PubMed Health⌕ Search

PubMed · 9429326

Parathyroid function after successful renal transplantation.

Abstract

PURPOSE: The aim of this retrospective study was to assess parathyroid function after renal transplantation in patients with good renal function (creatinine < 133 mumol/l). METHODS AND MATERIALS: Of 1,628 patients on whom we performed renal transplantation, 210 have stable good renal function as defined above. Total calcium (Ca), creatinine, albumin and parathyroid hormone (PTH) values were obtained from patient records at varying intervals after transplantation, and in 91/210 patients pre-transplant values were available. Patients who had undergone parathyroidectomy before the transplant were excluded from the study. Follow-up ranged from 6 months to 24 years. RESULTS: These 210 patients were divided into 4 groups according to PTH and Ca levels. Group 1 consisted of 118 patients (56%) with normal Ca and PTH levels and group 2 of 69 patients (33%) with normal Ca but persistently high PTH levels, of whom 25 persistently have Ca levels in the high normal range. The reason for the inappropriate PTH levels is not obvious. In group 3 there were 18 patients (8%) with high Ca and PTH levels. They have disease requiring parathyroidectomy. Group 4 comprised 5 patients (3%) with low Ca and high PTH levels. In the 91 patients for whom pre-transplant PTH values were available, 16/46 patients with tertiary hyperparathyroidism (3 degrees HPT) have normalised after transplant, 12/46 patients have ongoing 3 degrees HPT post transplant, while 4/45 patients with less severe disease (secondary HPT) have developed 3 degrees HPT (P < 0.059). CONCLUSIONS: In 56% of patients with good renal function after transplant parathyroid function is normal. Thirty-three per cent have high PTH levels with normal Ca, but 36% of these are in the high normal range. Eight per cent have persistent 3 degrees HPT. Post-transplant parathyroid dysfunction correlates with the severity of pre-transplant disease.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J F Botha, J R Botha. 1997. Parathyroid function after successful renal transplantation.. https://pubmed.ncbi.nlm.nih.gov/9429326/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Stability and catalytic activity of alpha-amylase from barley malt at different pressure-temperature conditions.

The impact of high hydrostatic pressure and temperature on the stability and catalytic activity of alpha-amylase from barley malt has been investigated. Inactivation experiments with alpha-amylase in the presence and absence of calcium ions have been carried out under combined pressure-temperature treatments in the range of 0.1-800 MPa and 30-75 degrees C. A stabilizing effect of Ca(2+) ions on the enzyme was found at all pressure-temperature combinations investigated. Kinetic analysis showed deviations of simple first-order reactions which were attributed to the presence of isoenzyme fractions. Polynomial models were used to describe the pressure-temperature dependence of the inactivation rate constants. Derived from that, pressure-temperature isokinetic diagrams were constructed, indicating synergistic and antagonistic effects of pressure and temperature on the inactivation of alpha-amylase. Pressure up to 200 MPa significantly stabilized the enzyme against temperature-induced inactivation. On the other hand, pressure also hampers the catalytic activity of alpha-amylase and a progressive deceleration of the conversion rate was detected at all temperatures investigated. However, for the overall reaction of blocked p-nitrophenyl maltoheptaoside cleavage and simultaneous occurring enzyme inactivation in ACES buffer (0.1 M, pH 5.6, 3.8 mM CaCl(2)), a maximum of substrate cleavage was identified at 152 MPa and 64 degrees C, yielding approximately 25% higher substrate conversion after 30 min, as compared to the maximum at ambient pressure and 59 degrees C.

Calcium↗

A role for PLCgamma2 in platelet activation by homocysteine.

The aim of this study was to examine the homocysteine effect on phospholipase Cgamma2 (PLCgamma2) activation and to investigate the signaling pathway involved. We found that homocysteine stimulated the tyrosine phosphorylation and activation of platelet PLCgamma2. The tyrosine kinases p60src and p72syk appeared to be involved upstream. Reactive oxygen species were increased in homocysteine treated platelets. Likely oxidative stress could prime the non receptor-mediated tyrosine kinase p60src, inducing phosphorylation and activation of p72syk. The antioxidant N-acetyl-L-cysteine prevented the activation of these kinases. The phosphorylation and activation of PLCgamma2 were greatly reduced by the inhibition of p72syk through piceatannol. Moreover indomethacin diminished the homocysteine effect on p60src, p72syk and PLCgamma2, suggesting that thromboxane A(2) could be involved. In addition the treatment of platelets with homocysteine caused intracellular calcium rise and protein kinase C activation. Finally homocysteine induced platelet aggregation, that was partially reduced by indomethacin and by N-acetyl-L-cysteine of 35% or 50% respectively, while the PLCgamma2 specific inhibitor U73122 diminished platelet response to homocysteine of 70%. Altogether the data indicate that PLCgamma2 plays an important role in platelet activation by homocysteine and that the stimulation of this pathway requires signals through oxygen free radicals and thromboxane A(2).

Calcium↗

Prothrombotic effect of prostasomes of metastatic cell and seminal origin.

BACKGROUND: Prostasomes are secretory granules produced by the glandular epithelial cells of the prostate. Seminal prostasomes contain high amounts of Tissue Factor (TF) but no studies of TF on malignant cell prostasomes have been made. Here we compare the expression, phosphorylation, and function of TF on prostasomes of different origin. METHODS: TF was detected on prostasomes isolated from seminal fluid and human prostate cancer cell lines (PC-3, DU145, and LNCaP) using FACS and enzyme immunoassay (EIA). Incubation of prostasomes with radioactive ATP under conditions favoring protein kinase A activity led to phosphorylation of TF as detected by immunoprecipitation and SDS-PAGE. The prothrombotic effect of prostasomes was investigated in whole blood and recalcified plasma. Blocking experiments were performed using anti-TF antibodies and corn trypsin inhibitor. RESULTS: TF was expressed on all tested prostasome preparations with lowest values found for seminal ones. Prostasomal TF was the main endogenous substrate for prostasomal protein kinase A. All tested prostasome preparations greatly enhanced the rate of clot formation in a dose-dependent fashion, that is, the clotting capability of prostasomes seemed to be related to the extent of their expression of TF. In addition, the density of the clot varied between different prostasome preparations. When incubated in whole blood, prostasomes were found to associate to WBC thereby inducing them to express and release TF. CONCLUSIONS: These data show that TF is overexpressed and also subjected to phosphorylation by malignant cell prostasomes. This suggests major roles for prostasomes in thrombotic events that occur in some advanced cases of prostate cancer.

Calcium↗