Selenium attenuates pro‐inflammatory gene expression in macrophages

Vunta, Hema; Belda, Benjamin J.; Arner, Ryan J.; Reddy, C. Channa; Heuvel, John P. Vanden; Prabhu, K. Sandeep

doi:10.1002/mnfr.200700346

Cited by 144 publications

(113 citation statements)

References 25 publications

(35 reference statements)

Supporting

Mentioning

106

Contrasting

Unclassified

Order By: Relevance

“…The literature has extensively implicated selenium in the modulation of immune processes, particularly in relation to macrophage activity (54)(55)(56). We noted an increase in M2 polarized macrophages in tumors of AOM/DSS-treated Sepp1 +/-mice and hypothesized that this was due to an effect of SEPP1 on macrophage polarization.…”

Section: Sepp1mentioning

confidence: 77%

Selenoprotein P influences colitis-induced tumorigenesis by mediating stemness and oxidative damage

et al. 2015

View full text Add to dashboard Cite

Section: Sepp1mentioning

confidence: 77%

Selenoprotein P influences colitis-induced tumorigenesis by mediating stemness and oxidative damage

et al. 2015

View full text Add to dashboard Cite

“…LPS-induced TNF-α secretion from macrophages cultured in selenium-depleted medium is markedly enhanced (51). A population study has correlated circulating TNF-α/IL-6 levels with a SNP in the SELS gene and siRNA knockdown of SELS in macrophages enhances LPS-induced TNF-α and IL-6 secretion (52).…”

Section: Figurementioning

confidence: 99%

Mutations in the selenocysteine insertion sequence–binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans

Schoenmakers¹,

Agostini²,

Mitchell³

et al. 2010

J. Clin. Invest.

288

236

View full text Add to dashboard Cite

Selenium, a trace element that is fundamental to human health, is incorporated into some proteins as selenocysteine (Sec), generating a family of selenoproteins. Sec incorporation is mediated by a multiprotein complex that includes Sec insertion sequence-binding protein 2 (SECISBP2; also known as SBP2). Here, we describe subjects with compound heterozygous defects in the SECISBP2 gene. These individuals have reduced synthesis of most of the 25 known human selenoproteins, resulting in a complex phenotype. Azoospermia, with failure of the latter stages of spermatogenesis, was associated with a lack of testis-enriched selenoproteins. An axial muscular dystrophy was also present, with features similar to myopathies caused by mutations in selenoprotein N (SEPN1). Cutaneous deficiencies of antioxidant selenoenzymes, increased cellular ROS, and susceptibility to ultraviolet radiation-induced oxidative damage may mediate the observed photosensitivity. Reduced levels of selenoproteins in peripheral blood cells were associated with impaired T lymphocyte proliferation, abnormal mononuclear cell cytokine secretion, and telomere shortening. Paradoxically, raised ROS in affected subjects was associated with enhanced systemic and cellular insulin sensitivity, similar to findings in mice lacking the antioxidant selenoenzyme glutathione peroxidase 1 (GPx1). Thus, mutation of SECISBP2 is associated with a multisystem disorder with defective biosynthesis of many selenoproteins, highlighting their role in diverse biological processes.

show abstract

“…In addition, we have evaluated the cellular uptake of Man-Lip-Se using M receptor expressing MH-S macrophage cells. The deficiency of selenium in macrophage cells has been linked to asthma (40). For this investigation, we have used sodium selenite as the dietary source of Se.…”

Section: Introductionmentioning

confidence: 99%

Freeze-Dried Targeted Mannosylated Selenium-Loaded Nanoliposomes: Development and Evaluation

et al. 2013

View full text Add to dashboard Cite

Abstract. The aim of this investigation was to develop and evaluate freeze-dried mannosylated liposomes for the targeted delivery of selenium. Dipalmitoylphosphatidylcholine, distearoylphosphatidylglycerol, and cholesterol were dissolved in a chloroform and methanol mixture and allowed to form a thin film within a rotatory evaporator. This thin film was hydrated with a sodium selenite (5.8 μM) solution to form multilamellar vesicles and homogenized under high pressure to yield unilamellar nanoliposomes. Seloaded nanoliposomes were mannosylated by 0.1%w/v mannosamine (Man-Lip-Se) prior to being lyophilized. Mannosamine concentration was optimized with cellular uptake studies in M receptor expressing cells. Non-lyophilized and lyophilized Man-Lip-Se were characterized for size, zeta potential, and entrapment efficiency. The influence of liposomal composition on the characteristics of Man-Lip-Se were evaluated using acidic and basic medium for 24 h. Thermal analysis and powder X-ray diffraction were used to determine the interaction of components within the Man-Lip-Se. The size, zeta potential and entrapment efficiency of the optimum Man-Lip-Se were observed to be 158±28.9 nm, 33.21±0.89 mV, and 77.27±2.34%, respectively. An in vitro Se release of 70-75% up to 24 h in PBS pH 6.8 and <8% Se release in acidic media (0.1 N HCl) in 1 h was observed. The Man-Lip-Se were found to withstand gastric-like environments and showed sustained release. Stable freeze-dried Man-Lip-Se were successfully formulated with a size of <200 nm, ∼75% entrapment, and achieved controlled release of Se with stability under acidic media, which may be of importance in the targeted delivery of Se to the immune system.

show abstract

Selenium attenuates pro‐inflammatory gene expression in macrophages

Cited by 144 publications

References 25 publications

Selenoprotein P influences colitis-induced tumorigenesis by mediating stemness and oxidative damage

Selenoprotein P influences colitis-induced tumorigenesis by mediating stemness and oxidative damage

Mutations in the selenocysteine insertion sequence–binding protein 2 gene lead to a multisystem selenoprotein deficiency disorder in humans

Freeze-Dried Targeted Mannosylated Selenium-Loaded Nanoliposomes: Development and Evaluation

Contact Info

Product

Resources

About