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PubMed2003

Intraoperative testing for parathyroid hormone: a comprehensive review of the use of the assay and the relevant literature.

OBJECTIVE: The rapid intraoperative parathyroid hormone assay is transforming the parathyroidectomy procedure. We present a review of the literature on the use of the assay as an adjunct to surgery. To our knowledge, this is the first review of the literature to encompass and compare all known primary studies of this assay in parathyroidectomy patients. DATA SOURCES: Articles were collected by searching MEDLINE databases using relevant terminology. The references of these articles were reviewed for additional studies. Supplementary articles pertinent to the parathyroidectomy procedure, preoperative parathyroid localization studies, and intraoperative parathyroid hormone assay development also were examined. STUDY SELECTION AND DATA EXTRACTION: One hundred sixty-five references were analyzed and categorized separately into groups. DATA SYNTHESIS: The primary studies of intraoperative data on patients undergoing parathyroidectomy were compared when possible. Studies were analyzed by type of assay used, where performed, turnaround time, and efficiency of use. Reviews of the types of parathyroid surgery and preoperative localization were included for educational purposes.Conclusions.-The intraoperative parathyroid hormone assay is a useful adjunct to preoperative imaging and parathyroid surgery because of its unique ability to detect an occult residuum of hyperfunctioning parathyroid tissue. Use of this assay will obviate the need for frozen section in most routine cases. The test facilitates minimally invasive parathyroidectomy for single parathyroid adenomas, which, in turn, improves cost-effectiveness and cosmetic outcome. Its use in patients with known preoperative multiglandular disease is promising but requires further study.

Humans↗
PubMedDate not supplied

Uremic vagal neuropathy: has parathyroid hormone a pathogenetic role?

Cardiac vagal reflexes were investigated in 19 dialysis patients, with the aim of verifying whether parathyroid hormone, proposed as an important uremic neurotoxin, plays a role in the development of uremic vagal neuropathy. The results indicate that parasympathetic control of heart function is frequently impaired in uremics. Plasma parathyroid hormone levels were significantly correlated with the time on dialysis. However, a correlation between autonomic disturbances and plasma parathyroid hormone concentrations was not found in this study.

Adult↗
PubMed2001

Parathyroid hormone (PTH) suppresses rat PTH/PTH-related protein receptor gene promoter.

Parathyroid hormone (PTH) regulates osteoblasts via a G protein-linked PTH/PTH-related protein (PTHrP) receptor. PTH effects on PTH/PTHrP receptor gene expression were studied in UMR 106 osteoblast-like cells. In heterogeneous nuclear RNA and Northern analysis, PTH suppressed PTH/PTHrP receptor transcription. We cloned the 7-kb promoter region of the rat PTH/PTHrP receptor gene and transiently transfected chimeric deletion constructs containing the 5'-flanking region and the luciferase gene into UMR 106 cells. In transfected cells the minimal region for basal promoter activity was between positions -128 and +103. The 5'-flanking region of exon U1 contained several putative-binding sites for Sp1 and the myc-associated zinc finger protein (MAZ). The minimal PTH-suppressive region (PTHSR) was between +1 and +25 in exon U1, but the 5'-flanking region or Sp1 and MAZ-binding sites also were required for PTH-mediated repression. By gel mobility shift assay PTH markedly decreased binding of PTHSR-protein complex in UMR 106 cells. The mutation experiments showed that the most critical sequence for the repression of PTH was 5'-GGGGGAGGGGAG-3' (+1 to +12) of PTHSR. This represents the first characterization of a PTH-suppressive region of the PTH/PTHrP receptor gene in rat.

Animals↗
PubMed1969

Metabolism of parathyroid hormone. Degradation of 125I-labelled hormone by a kidney enzyme.

