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PubMed1993

Effect of hypermagnesemia on the adenohypophyseal-gonadal function, parathyroid hormone secretion and some other hormonal indicators.

Hormonal secretory mechanisms are influenced positively or negatively by magnesium, the effect depending on its concentration. The submitted study is concerned with the effect of acute hypermagnesemia induced by intravenous infusion of 6 g MgSO4 on quiescent and LHRH-induced secretion of FSH, LH, prolactin and testosterone; on the levels of intact parathyroid hormone; and on other hormonal and mineral indicators in 10 healthy male subjects. Gonadotropin secretion was not altered by hypermagnesemia. Quiescent testosterone levels decreased moderately (p < 0.01), and the secretory kinetics of the hormone slightly changed. Parathyroid hormone levels markedly dropped in the 60th minute of hypermagnesemia duration (p < 0.01), the drop depending on the initial values of the hormone prior to the administration of magnesium (r = 0.923, p < 0.01). Although in hypermagnesemia no correlations between the levels of parathyroid hormone and those of magnesium, calcium and phosphorus could be found, in normomagnesemia significant correlations were confirmed between the levels of parathyroid hormone and magnesemia (r = -0.8068, p < 0.05), and the levels of parathyroid hormone and calcemia (r = -0.9451, p < 0.01). In hypermagnesemia there were no alterations in the levels of the plasma prolactin, cortisol or catecholamines, nor was there any alteration in the rate at which catecholamines were excreted in urine. In conclusion, magnesium in supraphysiologic concentrations does not significantly change the function of the adenohypophyseal-gonadal axis or other hormonal indicators studied. The slight decline of quiescent testosterone levels does not seem to have any clinical significance, although this must be verified by further studies.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1981

Metabolism of parathyroid hormone by isolated rat Kupffer cells and hepatocytes.

Data from several laboratories indicate that hepatic mechanisms may have a distinctive role in the metabolism of intact hormone after secretion, a process that accounts, at least partly, for the heterogeneity of circulating parathyroid hormone. Accordingly, we studied the proteolysis of intact hormone by isolated rat Kupffer cells and hepatocytes. Kupffer cells (10(6) cells/ml) and hepatocytes (10(7) cells/ml) were incubated with unlabeled and (125)I-labeled bovine parathyroid hormone at 37 degrees C for periods ranging up to 2 h. When incubated with Kupffer cells, intact hormone disappeared with a t((1/2)) of 12+/-4 min. Radio-immunoassays using sequence-specific antisera showed that the dominant hormonal fragments recovered in the medium have an apparent molecular weight of approximately 6,000, lack amino-terminal antigenic determinants, and react in assays that specifically recognize determinants in the carboxy-terminal portion of the intact hormone. Amino-terminal fragments also were detected in high concentrations, particularly after short incubation periods. Radioiodinated fragments resulting from incubation of (125)I-labeled bovine parathyroid hormone with Kupffer cells had the same apparent size as fragments derived from the metabolism of unlabeled, intact hormone; when analyzed by Edman degradation, positions 34 and 37 of the intact hormone sequence were the amino-terminal amino acids of these dominant carboxy-terminal fragments. Hepatocytes did not hydrolyze the hormone. Thus, metabolism of parathyroid hormone by Kupffer cells results in the appearance of fragments in the media that are immunochemically indistinguishable from, and chemically identical with, those found in plasma when intact hormone is injected intravenously. This indicates that the proteolysis observed in vitro accurately reflects the metabolism of the hormone in vivo. The detection of amino-terminal fragments in concentrations nearly equal to those of carboxy-terminal fragments indicates that cleavage of intact hormone is, initially, by an endopeptidase(s). Kupffer cells may be a source from which specific protease(s) that hydrolyze parathyroid hormone can be characterized, particularly in terms of enzymic specificity and requirements for inhibition. Detailed analysis of the cellular and molecular events during incubation of parathyroid hormone with these cells may help to clarify the biologic significance of the peripheral metabolism of the hormone.

Animals↗
PubMed1988

Effects of fluoride on parathyroid hormone secretion and intracellular second messengers in bovine parathyroid cells.

