Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

Simić-Krstić, Jovana; Ševaljević, Ljiljana

doi:10.1159/000163471

Cited by 2 publications

(1 citation statement)

References 12 publications

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“…Notably, the water-soluble hydroxylated fullerene, fullerenol, has been applied in many biomedical areas. Fullerenol can inhibit tumor cell growth via blocking the microtubule assembly in vitro [2] and metallofullerenol Gd@C 82 (OH) 22 shows strong antitumor activity in tumor-bearing mice without side effects [3]. Because of the impressive antioxidative potential and radical scavenging activity, fullerenol also has been used to reduce the cardiotoxicity [4] and provide radioprotection [5].…”

Section: Introductionmentioning

confidence: 99%

Interaction of fullerenol with lysozyme investigated by experimental and computational approaches

et al. 2008

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The potential biomedical applications of fullerenol C(60)(OH)(x) (x≈24) have been extensively studied. However, the structural information of the interaction of fullerenol with the bio-system at the molecular level, which is essential for understanding its bioactivity and toxicity, is still missing. In this study, lysozyme was selected as a model protein to investigate the interaction between fullerenol and biomolecules. A strong induced circular dichroism (CD) signal of achiral fullerenol was observed after binding with lysozyme. Activity assay shows that lysozyme activity is inhibited significantly by fullerenol. No heat capacity difference between the folded and unfolded states of lysozyme was measured by differential scanning calorimetry (DSC) in the presence of fullerenol, indicating that fullerenol prefers to bind with the hydrophobic residues. Both experimental and Autodock computational results suggest that the binding site on lysozyme for fullerenol is close to Trp 62, and a π-π stacking interaction might play an important role in binding.

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Section: Introductionmentioning

confidence: 99%

Interaction of fullerenol with lysozyme investigated by experimental and computational approaches

et al. 2008

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The expression of functional MSH receptors on cultured human melanocytes

et al. 1992

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Although alpha-MSH increases skin darkening in humans, there are several reports that it fails to have melanogenic effects on human melanocytes in vitro. The purpose of this study was to see whether cultured human melanocytes express MSH receptors. Human melanocytes were grown in the absence of artificial mitogens such as 12-O-tetradecanoyl phorbol-13-acetate (TPA) and cholera toxin (CT) and incubated for 2 h at room temperature with increasing amounts of 125I-labelled Nle4DPhe7-alpha-MSH with and without excess cold peptide. Binding was saturable and specific: Scatchard analysis gave a Kd of 4.9 x 10(-11) M and approximately 700 binding sites/cell. Human keratinocytes and fibroblasts showed no specific binding. The addition of 1 mM dibutyryl cAMP to the culture medium caused a 62% increase in MSH binding to human melanocytes. A smaller increase (25%) was seen with 10(-9) M CT while 25 mM TPA caused a 24% decrease. These results show that human melanocytes in culture express MSH receptors and that this expression can be modulated by mitogens.

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Adrenocorticotropin Binding Activity of B16/C3 Melanoma Cells

Cited by 2 publications

References 12 publications

Interaction of fullerenol with lysozyme investigated by experimental and computational approaches

Interaction of fullerenol with lysozyme investigated by experimental and computational approaches

The expression of functional MSH receptors on cultured human melanocytes

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