A study was made of the enzymic degradation of (125)I-labelled parathyroid hormone by rat kidney microsomes. Incubation with microsomes resulted in rapid destruction of the labelled hormone. The microsomal factor was not separable by dialysis, and the reaction was favoured by pH values in the physiological range. Velocity of the reaction varied directly as the substrate concentration, and additional crude parathyroid hormone (trichloroacetic acid-precipitated, 3.68mg./ml.) inhibited destruction of labelled hormone. There was much less inhibition with added trichloroacetic acid-precipitated calcitonin (3.92mg./ml.) and virtually none with added pig insulin (3.80mg./ml.). Gel filtration of control medium on P6 (Bio-Gel) yielded one radioactive peak at the void volume. After incubation with microsomes three further peaks were obtained on gel filtration. Only the void-volume peak contained intact (125)I-labelled parathyroid hormone, indicating that the microsomal enzyme degraded labelled hormone to a number of smaller fragments.

Animals↗
PubMed1991

Parathyroid hormone-(1-34) peptide activates cyclic adenosine 3',5'-monophosphate in the human placenta.

Dually perfused human term placental lobules were exposed to forskolin, bovine parathyroid hormone (bPTH(1-34)) and human parathyroid hormone related-peptides, hPTHrP(1-34), hPTHrP(67-86)NH2 or PTHrP(107-138) for 15 min in the presence of 3-iso-butyl-1-methyl-xanthine (IBMX); control lobules were exposed to IBMX alone. Homogenates of these tissues were then assayed for cyclic adenosine 3',5'-monophosphate (cyclic AMP) and results normalized per mg of protein. Exposure to forskolin or bPTH(1-34) on both sides, and exposure to bPTH(1-34) at a concentration of 30 nM on the maternal side of the placenta or 120 nM on the fetal side of the placenta, significantly enhanced tissue cyclic AMP production compared with tissue exposed to IBMX alone. Exposure to hPTHrP(1-34), hPTHrP(67-86)NH2 and hPTHrP(107-138) at a concentration of 30 nM on both sides of the placenta had no significant effect upon tissue cyclic AMP production.

Cyclic AMP↗
PubMed1979

Inhibition of adenosine 3',5'-monophosphate accumulation and parathyroid hormone release by sodium nitroprusside.

Sodium nitroprusside effected a significant reduction in intracellular cAMP accumulation and parathyroid hormone release in dispersed bovine parathyroid cells. The inhibition was apparent at 3 x 10-4 M and maximal at 10-2 M nitroprusside. The effect was rapid and reversible and could be demonstrated in both the presence and absence of stimulating agonists [i.e. (-)isoproterenol, dopamine, and cholera toxin]. The inhibition was additive with that previously described for alpha-adrenergic agonists and prostaglandin F2 alpha and was not affected by phentolamine, suggesting that nitroprusside does not act through the inhibitory receptors previously described in this system. The nitroprusside effect on cAMP accumulation and parathyroid hormone release was present at virtually all concentrations of extracellular calcium tested; 2mM EGTA failed to prevent the inhibition. While extracellular calcium may play some role in this inhibition, it is not required for demonstration of the effect.

Animals↗
PubMed2006

Osteoporosis-treating parathyroid hormone peptides: What are they? What do they do? How might they do it?

The first experiments demonstrating parathyroid hormone's (PTH's) dramatic bone-building activity in rat pups, using a bovine parathyroid extract called parathormone were reported 74 years ago. Over the next decades, the native parathyroid hormone (human (h)PTH(1-84)) was purified and two of its fragments (hPTH(1-34) and (Leu27)cycloGlu22-Lys26hPTH(1-31)NH2) have been developed for the treatment of osteoporosis. One of these, recombinant (r)hPTH(1-34), is now on the market under the trade name of Forteo. The native hormone has also completed clinical trials and (Leu27)cycloGlu22-Lys26hPTH(1-31)NH2 is in phase II clinical trials under the trade name Ostabolin-C. All three of these peptides potently stimulate bone growth, reinforce bone microstructure weakened by estrogen deprivation and reduce further fracturing. Furthermore, future studies may demonstrate that these peptides also promote the repair of existing fractures and implant anchorage in both healthy and osteoporotic humans. PTHs have the potential to become more successful by using cost-cutting, but still effective, cyclical treatment regimens and by formulating them for non-injectable delivery. This review will discuss the identification of PTH peptides, how they function and their future role in the treatment of osteoporosis.