Fluoride ion (F-) alone or in conjunction with aluminum (Al3+) has been shown to stimulate the activity of guanine nucleotide-binding proteins (G proteins) in cell membrane preparations from a variety of cell types and in intact hepatic cells. Several studies have indicated that G proteins are involved in the regulation of parathyroid hormone (PTH) secretion. Intracellular second messengers which modulate PTH secretion (e.g., cAMP) have also been found to be regulated by G proteins. We have, therefore, employed F- as a probe to investigate the possible role of G proteins in the modulation of PTH release and the intracellular second messengers that have been implicated in the control of PTH secretion. F- produces a dose-dependent inhibition of PTH release with a maximal inhibitory effect (67%) at 5 mM. F- exerts its inhibitory effect within 5 min and the degree of suppression of PTH secretion gradually increases over 1 hr. F- (5 mM) inhibits PTH secretion at 0.5 mM Ca2+ to the level observed with 2 mM Ca2+ alone; moreover, the effects of F- and high Ca2+ are not additive. While 1 mM F- suppresses PTH secretion by only 21%, and 10 microM Al3+ has virtually no effect at all, together they inhibit PTH release approximately to the level (63% inhibition) observed with 5 mM NaF alone. In the presence of 10(-5) M dopamine, F- produces a concentration-dependent inhibition of cAMP accumulation (0.684 +/- 0.033 pmoles/10(5) cells at 0 mM F- vs. 0.256 +/- 0.048 at 5 mM F-). However, the F- -induced decrease in cAMP cannot account for the inhibition of PTH release by this agent, since addition of methylisobutylxanthine (10(-4) M) by F- -treated cells raises intracellular cAMP content above that of control cells but fails to reverse the inhibition of PTH release. The cytosolic calcium concentration in Fura-2-loaded cells increases from 210 +/- 20 nM to 340 +/- 44 nM after 5 mM F- was added to incubation media. Prior removal of extracellular Ca2+ by EGTA totally blocks the F- -induced rise in cytosolic Ca2+ without preventing the inhibition of PTH release by NaF. F- also produces a time- and dose-dependent increase in the accumulation of IP, IP2, and IP3 in cells prelabeled with [3H]inositol and incubated with 10 mM Li+, consistent with activation of phospholipase C. We conclude that F- is a potent inhibitor of PTH secretion.(ABSTRACT TRUNCATED AT 400 WORDS)

1-Methyl-3-isobutylxanthine↗
PubMed1992

Parathyroid hormone and genetic hypertension.

Recent research provides evidence that parathyroid hormone is implicated in the pathogenesis of genetic hypertension. Abnormalities in calcium metabolism in genetic hypertension have been reported. These include hypercalciuria, depressed serum ionized calcium associated with enhanced serum parathyroid hormone levels. Calcium supplement resulted in normalization of calcium metabolism and reduction in blood pressure. In addition, removal of parathyroid glands attenuated the rise in blood pressure in genetic hypertensive rat. This review focuses on the links between calcium metabolism and calcium endocrine system abnormalities and the etiology of experimental genetic hypertension. The mechanisms by which dietary supplement and parathyroidectomy lower genetic hypertension are also discussed. Although the causality of raised parathyroid hormone in genetic hypertension is not yet fully understood, we conclude that this hormone may play a permissive effect in the development of hypertension.

Age Factors↗
PubMed1973

Heterogeneity of parathyroid hormone. Clinical and physiologic implications.

