Zinc as activating cation for muscle glycolysis.

Tamaki, Nanaya; Ikeda, Tatsuhiko; Funatsuka, Akimi

doi:10.3177/jnsv.29.655

Cited by 22 publications

(15 citation statements)

References 11 publications

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“…Furthermore, Zn participates in apo-enzyme synthesis by influencing DNA stability as well as being an integral part of DNAbinding protein (Zn-finger) motifs. A direct relationship between cellular Zn concentrations and altered carbohydrate metabolism in rat hepatocytes has been described [229], supporting previous studies showing Zn stimulation of muscle glycolysis [230], inhibition of glycogen synthesis [231] and alterations of cellular energy metabolism [232]. The reactivation of Zn requiring apo-forms of aldolase, alkaline phosphatase and carbonic anhydrase by ZnMT was first demonstrated over 20 years ago [233,234].…”

Section: Mt and Metabolismmentioning

confidence: 71%

Metallothionein: the multipurpose protein

Coyle¹,

Philcox²,

Lc³

et al. 2002

Cellular and Molecular Life Sciences (CMLS)

1,159

803

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Metallothioneins (MTs) are intracellular, low molecular, low molecular weight, cysteine-rich proteins. Ubiquitous in eukaryotes, MTs have unique structural characteristics to give potent metal-binding and redox capabilities. A primary role has not been identified, and remains elusive, as further functions continue to be discovered. The most widely expressed isoforms in mammals, MT-1 and MT-2, are rapidly induced in the liver by a wide range of metals, drugs and inflammatory mediators. In teh gut and pancreas, MT responds mainly to Zn status. A brain isoform, MT-3, has a specific neuronal growth inhibitory activity, while MT-1 and MT-2 have more diverse functions related to their thiolate cluster structure. These include involvement in Zn homeostasis, protection against heavy metal (especially Cd) and oxidant damage, and metabolic regulation via Zn donation, sequestration and/or redox control. Use of mice with altered gene expression has enhance our understanding of the multifaceted role of MT, emphasised in this review.

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Section: Mt and Metabolismmentioning

confidence: 71%

Metallothionein: the multipurpose protein

Coyle¹,

Philcox²,

Lc³

et al. 2002

Cellular and Molecular Life Sciences (CMLS)

1,159

803

View full text Add to dashboard Cite

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“…Zinc is known to stimulate glycolysis and inhibit gluconeogenesis, an effect that is not overcome by the presence of glucagon [ 42 – 44 ]. In-vitro studies have demonstrated that Zinc increases the activity of glycolytic enzymes, phosphofructokinase (PFK) and pyruvate kinase (PK) in a concentration- and time-dependent manner [ 45 , 46 ]. Lactate production which reflects the PFK activity, was increased by Zinc [ 46 ].…”

Section: Resultsmentioning

confidence: 99%

“…In-vitro studies have demonstrated that Zinc increases the activity of glycolytic enzymes, phosphofructokinase (PFK) and pyruvate kinase (PK) in a concentration- and time-dependent manner [ 45 , 46 ]. Lactate production which reflects the PFK activity, was increased by Zinc [ 46 ]. However, the effects of Zinc and insulin were not additive and Zinc pretreatment prevented the stimulation of glycolytic enzymes by insulin.…”

Section: Resultsmentioning

confidence: 99%

Zinc and diabetes mellitus: understanding molecular mechanisms and clinical implications

et al. 2015

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BackgroundDiabetes mellitus is a leading cause of morbidity and mortality worldwide. Studies have shown that Zinc has numerous beneficial effects in both type-1 and type-2 diabetes. We aim to evaluate the literature on the mechanisms and molecular level effects of Zinc on glycaemic control, β-cell function, pathogenesis of diabetes and its complications.MethodsA review of published studies reporting mechanisms of action of Zinc in diabetes was undertaken in PubMed and SciVerse Scopus medical databases using the following search terms in article title, abstract or keywords; (“Zinc” or “Zn”) and (“mechanism” or “mechanism of action” or “action” or “effect” or “pathogenesis” or “pathology” or “physiology” or “metabolism”) and (“diabetes” or “prediabetes” or “sugar” or “glucose” or “insulin”).ResultsThe literature search identified the following number of articles in the two databases; PubMed (n = 1799) and SciVerse Scopus (n = 1879). After removing duplicates the total number of articles included in the present review is 111. Our results show that Zinc plays an important role in β-cell function, insulin action, glucose homeostasis and the pathogenesis of diabetes and its complications.ConclusionNumerous in-vitro and in-vivo studies have shown that Zinc has beneficial effects in both type-1 and type-2 diabetes. However further randomized double-blinded placebo-controlled clinical trials conducted for an adequate duration, are required to establish therapeutic safety in humans.Electronic supplementary materialThe online version of this article (doi:10.1186/s40199-015-0127-4) contains supplementary material, which is available to authorized users.

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“…After 20 min, the incubations were stopped by the addition of 0.1 volume of 35% HClO 4 . The values are the means Ϯ S.E.…”

Section: On Metabolite Concentration Of Hepatocytes In the Presence Amentioning

confidence: 99%

Intracellular Zinc Movement and Its Effect on the Carbohydrate Metabolism of Isolated Rat Hepatocytes

Brand

Kleineke

1996

Journal of Biological Chemistry

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The effect of zinc ions on carbohydrate metabolism and intracellular Zn2+ was studied in hepatocytes from fed rats. The addition of ZnCl2 to the medium led to an almost 3-fold increase in lactate production and an increase in net glucose production of about 50%. Half-maximal rates occurred at about 40 microM ZnCl2. These effects were not seen with Mn2+, Co2+, or Ni2+ up to 80 microM, whereas Cu2+ at 80 microM and Cd2+ or Pb2+ at 8 microM exhibited similar effects as 80 microM ZnCl2. Changes in intracellular Zn2+ were followed by single cell epifluorescence using zinquin as a specific probe. Intracellular free Zn2+ in isolated hepatocytes was 1.26 +/- 0.27 microM, and the addition of ZnCl2 led to a concentration-dependent increase in epifluorescence. CdCl2 or PbCl2 at 8 microM was as potent as ZnCl2 at 20-80 microM, whereas NiCl2 at 80 microM was without effect. ZnCl2 completely abolished the inhibition of glycolysis by glucagon (cAMP). Glucagon led to a pronounced drop in cytosolic Zn2+. Both glucagon and zinc stimulated glycogenolysis by increasing the phosphorylation of glycogen phosphorylase but acted oppositely on glycolysis. Zinc overcame the inactivation of pyruvate kinase by glucagon without changing the hormone-induced protein phosphorylation. The antagonistic action of zinc and cAMP on glycolysis together with the rapid and marked decrease in free zinc concentration induced by glucagon (cAMP) may indicate an as yet unknown role of zinc as an important mediator of regulation of carbohydrate metabolism.

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Zinc as activating cation for muscle glycolysis.

Cited by 22 publications

References 11 publications

Metallothionein: the multipurpose protein

Metallothionein: the multipurpose protein

Zinc and diabetes mellitus: understanding molecular mechanisms and clinical implications

Intracellular Zinc Movement and Its Effect on the Carbohydrate Metabolism of Isolated Rat Hepatocytes

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