Animals↗
PubMed1988

Effect of estrogens on renal responsiveness to parathyroid hormone in elderly female subjects.

The effect of estrogens on the renal responsiveness to parathyroid hormone (PTH) was examined by PTH loading tests with synthetic human-PTH (1-34) in 8 normal elderly females (mean +/- SD age, 81.0 +/- 7.1 yr) before and after administration of estrogen (Premarin 1.25 mg/day for 4 weeks). Basal urinary adenosine cyclic 3', 5'-monophosphate (cAMP) excretion showed a tendency to increase after estrogen administration (5.47 +/- 1.68 vs 6.60 +/- 2.67 nmol/100 ml GFR) and the theoretical renal phosphorous threshold showed a tendency to decrease from 3.22 +/- 0.98 to 2.73 +/- 0.56 mg/dl. The blood ionized calcium concentration did not change after estrogen administration (4.44 +/- 0.16 vs 4.32 +/- 0.20 mg/dl) and serum phosphorous (P) decreased significantly (3.65 +/- 0.47 vs 3.01 +/- 0.42 mg/dl, p less than 0.05). There was no increase in mean serum immunoreactive PTH (0.34 +/- 0.10 vs 0.34 +/- 0.05 ngeq/ml). The urinary excretions of cAMP in response to PTH loading [100 U of human-PTH (1-34), intravenously] significantly (p less than 0.05) increased (94.8 +/- 57.0 vs 196.7 +/- 118.3 nmol/100 ml GFR/h) after estrogen administration. Moreover the changes in urinary excretion of cAMP (r = 0.698, p less than 0.01) and P (r = 0.555, p less than 0.05) induced by the PTH loading were positively correlated with serum estradiol in elderly females, assessed as groups before and after estrogen administration. These results suggest that estrogens may enhance the renal responsiveness to exogenous PTH administration.

Adult↗
PubMed1982

In vitro studies of parathyroid hormone release: effect of cimetidine.

We studied parathyroid hormone (PTH) release from cell suspensions of fresh and cryopreserved human parathyroid tissue. A sensitive PTH assay with midregion specificity and adaptation of "micro" methods of cell plating permitted conservation of tissue (200 microliters aliquots) and high reproducibility (5 to 10 aliquots per experimental condition). Viability of cells in suspension was confirmed by increased PTH release with increased incubation, increased incorporation of tritiated leucine with increased incubation, and incorporation of tritiated leucine following experimental incubation. Because of conflicting reports regarding the in vivo effect of cimetidine on PTH release, we incubated cells from both adenomatous and hyperplastic glands at 0, 10(-4)M, 10(-5)M, and 10(-6)M cimetidine (10(-5)M is therapeutic) and at 0.25, 1 to 1.2, and 2 mM Ca++. Despite occasional statistically significant (P = 0.05) differences in PTH release with and without cimetidine, therapeutic levels of cimetidine had no consistent effect on PTH release from pathologic parathyroid tissue in vitro.

Calcium↗
PubMed1979

Analysis of parathyroid hormone and its fragments in rat tissues: chemical identification and microscopical localization.

