On the physiological role of neurocuprein: Aponeurocuprein is an inhibitor of dopamine β-monooxygenase

Markossian, Kira A.; Paitian, Norair A.; Mikaelyan, Mariam V.; Nalbandyan, R.M.

doi:10.1016/0006-291x(86)90238-x

Cited by 8 publications

(1 citation statement)

References 27 publications

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“…It is interesting in this connection to mention the discovery of a small acidic non-blue protein, neurocuproin, that appears to be present in catecholamine storage vesicles of both adrenal medullae and adrenergic neurons (Grigoryan et al, 1981;Sharoyan et al, 1977), which may be a possible candidate for copper transfer to DBH. Of particular significance is the finding that aponeurocuproin is able to inhibit DBH activity, presumably by a mechanism related to copper chelation, and regulation of DBH activity has been suggested as a possible physiological role for the holoneurocuproin molecule (Markossian et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

Active site of dopamine .beta.-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy

et al. 1988

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Potentiometric titrations, continuous wave EPR, and microwave power saturation measurements have been used to examine 8-Cu and 4-Cu forms of native dopamine beta-hydroxylase and its azide derivative. The formation curve for the binding of Cu2+ to the apoenzyme is best fit by assuming two independent binding sites per subunit, with pK' values of 8.90 and 7.35 at pH 5.0. On the other hand, only minor differences are observed in either continuous wave EPR spectra or power saturation behavior of the 8- and 4-Cu forms of the native enzyme or of its azide derivative. The intensity of the EPR spectra of all derivatives integrates to greater than 95% of the total copper, and the temperature dependence of P1/2 shows no evidence for any S = 1 state of the copper ions in the enzyme. These results suggest a lower limit of ca. 7 A for the separation between the two copper ions per subunit and thus rule out a type 3 site in the oxidized enzyme. The data are most consistent with Cu(II) sites consisting of two or three N (imidazole) and one or two O donor ligands in the coordination sphere. The similarity in EPR spectra and power saturation of 8- and 4-Cu derivatives suggests that the difference in Cu-binding constants may be due either to differences in the identity of an axial ligand or to solvation effects in the active site.

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Section: Discussionmentioning

confidence: 99%

Active site of dopamine .beta.-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy

et al. 1988

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Reconstitution of neurocupreins by Cu-thioneins

1989

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Immunological characterization of peptidyl‐glycine‐α‐amidating monooxygenases

Sharoyan¹,

Nalbandyan²

1991

FEBS Letters

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Antibodies to the soluble form of the copper‐containing enzyme, peptidyl‐glycine‐α‐amidating monooxygenase isolated from secretory granules of bovine pituitary anterior lobes were found to belong to immunoglobulin G1. The antibodies were used to study the subcellular distribution of the enzyme in this tissue, and positive tests were found only for granular and cytosol fractions. The antibodies do not crossreact with other copper‐containing systems of secretory granules, such as neurocuprein and dopamine‐ß‐monooxygenase. It was shown that the antibodies give the crossreaction with the enzyme isolated from secretory granules of bovine pituitary anterior lobes, cardiac atria, pancreas and adrenal medulla, indicating the antigenic identity of the enzyme from secretory granules of different glands.

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On the physiological role of neurocuprein: Aponeurocuprein is an inhibitor of dopamine β-monooxygenase

Cited by 8 publications

References 27 publications

Active site of dopamine .beta.-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy

Active site of dopamine .beta.-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy

Reconstitution of neurocupreins by Cu-thioneins

Immunological characterization of peptidyl‐glycine‐α‐amidating monooxygenases

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