When immunoreactive human parathyroid hormone (hPTH), extracted by three different solvents (20% acetone in 1% acetic acid, 8 M urea, or normal saline) from parathyroid glandular tissue was subjected to Sephadex G-100 gel filtration and immunoassay using two different antisera (273 and C-329), four distinct fractions were observed. The first (I), a void volume peak, was detected by both antisera with similar immunoreactivity, as was a second (II), which had the elution and sedimentation properties of highly purified bovine parathyroid hormone (bPTH); a third (III) eluted between [(125)I]growth hormone and [(125)I]insulin, sedimented with the velocity of a molecule of approximately 6,000 mol wt, and was detected primarily by antiserum 273; a final fraction (IV), detected primarily by C-329, eluted just prior to [(125)I]insulin. The elution profiles of the acetone-acetic acid and 8 M urea extracts were similar and contained fraction II as their major component. In saline extracts, however, fraction III predominated. Three fractions, having gel filtration and immunologic characteristics similar to fractions II, III, and IV, respectively, of saline glandular extracts, were detected in the plasma of patients with both primary (adenomatous or carcinomatous) and secondary hyperparathyroidism. The predominant component in every plasma was the intermediate fraction that, like III, was detected primarily by antiserum 273, while the least abundant form was consistently the final fraction, detected primarily by antiserum C-329. The first fraction, like II, was detected with about equal potency by both antisera and had an elution volume on Sephadex corresponding to that of intact bPTH. It bore a reciprocal relationship to serum calcium and disappeared from the plasma of a uremic patient during calcium infusion or following parathyroidectomy with a half-time of no more than 20 min. This component therefore probably represents biologically active hormone. The intermediate and final fractions had turnover times in the plasma of a uremic patient more than 100 times greater than the active form, remained elevated even in the presence of post-parathyroidectomy hypoparathyroidism in this patient and were presumed to be biologically inactive. The ratio of biologically inactive fragments to the active form was greater in secondary hyperparathyroidism. The evidence presented favors a glandular origin for the fragments. Comparison of hormonal assays with the two antisera reveals a striking advantage in the preoperative diagnosis of primary hyperparathyroidism with antiserum 273 that is due to the enhanced sensitivity occasioned by its detection of a biologically inactive as well as the biologically active hormonal form.

Adenoma↗
PubMed1985

Functional mediastinal parathyroid cyst. Dynamics of parathyroid hormone secretion during cyst aspirations and surgery.

A patient presented with a large neck mass, hypercalcemia, and elevated serum parathyroid hormone levels. Aspiration of the cystic mass yielded 100 ml of fluid that contained a low concentration of thyroxine, but large amounts of parathyroid hormone, as measured by bioassay or with three different radioimmunoassays. After each of four aspirations, the serum calcium level declined significantly. Serial measurements showed that serum amino-terminal and mid-region parathyroid hormone levels and urinary cyclic adenosine monophosphate values declined after aspiration. Surgical resection of the cervical-mediastinal cyst restored normal serum calcium and parathyroid hormone levels, and these have been maintained for nine months. Calculations suggest that parathyroid hormone traversing the cyst lumen might contribute significantly to the excess circulating parathyroid hormone.

Aged↗
PubMed1980

Biosynthesis of parathyroid hormone.

Figure 11 summarizes our present concepts of the biosynthetic sequence for parathyroid hormone, deduced largely from observations in vitro. Many aspects of the presumed process whereby preproparathyroid hormone is converted via proparathyroid hormone to the hormone remain unclarified and require much further study, as is true for many other prehormones. These studies, however, coupled with (1) further investigations of intracellular degradation of parathyroid hormone, if this indeed operates in vivo; (2) the proteolytic conversion of secreted hormone in peripheral tissues; and (3) analysis of transcriptional control of biosynthesis of parathyroid hormone, using radioactive cDNA for hybridization studies of mRNA production and turnover, hold great promise for further understanding of critical regulatory factors central to expression of the actions of parathyroid hormone.

Adenylyl Cyclases↗
PubMed1995

Resetting of parathyroid hormone secretion after vitamin D3 treatment in hypoparathyroidism and after parathyroid adenectomy in primary hyperparathyroidism.

The relationship between parathyroid hormone (PTH) secretion and extracellular calcium (Ca) level is reciprocal causality. The equilibrium operating point determines basal PTH secretion rate and basal extracellular Ca level. We studied how this equilibrium was achieved in the subjects with decreased PTH secretion or decreased parathyroid glands number. Basal/maximum ratio of serum PTH, which reflects the basal secretory state of parathyroid glands, was increased in 9 hypoparathyroid patients treated with vitamin D3 (VD3) [7 patients with idiopathic hypoparathyroidism] and in seven of nine parathyroid adenectomized patients. There was a negative correlation between the ratio and basal serum Ca level in the patients with IHP after VD3 treatment (r = 0.7167, P < 0.05) and in the patients after parathyroid adenectomy (r = 0.7760, P < 0.05). The regression curves in these two groups coincided regardless of the difference in maximum PTH secretion rate, which suggested that the basal secretory state of parathyroid glands was determined by extracellular Ca level in a similar manner in these subjects. There was a sigmoidal relationship between basal/maximum ratio of serum PTH and basal serum Ca level, when the data were collected from 15 hypoparathyroid patients before or after VD3 treatment, 9 parathyroid adenectomized patients, and 10 normal subjects (r = 0.9057, P < 0.001). This sigmoidal curve is thought to represent the fundamental relationship between the basal secretory state of parathyroid glands and extracellular Ca level.

