Methylamine but not mafenide mimics insulin-like activity of the semicarbazide-sensitive amine oxidase-substrate benzylamine on glucose tolerance and on human adipocyte metabolism

Iglesias-Osma, María Carmen; Bour, Sandy; Garcı́a-Barrado, Marı́a José; Visentin, Virgile; Pastor, Maria-Francisca; Testar, Xavier; Marti, Luc; Enrique-Tarancón, Gemma; Valet, Philippe; Moratinos, Julio

doi:10.1016/j.phrs.2005.07.008

Cited by 28 publications

(23 citation statements)

References 35 publications

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“…C ATTANÉ and others 25 apelin had a modest effect on glucose uptake in human AT explants and isolated adipocytes. Insulin, at physiological concentrations, stimulated glucose transport in human AT explants twofold above basal, which is in agreement with previous studies performed on human isolated adipocytes (Iglesias-Osma et al 2005, Wanecq et al 2009) or differentiated cultured adipocytes (Hauner et al 1998). It should be noticed that conversion of glucose into fatty acids (de novo lipogenesis) especially in AT is much lower in humans compared to rodents (Zelewski & Swierczyń ski 1990).…”

Section: Discussionsupporting

confidence: 91%

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Apelin stimulates glucose uptake but not lipolysis in human adipose tissue ex vivo

Attané

Daviaud²,

Dray³

et al. 2010

Journal of Molecular Endocrinology

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Apelin is a peptide present in different cell types and secreted by adipocytes in humans and rodents. Apelin exerts its effects through a G-protein-coupled receptor called APJ. During the past years, a role of apelin/APJ in energy metabolism has emerged. Apelin was shown to stimulate glucose uptake in skeletal muscle through an AMP-activated protein kinase (AMPK)-dependent pathway in mice. So far, no metabolic effects of apelin have been reported on human adipose tissue (AT). Thus, the effect of apelin on AMPK in AT was measured as well as AMPK-mediated effects such as inhibition of lipolysis and stimulation of glucose uptake. AMPK and acetyl-CoA carboxylase phosphorylation were measured by western blot to reflect the AMPK activity. Lipolysis and glucose uptake were measured, ex vivo, in response to apelin on isolated adipocytes and explants from AT of the subcutaneous region of healthy subjects (body mass index: 25 . 6 G0 . 8 kg/m 2 , nZ30 in total). APJ mRNA and protein are present in human AT and isolated adipocytes. Apelin stimulated AMPK phosphorylation at Thr-172 in a dose-dependent manner in human AT, which was associated with increased glucose uptake since C compound (20 mM), an AMPK inhibitor, completely prevented apelin-induced glucose uptake. However, in isolated adipocytes or AT explants, apelin had no significant effect on basal and isoprenaline-stimulated lipolysis. Thus, these results reveal, for the first time, that apelin is able to act on human AT in order to stimulate AMPK and glucose uptake.

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Section: Discussionsupporting

confidence: 91%

“…Glucose uptake by isolated adipocytes was measured as previously described (Iglesias-Osma et al 2005). Briefly, adipocytes (1:10 dilution) were incubated with 1 mM of apelin or 100 nM insulin as a positive control for 45 min at 37 8C and 0 .…”

Section: Glucose Uptakementioning

confidence: 99%

Apelin stimulates glucose uptake but not lipolysis in human adipose tissue ex vivo

Attané

Daviaud²,

Dray³

et al. 2010

Journal of Molecular Endocrinology

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“…In order to verify whether visfatin/Nampt /PEBF1 was able to reproduce the stimulatory effect of insulin on glucose uptake, we chose to study the acute effects of the adipokine/multifunctional enzyme (renamed visfatin for clarity throughout this report) on human fat cells, a model of utmost physiological interest. Therefore, we have tested different origins of visfatin on fat cells preparations highly responsive to insulin, in conditions already used to investigate the insulin-like activity of pharmacological agents (2,11) or hormones (6). Since lipolysis inhibition is also an insulin-sensitive response in human fat cells, we compared insulin and visfatin actions on lipolytic activity.…”

mentioning

confidence: 99%

“…Two groups of age-and weight-matched subjects were constituted over a one-year period. The clinical characteristics of the donors and the biochemical profiles of the corresponding adipocyte preparations are described in Table I (11). Once digested, WAT was filtered and the buoyant adipocytes immediately used for functional assays.…”

