The expression of human resistin in different leucocyte lineages is modulated by LPS and TNFα

Kunnari, Anne; Savolainen, Eeva‐Riitta; Ukkola, Olavi; Kesäniemi, Y. Antero; Jokela, Maarit

doi:10.1016/j.regpep.2009.05.002

Cited by 54 publications

(38 citation statements)

References 32 publications

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“…Further studies have shown that, in humans, peripheral blood mononuclear cells, macrophages and neutrophils are the primary source of resistin (Bostrom et al 2009;Jung et al 2006;Kunnari et al 2009;Johansson et al 2009) and that resistin is mainly involved in inflammation (Nagaev et al 2006). Clinical studies have demonstrated that serum resistin level is elevated in patients with obesity-associated diabetes or cardiovascular disease and that the plasma resistin level is correlated with the markers of inflammation (Reilly et al 2005;Takata et al 2008).…”

Section: Discussionmentioning

confidence: 99%

“…The sites of resistin expression differ considerably amongst species. Whereas resistin in mice is mainly expressed in adipocytes (Steppan et al 2001), it is primarily synthesized by monocytes/macrophages and neutrophils in humans (Patel et al 2003;Yang et al 2003;Bostrom et al 2009;Kunnari et al 2009;Johansson et al 2009). Studies to determine the function of resistin in humans have indicated that recombinant human resistin promotes endothelial cell activation by inducing the release of endothelin-1, the upregulation of vascular cell adhesion molecule 1 (VCAM-1) and monocyte chemoattractant protein 1 (MCP-1) and the downregulation of tumor necrosis factor receptor-associated factor-3 (TRAF3) in human saphenous vein endothelial cells (Verma et al 2003), the up-regulation of adhesion molecules VCAM-1, intercellular adhesion molecule-1 (ICAM-1), and long pentraxin 3, a marker of inflammation in vascular endothelial cells (Kawanami et al 2004) and the upregulation of fractalkine (Manduteanu et al 2009) and P-selectin ( Manduteanu et al 2010) in human endothelial cells; these factors are functional in monocyte adhesion to the endothelium.…”

Section: Introductionmentioning

confidence: 99%

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High glucose induces enhanced expression of resistin in human U937 monocyte-like cell line by MAPK- and NF-kB-dependent mechanisms; the modulating effect of insulin

Stan¹,

Calin²,

Manduteanu³

et al. 2010

Cell Tissue Res

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Resistin has emerged as a significant local and systemic regulatory cytokine involved in inflammation. In diabetic patients, the serum resistin level is increased, monocytes/macrophages being an important source of resistin production. We therefore hypothesize that high glucose concentrations (HG) regulate resistin expression in human monocytes. Our aim has been to uncover the potential signalling pathways involved in this process. We have also questioned whether insulin has an effect on the regulation of resistin expression induced by HG. Human monocytes (U937 cell line) were exposed to 25 mM glucose for 24 h and then resistin gene expression and protein levels were determined by reverse transcription with the polymerase chain reaction and Western blot assays. We found that (1) the gene expression and protein level of resistin were up-regulated by HG; (2) the inhibitors of the mitogen-activated protein kinases (MAPKs) p38 (SB203580), extracellular signal-regulated kinases 1/2 (ERK1/2; PD98059) and c-Jun N-terminal kinase (SP600125) and of the transcription factor nuclear factor kappa-B (PDTC) inhibited HG-induced resistin protein production and (3) insulin reduced HG-induced resistin expression via a mechanism independent of phosphatidylinositol 3-kinase (PI3K) or p38 and ERK1/2. Therefore, HG significantly increases resistin gene expression and protein production in the U937 cell line by mechanisms involving MAPKs and the transcription factor NF-kB, whereas insulin reduces its expression. This study adds new data concerning the molecular mechanisms involved in the pro-inflammatory effects of HG on human monocytes.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

High glucose induces enhanced expression of resistin in human U937 monocyte-like cell line by MAPK- and NF-kB-dependent mechanisms; the modulating effect of insulin