Adenoma↗
PubMed1997

Initiation of the phosphoinositide cycle by parathyroid hormone in synaptosomes.

We studied the effects of parathyroid hormone 10(-9) M) on the contents of mono-, di-, and triglycerides, total phospholipids, and free arachidonic acid in rat brain cortex synaptosomes using [1-(14)C]arachidonic acid at 2, 5, and 10 sec after addition of the hormone. Our data demonstrated the changes in lipid metabolism in synaptosomal membranes which were especially pronounced at 5 sec after addition of parathyroid hormone. Incorporation of 70% of [1-(14)C]arachidonic acid into the phosphoinositide fraction and the progress of changes in lipid metabolite composition suggest that the phosphoinositide cycle is initiated by parathyroid hormone, and the hormonal signal may be subsequently mediated in nerve cells by 1,2-diacylglycerol, a product of the phosphoinositide cycle.

Animals↗
PubMed1985

Organ distribution of aluminium in uremic rats: influence of parathyroid hormone and 1,25-dihydroxyvitamin D3.

Investigations were performed in order to see whether or not the application of parathyroid hormone or 1,25-dihydroxyvitamin D3, or both might influence the organ distribution of orally and parentally administered aluminium in control and uremic rats. The data show that 1,25-dihydroxyvitamin D3, affects the organ uptake in a different way than parathyroid hormone. Whereas parathyroid hormone increased the aluminium concentration in the liver, 1,25-dihydroxyvitamin D3 enhanced the aluminium uptake in the heart and the muscle, on the other hand, simultaneous application of 1,25-dihydroxyvitamin D3 and parathyroid hormone decreased the aluminium content of the bone, liver and brain.

Aluminum↗
PubMed1995

Identification and functional expression of a receptor selectively recognizing parathyroid hormone, the PTH2 receptor.

We have identified a G-protein-coupled receptor specifically activated by parathyroid hormone, which we refer to as the PTH2 receptor. Parathyroid hormone (PTH) and parathyroid hormone-related peptide (PTHrP, hypercalcemia of malignancy factor) activate a previously identified PTH/PTHrP receptor, which has a widespread tissue distribution. The PTH2 receptor is much more selective in ligand recognition and appears to have a more specific tissue distribution. It is activated by PTH and not by PTHrP and is particularly abundant in the brain and pancreas.

Amino Acid Sequence↗
PubMed1976

Hormonal control of bone collagen synthesis in vitro: effects of parathyroid hormone and calcitonin.

The effects of parathyroid hormone (PTH) on bone collagen synthesis were assessed in organ cultures of fetal rat calvaria by measuring the incorporation of [3H]proline into collagenase-digestible (CDP) and non-collagen protein (NCP) using purified bacterial collagenase. 1) PTH decreased the incorporation of labeled proline into CDP at concentrations similar to those which stimulate bone resorption in vitro. 2) This effect was observed in bones treated for 6 h, but not for 3 h; it was maximal at 24 h and was maintained for 96 h. Bones treated with PTH for 48 h and transferred to control media for 48 h showed recovery of CDP labeling to control values. 3) the effect was specific for bone collagen. There was little alteration in the incorporation of proline into NCP, and incorporation into collagen was not inhibited. 4) The effect could be ascribed to decreased collagen synthesis and not to changes in amino acid uptake, precursor pool size, or degradation of newly synthesized CDP. In 3 hour experiments, PTH did increase the labeling of CDP and NCP, but only at tracer concentration of proline in the medium, compatible with an early stimulation of amino acid uptake. 5) Similar inhibition was observed with purified bovine (1-84) PTH and synthetic bovine PTH (1-34) as well as with crude homologous PTH obtained from rat parathyroid gland culture fluid. Human (hCT) and salmon (sCT) calcitonin did not inhibit the effect of PTH on the labeling of CDP nor did they stimulate CDP labeling directly at concentrations which inhibited bone resorption. Dibutyryl cyclic-3',5'-adenosine monophosphate (D3cAMP) inhibited labeling of CDP at concentrations of .03 to .3 mM, thus mimicking the action of PTH. However, in this system DBcAMP inhibited 45Ca release, thus mimicking CT. We conclude that the direct effect of PTH on bone collagen synthesis is a slow reversible inhibition, not opposed by CT. This effect may be mediated by cAMP formation in bone cells.