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confidence: 99%

Lack of direct insulin-like action of visfatin/Nampt/PBEF1 in human adipocytes

2009

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Visfatin, a protein identified as a secretion product of visceral fat in humans and mice, is also expressed in different anatomical locations, and is known as pre-B cell-colony enhancing factor (PEBF1). It is also an enzyme displaying nicotinamide phosphoribosyltransferase activity (Nampt). The evidence that levels of visfatin correlate with visceral fat mass has been largely debated and widely extended to other regulations in numerous clinical studies and in diverse animal models. On the opposite, the initial findings regarding the capacity of visfatin/Nampt/PEBF1 to bind and to activate the insulin receptor have been scarcely reproduced, and even were contradicted in recent reports. Since the putative insulin mimicking effects of visfatin/Nampt/PEBF1 have never been tested on mature human adipocytes, at least to our knowledge, we tested different human visfatin batches on human fat cells freshly isolated from subcutaneous abdominal fat and exhibiting high insulin responsiveness. Up to 10 nM, visfatin was devoid of clear activatory action on glucose transport in human fat cells while, in the same conditions, insulin increased by more than threefold the basal 2-deoxyglucose uptake. Moreover, visfatin was unable to mimic the lipolysis inhibition induced by insulin. Visfatin definitively cannot be considered as a direct activator of insulin signalling in human fat cells. Nevertheless itsin vivo effects on insulin release and on glucose handling deserve to further study the role of this multifunctional extracellular enzyme in obese and diabetic states.

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“…15,16 However, in diabetic animal studies, modulating SSAO has divergent effects, some adverse and some beneficial. Administration of methylamine (another SSAO substrate) to animals improves glycaemia, 17 but promotes hypertension, atherosclerosis and glomerulosclerosis, 18 thought to relate to reactive aldehydes from methylamine oxidation, which has been averted by administration of different SSAO substrates. 13,19,20 Most human data regarding SSAO activity in diabetes relate to type 2 diabetes (T2DM), with few studies in type 1 diabetes (T1DM).…”

Section: Introductionmentioning

confidence: 99%

Plasma semicarbazide-sensitive amine oxidase activity in type 1 diabetes is related to vascular and renal function but not to glycaemia

Januszewski

Mason

Karschimkus

et al. 2014

Diabetes and Vascular Disease Research

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Purpose: Associations of semicarbazide-sensitive amine oxidase (SSAO) activity with renal and vascular function, oxidative stress, glycaemia and diabetes complications were determined. Methods: Plasma SSAO activity in 94 type 1 diabetes (T1DM) patients, including 34 with microvascular complications T1DM CX [+], and in 96 healthy subjects (CON) was measured by production of benzaldehyde using high-performance liquid chromatography (HPLC). Conclusion:In T1DM, SSAO activity correlates with renal dysfunction, but not with glycaemia, and may promote vascular inflammation and be a therapeutic target.

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Methylamine but not mafenide mimics insulin-like activity of the semicarbazide-sensitive amine oxidase-substrate benzylamine on glucose tolerance and on human adipocyte metabolism

Cited by 28 publications

References 35 publications

Apelin stimulates glucose uptake but not lipolysis in human adipose tissue ex vivo

Apelin stimulates glucose uptake but not lipolysis in human adipose tissue ex vivo

Lack of direct insulin-like action of visfatin/Nampt/PBEF1 in human adipocytes

Plasma semicarbazide-sensitive amine oxidase activity in type 1 diabetes is related to vascular and renal function but not to glycaemia

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