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PubMed1991

Glycochenodeoxycholic acid inhibits calcium phosphate precipitation in vitro by preventing the transformation of amorphous calcium phosphate to calcium hydroxyapatite.

Calcium hydroxyapatite can be a significant component of black pigment gallstones. Diverse molecules that bind calcium phosphate inhibit hydroxyapatite precipitation. Because glycine-conjugated bile acids, but not their taurine counterparts, bind calcium phosphate, we studied whether glycochenodeoxycholic acid inhibits calcium hydroxyapatite formation. Glycochenodeoxycholic acid (2 mM) totally inhibited transformation of amorphous calcium phosphate microprecipitates to macroscopic crystalline calcium hydroxyapatite. This inhibition was not mediated by decreased Ca2+ activity. Taurocholic acid (2-12 mM) did not affect hydroxyapatite formation, but antagonized glycochenodeoxycholic acid. Both amorphous and crystalline precipitates contained a surface fraction relatively rich in phosphate. The surface phosphate content was diminish by increasing glycochenodeoxycholic acid concentrations, and this relationship was interpreted as competition between bile acid and HPO4(-4) for binding sites on the calcium phosphate surface. A phosphate-rich crystal surface was associated with rapid transition from amorphous to crystalline states. These results indicate that glycochenodeoxycholic acid prevents transformation of amorphous calcium phosphate to crystalline hydroxyapatite by competitively inhibiting the accumulation of phosphate on the crystal embryo surface.

Calcium↗
PubMedDate not supplied

Competition of pyridoxal 5'-phosphate with ribulose 1,5-bisphosphate and effector sugar phosphates at the reaction centers of the spinach ribulose 1,5-bisphosphate carboxylase/oxygenase.

The stimulation of the carboxylase reaction by effectors of ribulose 1,5-bisphosphate carboxylase/oxygenase displays higher sensitivity towards pyridoxal 5'-pyridoxal 5'-phosphate inhibition than the catalytical process itself. Pyridoxal 5'-phosphate binding to the enzyme is not affected by the modulators 6-phosphogluconate and fructose 1,6-bisphosphate at low concentrations at which these agents stimulate the carboxylation rate. At higher concentrations these sugar phosphates protect the enzyme against pyridoxal 5'-phosphate inhibition in a similar fashion like the substrate ribulose 1,5-bisphosphate. Such protection experiments in combination with spectrophotometrical studies of pyridoxal 5'-phosphate binding demonstrate two binding states of ribulose 1,5-bisphosphate at the reaction centers of the enzyme with different requirements for Mg2+. 6-Phosphogluconate functions as protector only in the presence of Mg2+. Our results imply a competition between pyridoxal 5'-phosphate and substrate or effector sugar phosphates at the reaction centers of the spinach carboxylase. It is proposed that the pyridoxal 5'-phosphate inhibition of the stimulatory activity of these effectors originates from a modification of the regulatory sites of the enzyme caused by pyridoxal 5'-phosphate binding to the catalytical sites.

Binding Sites↗
PubMedDate not supplied

Relationship of phosphate administration to serum and red cell phosphate concentration, erythrocyte 2,3-diphosphoglycerate (2,3-DPG) and blood P50 in the hyperglycemic dog.

In vitro studies indicate that acute increases in intracellular phosphate concentration decrease red blood cell 2,3-diphosphoglycerate levels (G. Momsen, B. Vestergaard-Bogind, Arch Biochem Biophys 190:67, 1978). We have examined the relationship in vivo of serum phosphate concentration, red cell phosphate, 2,3-DPG and blood P50 in hyperglycemic dogs infused alternately with phosphate or chloride (control) solutions. During the 8-hr insulin infusion, serum phosphate (Pi) fell 40% in the chloride-treated animals and rose 71% in the phosphate-treated dogs (P less than 0.001, phosphate vs. control). RBC Pi concentration declined in the controls and rose significantly in the phosphate-infused dogs (P less than 0.02). Serum Pi and RBC Pi were correlated in the phosphate-managed animals (r = 0.76, P less than 0.02), but not in the controls. RBC 2,3-DPG failed to rise in either group during insulin infusion and regression analysis showed a negative correlation between serum Pi and 2,3-DPG (r = -0.90, P less than 0.005) and between RBC Pi concentration and 2,3-DPG (r = -0.84, P less than 0.02). P50 failed to change in either group during insulin treatment and for up to 24 hr after initiation of the 8-hr infusion of insulin.

2,3-Diphosphoglycerate↗
PubMed1983

Restoration of phosphaturia in phosphate-deprived rats in the presence of both parathyroid hormone and phosphate infusion.