After intravenous injection of [(125)I]-iodo-parathyroid hormone in the rat, uptake of the hormone was greatest in the liver and kidneys. Uptake was rapid, reaching a maximal concentration by 4 and 8 min, respectively. Extracts, prepared from both these organs at intervals soon after the injection of intact hormone, showed three main radioactive peaks when samples were subjected to gel filtration under protein-denaturing conditions. The first peak coeluted with intact hormone. The second eluted at a position corresponding to the carboxy-terminal fragments previously described in plasma, and the last eluted at the salt volume of the column. Microsequence analysis of the radioiodinated fragments, a method that has proved valuable for chemically defining the circulating fragments resulting from metabolism of injected hormone, showed that extracts of liver and kidney, prepared at 4 and 8 min after injection of the intact hormone, contained different fragments. The radioiodinated fragments in liver extracts were identical to those previously reported in the plasma of rats and dogs, fragments resulting principally from proteolysis between positions 33 and 34, and 36 and 37 of the intact hormone. Although the same fragments were also present in the kidneys, they constituted less than 15% of the amount present in the liver. More than 50% of the labeled renal fragments consisted of a peptide whose amino-terminal amino acid was position 39 of the intact hormone, a fragment not present in plasma. The rate of appearance of radioiodinated fragments that were chemically identical to those in plasma was more rapid in the liver than in plasma. Correlation of these chemical analyses with studies of the localization of (125)I by autoradiography showed that at the times when the intact hormone and the carboxy-terminal fragments comprised nearly all of the (125)I-labeled moieties in the tissues, the proximal convoluted tubules of the kidney and sinusoidal lining cells of the liver, which probably are Kupffer cells, contained the highest concentration of (125)I. Preferential localization of immunoreactive parathyroid hormone to these tissue sites also was shown by immunoperoxidase staining in studies with unlabeled hormone. Our results suggest that, unless multiple renal mechanisms are present for release of hormonal fragments, one of which releases the circulating fragments preferentially, the liver, rather than the kidney, is principally responsible for generating the carboxy-terminal fragments in plasma after injection of intact hormone, and the Kupffer cells may contain the enzymes that hydrolyze parathyroid hormone.

Animals↗
PubMed1990

Parathyroid hormone inhibits B cell proliferation: implications in chronic renal failure.

B cell proliferation is impaired in patients with chronic renal failure, but the mechanisms underlying this defect are not known. Lymphocytes have receptors for parathyroid hormone, and it is possible that the state of secondary hyperparathyroidism of renal failure is responsible for the B cell defect. Our studies were designed to (a) examine T cell-independent B cell proliferation [3H)thymidine incorporation) induced by Staphylococcus aureus Cowan 1 after 5 days of culture, (b) evaluate the effect of parathyroid hormone on S. aureus Cowan I-induced B cell proliferation, and (c) investigate the mechanisms through which parathyroid hormone may exert its effect on B cell proliferation. Lymphocytes were obtained from 37 normal subjects and 21 dialysis patients. S. aureus Cowan I induced significant stimulation (P less than 0.01) of the proliferation of B cells from both groups, but the effect was smaller on B cells from dialysis patients (10.0 x 10(3) +/- 1.4 x 10(3) cpm) than on those from normal subjects (21.8 x 10(3) +/- 2.0 x 10(3) cpm). Both the intact molecule of parathyroid hormone (1-84 PTH) and its amino-terminal fragment (1-34 PTH) caused significant inhibition of proliferation of B cells from normal subjects in a dose-dependent manner, with the effect being significantly greater (P less than 0.01) with an equimolar concentration of 1-84 PTH than that of 1-34 PTH. Inactivation of 1-84 PTH by oxidation abolished most of its inhibitory effect on B cell proliferation.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1999

[The study of parathyroid hormone in the serum of patient with hypopharyngeal cancer].

Measurements of parathyroid hormone concentrations were made in the serum of patients with vestibular larynx before treatment, after radiation treatment and after radiation treatment followed by surgery. Patients with laryngeal cancer were found to have impaired calcium metabolism, their serum parathyroid hormone concentrations were elevated. After radiotherapy, in a favorable clinical course, patients with cancer of the vestibular larynx stage II show normalization of the hormone levels, whereas the above combined treatment diminished the concentrations, but they still remain above normal.

Adult↗
PubMed1990

Desensitization of parathyroid hormone receptors on cultured bone cells.

