Soluble and membrane-bound forms of dopamine beta-hydroxylase are encoded by the same mRNA.

Lewis, Elaine J.; Asnani, L P

doi:10.1016/s0021-9258(18)48522-5

Cited by 36 publications

(4 citation statements)

References 30 publications

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“…As mentioned above, the copper enzyme, DβM, catalyzes the conversion of DA to NE in NE and E synaptic vesicles [for reviews see refs ( Stewart and Klinman, 1988 ; Gonzalez-Lopez and Vrana, 2020 ; Schemes 4 , 5 )]. Early estimates have demonstrated that equal amounts of sequentially and structurally related ( Stewart and Klinman, 1988 ; Gonzalez-Lopez and Vrana, 2020 ) membrane bound (mDβM) and soluble (sDβM) forms of DβM are present in NE and E synaptic vesicles ( Lewis and Asnani, 1992 ). After exocytotic release, while sDβM is discarded ( Scheme 6 ), mDβM is recycled through synaptic membrane recycling pathway ( Wimalasena and Wimalasena, 2004 ).…”

Section: Critical Evaluation and Discussion Of The Evidence For The H...mentioning

confidence: 99%

Metabolic energy decline coupled dysregulation of catecholamine metabolism in physiologically highly active neurons: implications for selective neuronal death in Parkinson’s disease

Wimalasena,

Adetuyi,

Eldani

2024

Front. Aging Neurosci.

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Parkinson’s disease (PD) is an age-related irreversible neurodegenerative disease which is characterized as a progressively worsening involuntary movement disorder caused by the loss of dopaminergic (DA) neurons in substantia nigra pars compacta (SNpc). Two main pathophysiological features of PD are the accumulation of inclusion bodies in the affected neurons and the predominant loss of neuromelanin-containing DA neurons in substantia nigra pars compacta (SNpc) and noradrenergic (NE) neurons in locus coeruleus (LC). The inclusion bodies contain misfolded and aggregated α-synuclein (α-Syn) fibrils known as Lewy bodies. The etiology and pathogenic mechanisms of PD are complex, multi-dimensional and associated with a combination of environmental, genetic, and other age-related factors. Although individual factors associated with the pathogenic mechanisms of PD have been widely investigated, an integration of the findings to a unified causative mechanism has not been envisioned. Here we propose an integrated mechanism for the degeneration of DA neurons in SNpc and NE neurons in LC in PD, based on their unique high metabolic activity coupled elevated energy demand, using currently available experimental data. The proposed hypothetical mechanism is primarily based on the unique high metabolic activity coupled elevated energy demand of these neurons. We reason that the high vulnerability of a selective group of DA neurons in SNpc and NE neurons in LC in PD could be due to the cellular energy modulations. Such cellular energy modulations could induce dysregulation of DA and NE metabolism and perturbation of the redox active metal homeostasis (especially copper and iron) in these neurons.

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Section: Critical Evaluation and Discussion Of The Evidence For The H...mentioning

confidence: 99%

Metabolic energy decline coupled dysregulation of catecholamine metabolism in physiologically highly active neurons: implications for selective neuronal death in Parkinson’s disease

Wimalasena,

Adetuyi,

Eldani

2024

Front. Aging Neurosci.

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“…Dopamine fl-hydroxylase (EC 1.14.17.1) is a glycoprotein which hydroxylates dopamine to norepinephrine during the biosynthesis of catecholamines. The enzyme occurs in the synaptic vesicles of noradrenergic and adrenergic brain nerves and sympathetic ganglions, as well as in the storage granules of chromaffinic cells of the adrenal medulla [163].…”

Section: Dopamine Fl-hydroxylasementioning

confidence: 99%

“…The holoenzyme is a tetramer of 290 kD molecular mass, consisting of two, reversibly associated, disulfide-linked dimers [164][165][166]. Dopamine/~-hydroxylase occurs in a soluble and a membrane-associated form [167,168], which are both encoded by the same mRNA [163]. Dissociation of the enzyme results in monomers of either approximately 72-73 kD or 75-77 kD molecular mass.…”

Section: Dopamine Fl-hydroxylasementioning

confidence: 99%

“…Its release would occur by the removal of the membrane anchor and the loss of a non-covalently bound phospholipid which possibly collaborates in keeping the enzyme membrane-bound [167,170]. These differences in weight of soluble and membrane-bound enzyme may, however, be based on differences in their degree of glycosylation and not on the lengths of their peptide chains [163,172], an explanation supported by the fact that the 72-73 kD monomers occur in both forms [163,169,171]. This, however, would require that the peptide anchor, if it even exists, is not the only structure for affixing the enzyme to the membrane, a role which might be assumed by the non-covalently bound phospholipid.…”

Section: Dopamine Fl-hydroxylasementioning

confidence: 99%

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Evolutionary aspects of copper binding centers in copper proteins

Abolmaali

Taylor

Weser

Structure and Bonding

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A great number of active centers in proteins and enzymes contain transition metals. Each metal imposes specific catalytic properties on the protein which could not be achieved when employing a different metal. The special role and characteristic reactivity of coordinated copper is illustrated by looking at the evolutionary aspects of copper proteins. The evolution of copper-binding sites is closely linked to that of copper proteins. Copper centers have evolved according to various principles, similar to the evolutionary development of proteins and enzymes. Three basic principles may be observed: the copper-binding centers of metallothioneins and type 1 copper centers developed in non-metal proteins; the transformation of the metal-binding centers of iron or manganese proteins led to the development of the type 2 copper centers; and the trinuclear copper-binding centers of the blue oxidases were formed by alterations and recombinations of type 1 copper centers. Simple, although as yet unknown, mononuclear copper centers gave rise to the type 3 copper-binding sites of the hemocyanins and tyrosinases, as well as to the Cu A-and CUB-centers of the cytochrome oxidases and N20reductase. According to this assignment, copper proteins containing either type 1 copper, type 3 copper, CUA-centers, or CUB-centers share a common ancestor. They developed at least in part by divergent evolution. Type 2 copper proteins are the products of convergent evolution and, consequently, show little or no phylogenetic homology.

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Dopamine Beta‐Hydroxylase

Kim¹,

Cubells²

2002

Wiley Encyclopedia of Molecular Medicine

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Soluble and membrane-bound forms of dopamine beta-hydroxylase are encoded by the same mRNA.

Cited by 36 publications

References 30 publications

Metabolic energy decline coupled dysregulation of catecholamine metabolism in physiologically highly active neurons: implications for selective neuronal death in Parkinson’s disease

Metabolic energy decline coupled dysregulation of catecholamine metabolism in physiologically highly active neurons: implications for selective neuronal death in Parkinson’s disease

Evolutionary aspects of copper binding centers in copper proteins

Dopamine Beta‐Hydroxylase

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