Pheochromocytoma

Warren, Shields; Chute, Rosanna N.

doi:10.1002/1097-0142(197202)29:2<327::aid-cncr2820290210>3.0.co;2-3

Cited by 95 publications

(35 citation statements)

References 4 publications

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“…The most definitive work on the purification of tyrosine 3-monooxygenase appears to be a recent report by Markey et al [3]. The purified the enzyme about 83-fold to a specific activity of 373 nmol min-' mg-' with a 9 % yield from PC-12 clonal cell lines, which were derived from a transplantable rat adrenal medullary pheochromocytoma [21,22].…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the activated state induced by purification was similar to that induced by phosphorylation through the action of CAMP-dependent protein kinase in their pH profiles for the enzyme activity and affinities for a pterin cofactor but was dissimilar in their V values, suggesting that both the activated states might result from distinct conformational alterations of the enzyme. The activation of the enzyme by the addition of polyanions [19], anionic phospholipids [20] and salts [21] was observed with partially purified enzymes from rat brains or bovine brains. In each case the stimulation appeared to be largely due to a decrease in the K , of the enzyme for its pterin cafactor.…”

Section: Discussionmentioning

confidence: 99%

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Purification and Some Properties of Tyrosine 3‐Monooxygenase from Rat Adrenal

Okuno

Fujisawa

1982

European Journal of Biochemistry

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Tyrosine 3-monooxygenase was purified to homogeneity, as judged by sodium dodecyl sulfate/polyacrylamide gel electrophoresis, from rat adrenal. The specific activity of the final preparation was approximately 1600 nmol min-' mg protein-', which was much higher than the highest yet reported. The enzyme was markedly stabilized in the presence of glycerol, Tween 80 and EDTA. As judged by gel filtration on Ultrogel AcA 34, sodium dodecyl sulfate/polyacrylamide gel electrophoresis and cross-linking studies, the enzyme appeared to be composed of four identical subunits, each possessing a molecular weight of 59000. The isoelectric point of the enzyme was estimated to be 6.7 in the presence of 8 M urea and 6.6 in its absence. Amino acid analysis of the enzyme revealed a fairly high content of serine residues in this protein.Purification of the enzyme caused changes in the kinetic properties of the enzyme. The K,,, for 2-amino-4-hydroxy-6-methyl-5,6,7,8-tetrahydropteridine decreased from 220 pM to 58 pM. The pH profile for the enzyme activity became more broad and the pH optimum was changed from an acid pH to a neutral pH. Although polyanions, such as heparin and dextran sulfate, markedly stimulated the activity of crude enzyme by increasing the V , they were much less effective in the activation of purified enzyme. A marked stimulation of the enzyme activity by phospholipids, such as phosphatidylserine, phosphatidylinositol, phosphatidylcholine and phosphatidylethanolamine, were not observed in both pure and crude preparations even at low concentrations of the pterin cofactor.Tyrosine 3-monooxygenase [L-tyrosine, tetrahydropteridine : oxygen oxidoreductase (3-hydroxylating)] catalyzes the conversion of tyrosine to 3,4-dihydroxyphenylalanine, which is the initial and rate-limiting step in the biosynthesis of catecholamines such as dopamine, norepinephrine and epinephrine [1,2].

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Purification and Some Properties of Tyrosine 3‐Monooxygenase from Rat Adrenal

Okuno

Fujisawa

1982

European Journal of Biochemistry

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“…We hypothesized that cocaine directly impairs neuronal differentiation and/or growth. As a model of in vitro neuronal differentiation, we used PC-12 cells, a clonal cell line derived from a transplantable rat adrenal pheochromocytoma induced by x-ray irradiation (18)(19)(20). These cells grow in culture as undifferentiated neuroblast cells that are exquisitely sensitive to the mitogenic effects of IGF-I.…”

Section: Introductionmentioning

confidence: 99%

Cocaine differentially inhibits neuronal differentiation and proliferation in vitro.

Zachor

Cherkes²,

Fay³

et al. 1994

J. Clin. Invest.

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The outcome of in utero cocaine exposure is unclear. To determine if cocaine affects neuronal growth and differentiation, we used PC-1 2 cells, which have a mitogenic response to IGF-I and differentiate into neurons on exposure to nerve growth factor. Differentiation was quantified as neurite extension after a 72-h exposure to 20 ng/ml nerve growth factor (dosage at 50% maximal effectiveness) and cocaine doses ranging from 0.01 to 10 gg/ml. The results were 49±2, 40±3, 29±2, 23±2, and 12±2% differentiation with respective cocaine concentrations of 0, 0.01, 0.1, 1, and 10 ,g/ml (P < 0.0001). Cocaine stability studies showed insignificant spontaneous hydrolysis under the conditions of this study. Cocaine did not affect cell viability or number, but had a relatively modest, statistically significant (P < 0.0001 ) inhibitory effect on IGF-I-stimulated thymidine incorporation. The dose-response curves for differentiation vs mitogenic response differed significantly (P = 0.021). Therefore, cocaine inhibition of these processes is probably mediated by different mechanisms, and not caused by generalized toxicity. To our knowledge, this is the first demonstration of cocaine effects on neuronal multiplication and differentiation in vitro. The results suggest in utero exposure may directly impair brain development. (J. Clin. Invest. 1994. 93:1179-1185

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“…Warren, DeLellis et al (4,5) have reported the induction and partial characterization of a transplantable rat pheochromocytoma which expressed the differentiated properties of adrenal chromaffin cells in vitro. Recently, we reported (6) that chromaffin granule-containing cells cultured from this tumor responded to treatment with nerve growth factor protein (NGF) (7)(8)(9) by extending long, branching neuronal-like processes.…”

mentioning

confidence: 99%

Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor.

Greene¹,

Tischler²

1976

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

5,017

3,231

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A single cell clonal line which responds reversibly to nerve growth factor (NGF) subjected to three cycles of washing (with phosphate-buffered saline) and pelleting (500 X g for 5 min) in order to free them from cell debris, and were resuspended in growth medium and plated on plastic tissue culture dishes (Falcon Plastics). The following day, the lightly-adhering pheochromocytoma cells were mechanically dislodged from the plates by forceful aspiration and expulsion of the medium with a pasteur pipette, and replated on culture dishes which were coated with rat tail collagen (10). The cells were subsequently passaged two more times on collagen-coated culture dishes and three more times on plastic culture dishes. This strategy was employed for two reasons. First, newly dissociated pheochromocytoma cells adhered very poorly to plastic culture dishes. After several passages on collagen-coated dishes (to which the cells more firmly attached), the cells had adapted to culture and could be passaged onto plastic dishes. Second, the dissociated tumors contained, in addition to the cells of interest, other cell types which grew much more rapidly than the pheochromocytoma cells and which overgrew the cultures. Such cells adhered very firmly to plastic and collagen-coated substrates and tended to be left behind on the culture dishes after mechanical dislodgement. By the means described, the slowly growing pheochromocytoma cells could be adapted to culture without being overgrown.

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Pheochromocytoma

Cited by 95 publications

References 4 publications

Purification and Some Properties of Tyrosine 3‐Monooxygenase from Rat Adrenal

Purification and Some Properties of Tyrosine 3‐Monooxygenase from Rat Adrenal

Cocaine differentially inhibits neuronal differentiation and proliferation in vitro.

Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor.

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