioactivity in PE and PC was observed, with a parallel increase in PI. This effect of Mp persisted even in the presence of a physiological activator of phospholipase A2, bradykinin (BK). No change in the net amount of phospholipids was observed at any of the Mp concentrations used. The results of this study show that Mp, at concentrations generally used to inhibit phospholipase A2, produced a transfer of arachidonic acid from PE and PC to PI, rather than a blockade in the release of AA from membrane phospholipids.

Animals↗

PubMed1989

Bradykinin-increased phospholipid deacylation-reacylation in rat renal medulla is inhibited by dBc AMP.

The effect of bradykinin on the mobilization of arachidonic acid was analyzed separately by acylation and degradation. Acylating activity was determined by the incorporation of [14C]arachidonic acid into the phospholipids at different times. Different concentrations of bradykinin had no effect on the phospholipid acylating activities. The degradation of the phospholipids was performed on renal medullary slices prelabeled with [14C]arachidonic acid. Treatment with bradykinin produced an initial degradation of phosphatidylcholine, phosphatidylethanolamine and phosphatidylinositol, with a concomitant increase in lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylinositol within 5 min of incubation. Phosphatidylcholine-, phosphatidylethanolamine- and phosphatidylinositol increased thereafter and reached the control values after 10 min of incubation. After 30 min, incubation of prelabeled slices with bradykinin produced a significant concentration-dependent increase in the phospholipid-labeling by reutilization of [14C]arachidonic acid. The effect of bradykinin on the phospholipid-labeling was blocked by preincubation with increasing concentrations of dBc AMP. Mepacrine also blocked the bradykinin stimulation in phosphatidylcholine and phosphatidylethanolamine, but had no effect on bradykinin-induced changes in the phosphatidylinositol arachidonic acid moiety.

Acylation↗