A Colorimetric Method for the Diagnosis of Phaeochromocytoma

Burn, G. P.; Field, Ellis

doi:10.1136/bmj.2.5002.1152

Cited by 26 publications

(7 citation statements)

References 2 publications

(3 reference statements)

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“…The assays at that time had poor reliability and were subject to interference by some drugs. In particular, the spectrophotometric methods used for analysis in these studies [11, 12] are subject to interference from a variety of antihypertensive drugs.…”

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Urinary catecholamine excretion in tetanus

Thwaites¹,

Yen²,

Cordon³

et al. 2006

Anaesthesia

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Summary Imperfect understanding of the pathophysiology of tetanus has limited therapeutic advances. Autonomic disturbance is a major cause of mortality and is believed to be associated with catecholamine release, predominantly norepinephrine. We measured epinephrine and norepinephrine concentrations in 24‐h urine collections from tetanus and critically ill patients suffering from other severe diseases. In patients with severe tetanus, mean (SD) epinephrine was 164.18 (129.37) nmol.day−1 compared with 45.18 (37.74) nmol.day−1 in mild‐moderate disease (p = 0.008). In the severe group, mean (SD) norepinephrine was 411.64 (208.5), and 121.00 (81.81) nmol.day−1 in moderately ill patients (p < 0.001). Compared with critically ill control patients, median epinephrine was 331.77 in tetanus patients and 89.70 nmol.day−1 in controls (p < 0.001). Median norepinephrine concentration was 788.02 nmol.day−1 in tetanus and 300.05 nmol.day−1 in control patients, p = 0.006. The study finds a novel result of increased epinephrine excretion in tetanus and confirms that catecholamine excretion in tetanus exceeds that in other critically ill patients. These results should be considered in designing more effective therapeutic strategies.

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confidence: 99%

Urinary catecholamine excretion in tetanus

Thwaites¹,

Yen²,

Cordon³

et al. 2006

Anaesthesia

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“…Aliquots (200 ,ul) of the cell lysate or media were incubated with 200 mM Tris acetate, pH 6.0/1 mM FeSO4/100,M tyrosine (New England Nuclear)/1 mM 6,7-dimethyl-5,6,7,8-tetrahydropterin/100 mM 2-mercaptoethanol at 37°C for 30 min (final vol, 500 ,ul). The reaction was stopped with 1 M perchloric acid and the 14C-labeled product was isolated by the aluminum hydroxide gel adsorption procedure (27).…”

mentioning

confidence: 99%

Restricted diffusion of tyrosine hydroxylase and phenylethanolamine N-methyltransferase from digitonin-permeabilized adrenal chromaffin cells.

Kelner¹,

Morita²,

Rossen³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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Tyrosine hydroxylase [TyrOHase; tyrosine 3-monooxygenase; L-tyrosie,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14. 16.2] and phenylethanolamine N-methyltransferase (PMTase; S-adenosyl-L-methionine:phenylethanolamine N-methyltransferase, EC 2.1. 1.28) are involved in catecholamine biosynthesis and are considered soluble proteins. However, they may actually be localized on the surface of the chromaffin granule. We have used the detergent digitonin to permeabilize the plasma membrane of cultured adrenal chromaffln cells to investigate the subcellular localization of TyrOHase and PMTase. A digitonin titration of the release of proteins and catecholamines revealed the existence of at least three subcellular compartments that are distinguished by their digitonin sensitivity: (i) soluble proteins, which were released upon treatment of the cells with low digitonin concentrations (S jM), (ii) a "digitonin-sensitive" cytoplasnic protein pool, which required higher concentrations of digitonin for release (10 ,uM) and included TyrOHase and PMTase, and (iii) the chromaffln granule, which was insensitive to digitonin. Analysis of the rates of release of all of these proteins revealed that the rate of TyrOHase and PMTase release was slower at 10 IAM than at 40 jaM digitonin, while the rates of release of the other proteins were similar at both concentrations and varied in proportion to their respective sizes. Treatment with cytoskeletal disrupting agents had no effect on TyrOHase or PMTase eftlux. These data suggest that TyrOHase and PMTase are in a detergent-labile association in the cell. This is consistent with the concept that TyrOHase and PMTase may be localized on the surface of the chromffin granule.In epinephrine-forming cells of the adrenal medulla, the catecholamine biosynthetic pathway is composed of four enzymes, tyrosine hydroxylase [TyrOHase; tyrosine 3-monooxygenase; L-tyrosine,tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2], aromatic amino acid decarboxylase (aromatic L-amino acid carboxy-lyase, EC 4.1.1.28), dopamine ,B-hydroxylase [dopamine l3-monooxygenase; 3,4-dihydroxyphenethylamine, ascorbate:oxygen oxidoreductase (P-hydroxylating), EC 1.14.17.1] and phenylethanolamine N-methyltransferase (PMTase; Sadenosyl-L-methionine:phenylethanolamine N-methyltransferase, EC 2.1.1.28). Dopamine o-hydroxylase is localized in the interior of the chromaffin granule and on the internal face of the granule membrane (1), while TyrOHase, aromatic amino acid decarboxylase, and PMTase are generally considered to be "soluble" cytoplasmic enzymes and ate synthesized on free ribosomes (2-4). However, morphological and subcellular fractionation studies suggest the possible particulate localization of PMTase and TyrOHase, perhaps on the surface of the chromaffmi granule. By immunocytochemistry, both PMTase and TyrOHase have been seen to be associated with chromaffin granules (5-9), and one report shows TyrOHase to be localized on microtubules (8). In purification procedur...

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“…Catecholamines and acid catechols were adsorbed on aluminium hydroxide and normeta nephrine and vanillylmandelic acid were separated into the supernatant solution. This method of the selective adsorption of catechols depends on the principle reported by Burn (31). Normetanephrine in the supernatant solution was separated by the method of Carlsson (32).…”

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Function and Metabolism of Catecholamines in the Brain

Matsuoka

1964

Japanese Journal of Pharmacology

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A Colorimetric Method for the Diagnosis of Phaeochromocytoma

Cited by 26 publications

References 2 publications

Urinary catecholamine excretion in tetanus

Urinary catecholamine excretion in tetanus

Restricted diffusion of tyrosine hydroxylase and phenylethanolamine N-methyltransferase from digitonin-permeabilized adrenal chromaffin cells.

Function and Metabolism of Catecholamines in the Brain

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