The present study tested the hypothesis that the combination of parathyroid hormone and phosphate infusion would be phosphaturic in phosphate-deprived rats. Clearance experiments were performed in Sprague-Dawley rats fed a low-phosphate diet for 4 days. The animals were first given a phosphate infusion and then administered parathyroid hormone. The reverse experiment was also performed in a second group of rats by giving the hormone first followed by a phosphate infusion. There was no increase in phosphate excretion in response to phosphate infusion or parathyroid hormone given alone. However, the combination of parathyroid hormone and phosphate infusions, given in either order, was phosphaturic in phosphate-deprived rats.

Animals↗
PubMed1991

[Exploration of the parathyroid gland function by intake or oral calcium and phosphate (only oral intake and sequential treatment with calcium-phosphate)].

The parathyroid hormone response to the oral intake of either calcium or phosphate was explored in 10 young adults (23-28 years). First, the subjects were investigated during free running diet. They ingested a single oral dose of 500 mg of calcium (as a bag of Sandocal) and 10 days later a single oral dose of phosphate (750 mg of phosphorus as a tablet of Phosphore Sandoz Forte). Samples of blood and urine were collected before and during the 4 hours following the ingestion of either calcium or phosphate. After intake of calcium an acute response was obtained with a 58% decrease in PTH 1-84 at 1 hr (p less than 0.001) and a 33% decrease in nephrogenous cAMP (p less than 0.001). After ingestion of phosphate the response was delayed and less constant with a 25% increase in PTH 1-84 at 3 hr (p less than 0.01) and a 27% increase in nephrogenous cAMP (p less than 0.001). Then, the effects of a calcium therapy (3 daily doses of 500 mg each for 20 days) and of a subsequent phosphate therapy (2 daily doses of 750 mg each for 10 days) on the parathyroid hormone response to the administration of a single dose of phosphate were studied. On days 10, 21 and 31 baseline blood and urine samples were obtained prior to calcium and phosphate administration for measuring PTH 1-84 and nephrogenous cAMP. No significant variation was found. On days 21 (after calcium therapy) and 31 (after phosphate therapy) an oral load of phosphate was administered according to the procedure described above.(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Oral↗
PubMed1984

Phosphate intestinal secretion and absorption by isolated ileal loop: effects of cholecalciferol and diet phosphate.

The effect of diet phosphate content and cholecalciferol on intestinal phosphate secretion and absorption was investigated in rachitic chicks. Phosphate absorption was determined by the in situ ligated loop technique. Phosphate secretion was estimated by a method proposed by the authors. Hydroxyapatite, placed in the lumen of a ligated loop, acts as trapping agent of 32P leaving the intestinal tissue. The fraction of rapid exchangeability of tissue phosphate was taken as the precursor pool of secreted phosphate. Control chicks fed diets containing 0.3% P (group 1) or 1.0% (group 2) showed similar Pi absorption; the secretion was larger for group 2. After cholecalciferol treatment for 2 or 4 consecutive days an increment of Pi absorption with simultaneous reduction of Pi secretion was evident for both groups of animals. Chicks treated for 7 days gave values similar to those of controls. It is concluded that the regulation of intestinal phosphate absorption and secretion could be one important mean of homeostatic control. Intestinal phosphate movement is adapted to dietary phosphate and is partially independent of cholecalciferol.

Animals↗
PubMed2006

Role of the sodium-dependent phosphate co-transporters and of the phosphate complexes of uranyl in the cytotoxicity of uranium in LLC-PK1 cells.

Although uranium is a well-characterized nephrotoxic agent, very little is known at the cellular and molecular level about the mechanisms underlying the uptake and toxicity of this element in proximal tubule cells. The aim of this study was thus to characterize the species of uranium that are responsible for its cytotoxicity and define the mechanism which is involved in the uptake of the cytotoxic fraction of uranium using two cell lines derived from kidney proximal (LLC-PK(1)) and distal (MDCK) tubule as in vitro models. Treatment of LLC-PK(1) cells with colchicine, cytochalasin D, concanavalin A and PMA increased the sodium-dependent phosphate co-transport and the cytotoxicity of uranium. On the contrary, replacement of the extra-cellular sodium with N-methyl-D-glucamine highly reduced the transport of phosphate and the cytotoxic effect of uranium. Uranium cytotoxicity was also dependent upon the extra-cellular concentration of phosphate and decreased in a concentration-dependent manner by 0.1-10 mM phosphonoformic acid, a competitive inhibitor of phosphate uptake. Consistent with these observations, over-expression of the rat proximal tubule sodium-dependent phosphate co-transporter NaPi-IIa in stably transfected MDCK cells significantly increased the cytotoxicity of uranium, and computer modeling of uranium speciation showed that uranium cytotoxicity was directly dependent on the presence of the phosphate complexes of uranyl UO(2)(PO(4))(-) and UO(2)(HPO(4))(aq). Taken together, these data suggest that the cytotoxic fraction of uranium is a phosphate complex of uranyl whose uptake is mediated by a sodium-dependent phosphate co-transporter system.

Animals↗