Animals↗
PubMed1998

Activation of dihydropyridine sensitive Ca2+ channels in rat hippocampal neurons in culture by parathyroid hormone.

We examined the effects of parathyroid hormone (PTH) on rat hippocampal neurons in culture to determine whether it caused a similar intracellular calcium concentration ([Ca2+]i) increase in these cells to that seen with renal epithelial cells and found that PTH induced the effect in about 30% of the neurons. The effects appeared gradually during continuous administration of full-length PTH(1-84) or its active fragment, PTH(1-34), but not of an inactive fragment, PTH(39-84). However, the active fragment of the PTH-related peptide (PTHrP(1-34)) had little effect on [Ca2+]i during 60 min of administration. The PTH effect was inhibited by nifedipine, an L-type Ca2+ channel antagonist, and facilitated by S-(-)-BAY K 8644, an L-type Ca2+ channel agonist. Our findings suggest that PTH is one of the causal factors for the age-related increase in the density of voltage gated Ca2+ channels in hippocampal neurons.

3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethy↗
PubMed1991

On the role of polyamines in bone resorption induced by parathyroid hormone.

In order to elucidate the possible role of polyamines in the mobilization of mineral from long-term bone cultures stimulated with parathyroid hormone we have measured the activity of ornithine decarboxylase in osteoblasts, the levels of polyamines in calvarial bone and determined the effect of added polyamines and inhibitors of polyamine biosynthesis on calcium mobilization. Parathyroid hormone (10 nmol l-1) stimulated omithine decarboxylase activity by approximately 50% in both cultured bone cells of osteoblastic phenotype, UMR 106 and in mouse calvarial osteoblast-like cells. In mouse calvaria the levels of putrescine and spermidine were increased by parathyroid hormone after 24 hours. The levels of spermine were very low and were unchanged by parathyroid hormone. The two polyamine synthesis inhibitors alpha-difluoromethylornithine (DFMO; 2 mmol l-1) and methylglyoxal-bis-guanylhydrazone (MGBG; 50 mu mol l-1) did not significantly affect the mobilization of 45Ca from parathyroid hormone-stimulated bones. All three polyamines, putrescine, spermidine and spermine, inhibited the mobilization of 45Ca induced by parathyroid hormone in a dose-dependent manner. The inhibition induced by putrescine was reversible. In summary, we have shown that parathyroid hormone increases the accumulation of polyamines in bone, but the effect is small. Furthermore, inhibition of polyamine biosynthesis does not reduce parathyroid hormone-induced mineral mobilization and the addition of polyamines leads to a reduced rather than a stimulated mineral mobilization. Thus, polyamines do not seem to be critically involved in the changes in bone resorption induced by parathyroid hormone.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1986

Effects of parathyroid hormone on cytosolic calcium in renal proximal tubular primary cultures.

The effects of parathyroid hormone on the cytoplasmic Ca2+ concentration of canine renal proximal tubule cells grown in primary culture were determined using the fluorescent Ca2+ indicator quin 2. The cultured cells exhibited responses to hormones, enzyme activities, transport functions, and morphology characteristic of the proximal convoluted tubule. Parathyroid hormone stimulated an immediate rise in cytoplasmic Ca2+, both in suspended cells and cells studied as a monolayer on Nuclepore filters. The rise in cytoplasmic Ca2+ induced by the hormone was sustained for 15-30 min, was dose dependent, and was not mimicked by cyclic AMP. Removing Ca2+ from the extracellular media markedly decreased cytoplasmic Ca2+ and abolished the effects of parathyroid hormone on cytosolic Ca2+. 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate blocked the effects of the hormone on cytosolic Ca2+, but mitochondrial uncouplers failed to inhibit the effects of the hormone to increase cytoplasmic Ca2+. These studies support a role of Ca2+ in the activation of proximal renal tubule cells by parathyroid hormone.