Administration of excessive amounts of parathyroid hormone (PTH) in the treatment of osteoporosis can reverse the beneficial effects of a low-dose, intermittent regime. To investigate the direct actions and the possible cellular mechanisms of PTH in inducing desensitization of PTH receptors, we studied the effects of desensitization on rat osteoblastic UMR-106 cells. When the osteoblasts were preincubated with bPTH-(1-34), complete refractoriness to a subsequent challenge with the hormone developed within 1 h and at hormone concentrations as low as 5 nM. When osteoblasts thus desensitized were incubated in hormone-free medium, recovery of the cAMP responses began within 2 h and reached maximum after 16 h. Cycloheximide did not affect the process of desensitization. [Nle8,Nle18,Tyr34]bPTH-(3-34)amide significantly impaired the desensitization process by PTH-(1-34) but did not have stimulatory effect on cAMP responses. No significant heterologous desensitization was obvious after preincubation with isoprenaline (50 microM), prostaglandin E1 (50 microM), or prostaglandin E2 (50 microM) for 2 h. Binding experiments with [125I]PLP-(1-36)amide after desensitization revealed that there was an approximate twofold decrease in receptor affinities as analyzed by Scatchard analysis, showing that the decrease in affinity was prominent in the process of desensitization. When the cells were treated with monensin during desensitization, PTH challenge after desensitization produced significantly lower cyclic AMP responses. Recovery after desensitization occurred over a period of 16 h. Inclusion of monensin, but not cycloheximide, impaired the recovery. The results show that homologous desensitization of rat osteoblasts to PTH is brought about by the occupancy of receptors by PTH-(1-34) but not by cAMP generation itself.(ABSTRACT TRUNCATED AT 250 WORDS)

Cyclic AMP↗
PubMed1978

Pseudohypoparathyroidism and idiopathic hypoparathyroidism: relationship between serum calcium and parathyroid hormone levels and urinary cyclic adenosine-3',5'-monophosphate response to parathyroid extract.

Forty patients with hypocalcemia and/or Albright's hereditary osteodystrophy were studied. Based on the estimation of serum calcium and parathyroid hormone (PTH) levels as well as the urinary cAMP response to infusions with parathyroid extract, it was possible to classify all of the patients studied as cases with idiopathic hypoparathyroidism (n = 6, low PTH, normal cAMP response), pseudohypoparathyroidism (PHP) type I (n = 18, high PTH, low cAMP response) and type II (n = 2, high PTH, normal cAMP response), as well as pseudopseudohypoparathyroidism (n = 14, normal PTH, normal cAMP response). In three cases studied at the age of 12, 17, and 23 yr, the signs of Albright's hereditary osteodystrophy were not observed. PTH levels were unusually high for a given serum calcium concentration in some patients with PHP, the increased PTH levels were, however, normalized during iv calcium infusions. In two young children with PHP, a gradual increase of serum PTH levels occurred despite persistent normocalcemia over a period of 3 yr. This suggests that factors other than hypocalcemia or frequent small unobservable falls of the serum calcium concentration, such as a deficient formation of 1,25-dihydroxyvitamin D3, secretion of an abnormal PTH, or an abnormal metabolism of the hormone, may contribute to the secondary hyperparathyroidism in PHP.

Adolescent↗
PubMed1988

Properties of parathyroid hormone receptors on circulating bovine lymphocytes.