Stan¹,

Calin²,

Manduteanu³

et al. 2010

Cell Tissue Res

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show abstract

“…In humans, resistin is expressed in and secreted by monocytes and macrophages in addition to adipocytes (140,170). It promotes vascular SMC migration (120) and proliferation (33), induces monocyte-endothelial cell adhesion, and increases the expression of VCAM-1, ICAM-1, and MCP-1 in endothelial cells (286).…”

Section: Adipokines With Less Strong Evidence For Involvement In Cardmentioning

confidence: 99%

Inflammation and metabolic dysfunction: links to cardiovascular diseases

Taube

Schlich

Sell

et al. 2012

American Journal of Physiology-Heart and Circulatory Physiology

204

133

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Abdominal obesity is a major risk factor for cardiovascular disease, and recent studies highlight a key role of adipose tissue dysfunction, inflammation, and aberrant adipokine release in this process. An increased demand for lipid storage results in both hyperplasia and hypertrophy, finally leading to chronic inflammation, hypoxia, and a phenotypic change of the cellular components of adipose tissue, collectively leading to a substantially altered secretory output of adipose tissue. In this review we have assessed the adipo-vascular axis, and an overview of adipokines associated with cardiovascular disease is provided. This resulted in a first list of more than 30 adipokines. A deeper analysis only considered adipokines that have been reported to impact on inflammation and NF-κB activation in the vasculature. Out of these, the most prominent link to cardiovascular disease was found for leptin, TNF-α, adipocyte fatty acid-binding protein, interleukins, and several novel adipokines such as lipocalin-2 and pigment epithelium-derived factor. Future work will need to address the potential role of these molecules as biomarkers and/or drug targets.

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“…In rodents, resistin is located within adipocytes, while human resistin is primarily expressed in macrophages and neutrophils (13)(14)(15). Human resistin is released in response to inflammatory stimuli (16), and is found at elevated levels in autoimmune disease and sepsis (17). Previous studies have shown that resistin impairs cardiomyocyte glucose handling and induces cardiac hypertrophy (8,10).…”

Section: Introductionmentioning

confidence: 99%

Resistin-induced cardiomyocyte hypertrophy is inhibited by apelin through the inactivation of extracellular signal-regulated kinase signaling pathway in H9c2 embryonic rat cardiomyocytes

et al. 2016

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Abstract. It has been reported that resistin induces, whereas apelin inhibits cardiac hypertrophy. However, the underlying molecular mechanisms of apelin inhibiting resistin-induced cardiac hypertrophy remain unclear. The aim of the current study is to investigate the effects of apelin on resistin-induced cardiomyocyte hypertrophy and elucidate the underlying molecular mechanism. H9c2 cells were used in the present study, and cell surface area and protein synthesis were evaluated. Reverse transcription-quantitative polymerase chain reaction was performed to analyze the expression levels of hypertrophic markers, brain natriuretic peptide (BNP) and β-myosin heavy chain (β-MHC). In addition, western blotting was conducted to examine phosphorylation of extracellular signal-regulated kinase (ERK)1/2. Following treatment of H9c2 cells with resistin, cell surface area, protein synthesis, and BNP and β-MHC mRNA expression levels were increased. Subsequent to co-treatment of H9c2 cells with apelin and resistin, lead to the inhibition of resistin-induced hypertrophic effects by apelin. In addition, treatment with resistin increased phosphorylation of ERK1/2, whereas pretreatment with apelin decreased phosphorylation of ERK1/2, which was increased by resistin. These results indicate that resistin-induced cardiac hypertrophy is inhibited by apelin via inactivation of ERK1/2 cell signaling.

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The expression of human resistin in different leucocyte lineages is modulated by LPS and TNFα

Cited by 54 publications

References 32 publications

High glucose induces enhanced expression of resistin in human U937 monocyte-like cell line by MAPK- and NF-kB-dependent mechanisms; the modulating effect of insulin

High glucose induces enhanced expression of resistin in human U937 monocyte-like cell line by MAPK- and NF-kB-dependent mechanisms; the modulating effect of insulin

Inflammation and metabolic dysfunction: links to cardiovascular diseases

Resistin-induced cardiomyocyte hypertrophy is inhibited by apelin through the inactivation of extracellular signal-regulated kinase signaling pathway in H9c2 embryonic rat cardiomyocytes

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