Aminoquinolines↗
PubMed1996

Stimulation by parathyroid hormone of interleukin-6 and leukemia inhibitory factor expression in osteoblasts is an immediate-early gene response induced by cAMP signal transduction.

Parathyroid hormone and other agents that stimulate bone resorption function, at least in part, by inducing osteoblasts to secrete cytokines that stimulate osteoclast differentiation and activity. We previously demonstrated that parathyroid hormone induces expression by osteoblasts of interleukin-6 and leukemia inhibitory factor without affecting the 16 other cytokines that were examined. We also showed that stimulation of osteoclast activity by parathyroid hormone is dependent on activation of the cAMP signal transduction pathway and secretion of interleukin-6 by osteoblasts. In the current study, we demonstrate that the rapid and transient stimulation of interleukin-6 and leukemia inhibitory factor is inhibited by actinomycin D and superinduced by protein synthesis inhibitors, the classical characteristics of an immediate-early gene response. Moreover, activation of cAMP signal transduction by parathyroid hormone and parathyroid hormone-related protein is necessary and sufficient to induce both interleukin-6 and leukemia inhibitory factor. In addition, cAMP analogues as well as vasoactive intestinal peptide and isoproterenol, two neuropeptides that stimulate bone resorption by activating cAMP signal transduction in osteoblasts, also induce interleukin-6 and leukemia inhibitory factor in these cells. Taken together with our previous results, this study suggests that interleukin-6 is crucial for stimulation of bone resorption not only by parathyroid hormone, but also by parathyroid hormone-related protein, vasoactive intestinal peptide, and beta-adrenergic agonists, like isoproterenol.

Animals↗
PubMed1980

Hypotensive action of parathyroid hormone preparations on rats and dogs.

Bovine parathyroid extract and two commercial preparations containing the first 34 amino acids of synthetic bovine parathyroid hormone [bPTH-(1-34)]produced dose-related hypotension in anesthetized rats. Dogs were 10 times more sensitive to the two bPTH-(1-34) preparations than were rats. Propranolol, phentolamine, atropine, and promethazine did not affect the hypotensive action of bPTH-(1-34) in rats and dogs. bPTH-(1-34) decreased perfusion pressure in rat hindlimbs perfused in situ with Ringer's solution and was a vasodilator in dog kidneys perfused in vitro with Ringer's solution. Helical strips of rabbit aorta were also relaxed by bPTH-(1-34). We conclude that the direct vasodilatory action of bPTH preparations represents an intrinsic property of parathyroid hormone and that the hypotensive effect of this hormone is produced by part or all of the first NH2-terminal 34 amino acids.

Adrenergic alpha-Antagonists↗
PubMed1977

Adenylate cyclase of human fat cell ghosts. Stimulation of enzyme activity by parathyroid hormone.

Some of the effects of native bovine parathyroid hormone and of the synthetic aminoterminal 1-34 fragment on the adenylate cyclase activity of human fat cell ghosts were studied. Saturating concentrations of both hormone preparations caused a significant increase of enzyme activity by about 200-300%. Guanosine 5'-triphosphate (0.1 mM) inhibited basal enzyme activity but had no substantial effect on parathyroid hormone-stimulated enzyme activity. The guanosine 5'-triphosphate analogue, 5'-guanylyl-imidodiphosphate, produced about a threefold enhancement of basal and parathyroid hormone-stimulated enzyme activities under standard conditions (5 mM Mg+2, 1mM ATP, pH 8.0, 30 degrees C). Activation by parathyroid hormone was not influenced by beta-adrenergic blockade in contrast to stimulation by epinephrine. The sensitivity of the enzyme system to the native and the synthetic parathyroid hormone was, however, abolished after pretreatment of the fat cells with trypsin (1 mg/ml). The stimulatory effects of epinephrine and NaF were not affected by pretreatment with trypsin. The results suggest that human fat cells, like rat adipocytes, contain a multireceptor-coupled adenylate cyclase.

Adenylyl Cyclases↗