Binding of parathyroid hormone (PTH) to circulating bovine lymphocytes was studied using, as the radioligand, a synthetic sulfur-free analog of bovine PTH, [Nle8,Nle18,Tyr34]bPTH-(1-34)amide, which was labeled to high specific activity with 125I and was purified by reverse-phase high-performance liquid chromatography. Binding of PTH to lymphocytes satisfies several criteria indicative of a specific interaction between the hormone and its receptor. Specific binding is saturable at 3.3 fmoles of radioligand bound per 10(7) cells, occurs more rapidly at 37 degrees C than at lower temperatures, and reaches equilibrium within 2 hr at 15 degrees C. Inhibition of specific binding occurs with intact PTH, with biologically active PTH analog or fragment, and with synthetic PTH antagonists, but not with biologically inactive PTH fragments, or peptide hormones unrelated to PTH antagonists, but not with biologically inactive PTH fragments, or peptide hormones receptors on lymphocytes and those previously reported with receptors in canine renal membranes, and on rat osteosarcoma cells. The dissociation constant (Kd) is approximately 10(-9) M, as calculated from the association and dissociation rate constants. This correlates very closely both with the apparent Kd, as estimated from Scatchard analysis of radioligand saturation and competition studies, and with previously reported Kd of PTH receptors in canine renal membranes and on intact rat osteosarcoma and opossum kidney cells. In addition, the relative binding affinity of intact hormone and a synthetic PTH agonist to to receptors on lymphocytes correlates closely with the relative biologic potency of these peptides in stimulating adenylate cyclase in membranes from these cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenylyl Cyclases↗
PubMed2003

Interaction of the parathyroid hormone receptor with the 14-3-3 protein.

The receptor for parathyroid hormone (PTH) and PTH-related protein (PTHrP) regulates calcium homeostasis, bone remodeling and skeletal development. 14-3-3 proteins bind to signaling proteins and act as molecular scaffolds and regulators of subcellular localization. We show that the parathyroid hormone receptor (PTHR) interacts with 14-3-3 and the proteins colocalize within the cell. 14-3-3 interacts with the C-terminal tail of the receptor containing a consensus 14-3-3 binding motif, but additional binding sites are also used. Protein kinase-A treatment of the receptor and especially the C-terminal tail reduces 14-3-3 binding. The expressed C-terminal tail is primarily localized in the nucleus, supporting the function of a putative nuclear localization signal that could be involved in the previously described nuclear localization of PTHR. The observed interaction between PTHR and the 14-3-3 protein implies that 14-3-3 could contribute to regulation of PTHR signaling.

14-3-3 Proteins↗
PubMed1996

Parathyroid hormone resistance and B cell lymphopenia in propionic acidemia.

The mechanisms of hypocalcemia, recurrent infections and hypogammaglobulinemia associated with metabolic decompensation of propionic acidemia due to propionyl-CoA carboxylase deficiency have not been defined. A 7-week-old infant with this disorder presented with severe hypocalcemia and B cell lymphopenia during an episode of metabolic acidosis and hyperammonemia. Hypocalcemia (1.1 mmol l-1) was associated with elevated serum intact parathyroid hormone (122 ng l-1), hyperphosphatemia, hypophosphaturia and hypercalcuria, indicating parathyroid hormone resistance. B cell lymphopenia (20 cells microliters-1) was associated with transient neutropenia, anemia and subsequent hypogamma-globulinemia (IgG < 294 mg dl-1, IgM < 8 mg dl-1, IgA < 8 mg dl-1), while T cells were normal. Parathyroid hormone resistance and B cell lymphopenia resolved following treatment with hemodialysis, diet and carnitine. These complications may be due to interference with parathyroid hormone renal tubular action and B cell maturation/proliferation by accumulated organic acids.

Amino Acid Metabolism, Inborn Errors↗
PubMed1984

Elevated serum parathyroid hormone, calcitonin, and 1,25-dihydroxyvitamin D in lactating women nursing twins.

The roles of vitamin D, calcitonin, and parathyroid hormone in calcium metabolism during lactation may be more evident in women secreting very large amounts of milk for a number of months, as in mothers nursing twins. We report significant increases in serum concentrations of parathyroid hormone, calcitonin, and 1,25(OH)2 vitamin D in mothers nursing twins compared to mothers nursing single infants. Serum concentrations of calcium actually increased in both groups during lactation. Maternal intakes of calories, calcium, and phosphorus were significantly higher in mothers nursing twins. Thus, mothers nursing twins were able to compensate for higher calcium losses in breast milk by increased dietary intakes of calcium as well as increased serum concentrations of parathyroid hormone, calcitonin, and 1,25(OH)2 vitamin D.

Adult↗