Antibody constant region: Potential to bind metal and nucleic acid

Radulescu, Razvan T.

doi:10.1016/0306-9877(95)90087-x

Cited by 10 publications

(9 citation statements)

References 48 publications

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“…It was previously shown that immunoglobulins express metal binding sites in the conserved [14] and variable region of the molecule [13,15]. Histidine or tryptophane residues participate in the formation of copper binding sites [13,15].…”

Section: Resultsmentioning

confidence: 99%

“…There are data on the expression of metal-binding sites in proteins of γ-globulin fraction, on the presence of bound copper in these biomacromolecules, and realization of some intermolecular interactions involving γ-globulins and IgG through copper cation exchange [2,3,14,15].…”

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confidence: 99%

“…Metal transport in biological fluids and tissues is realized by serum and tissue forms of ceruloplasmin (CP). In mammalians the greater part of copper ions is bound to CP.Albumin ranks second among copper transporter [5], while serum globulin fraction proteins, specifically, γ-globulins, little contribute to cation binding and transfer due to high rigidity of their molecular structure and compact spatial packing of the globule.There are data on the expression of metal-binding sites in proteins of γ-globulin fraction, on the presence of bound copper in these biomacromolecules, and realization of some intermolecular interactions involving γ-globulins and IgG through copper cation exchange [2,3,14,15].Our findings indicate that γ-globulins can expose carbohydrate-rich components of the molecule and unfold them into extramolecular space [3]. Polysaccharide (polyanion) chains in this form can effectively bind metal, thus regulating its content in cell microenvironment.…”

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confidence: 99%

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Biphasic Interaction of γ-Globulin with Copper Cations

2005

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Interactions of human serum gamma-globulin with copper cations in solution were studied by differential ultraviolet spectrophotometry. Copper in supraphysiological concentrations increases optical density of protein solution, reflecting the effect of gamma-globulin saturation with metal. In physiological and lower concentrations of copper cations we observed hypochromia in the protein absorption spectrum. Conformational changes in g-globulin molecule during interactions with copper by the surface and intramolecular binding sites and possible role of bivalent metal cations in the maintenance of certain conformations of immunoactive serum proteins are discussed.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Biphasic Interaction of γ-Globulin with Copper Cations

2005

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“…Carbohydrate component (CC) is associated with y-globulin molecule via metal ions of alternating valency [1]. These cations interact with specific sites of y-globulin molecule [ 13,14] and stimulate aggregation by forming bridges between protein molecules at a certain metal/IgG ratio. A positive correlation between IgG affinity to transition metal and the effect of protein on spontaneous LBT was found [2].…”

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confidence: 99%

Regulation ofin vitro human lymphocyte blast transformation associated with γ-globulin fraction containing a carbohydrate component

Чекнев

1999

Bull Exp Biol Med

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Carbohydrate-enriched components were isolated from human serum y-globulin by chelation of associated transition metals. Similar to the initial y-globulin preparation, these components stimulate in vitro blast transformation of human lymphocytes from healthy donors and inhibit subsequent phytomitogen-induced lymphocyte blast transformation. Key words: y-globulin; carbohydrate component, lymphocyte blast transformationThe ability of y-globulin to maintain a definite level of human lymphocyte blast transformation (LBT) in vitro [3] is known to depend on the expression of Fc Yreceptors in cell membrane [8,12]. The effect of LBT stimulation was shown to correlate with the presence of protein aggregates in the y-globulin preparation [3].The effector functions of y-globulin also depend on the presence of carbohydrate-containing fraction bound to polypeptide chains via non-covalent bonds [1]. Carbohydrate component (CC) is associated with y-globulin molecule via metal ions of alternating valency [1]. These cations interact with specific sites of y-globulin molecule [ 13,14] and stimulate aggregation by forming bridges between protein molecules at a certain metal/IgG ratio. A positive correlation between IgG affinity to transition metal and the effect of protein on spontaneous LBT was found [2].y-Globulin aggregation is accompanied by significant changes in its conformation stability and enhances the release or exposure of components not bound covalently to polypeptide chains. MATERIALS AND METHODSMononuclear cells (MNC) were isolated from peripheral venous blood of 4 healthy men aged 20-46. The cells were separated in Ficoll-Verografin (d = 1.077 g/cm 3) one-step density gradient and MNC were harvested from the interface layer. After repeated washout with medium 199 MNC were resuspended in complete nutrient medium (CNM) consisting of RPMI-1640 (Flow) supplemented with 12% fetal calf serum (Hamaleya Institute of Epidemiology and Microbiology), 2 mM glutamine and 40 ~tg/ml gentamicin (Pharmachim) to a concentration of 2• cells/ml. To initiate spontaneous LBT, 0.1 ml MNC suspension was applied to round-bottom 96-well plates, 0.1 ml CNM and 10 ~tCi/ ml 3H-thymidine were added to each well and the plates were incubated for 18 h at 37~ in humidified atmosphere containing 5% CO 2. LBT was induced by 2 ~tg/ml phytohemagglutinin M (PHA, Serva) or 1 ~tg/ml con-0007 -4888/99/0006-0610522.00 9

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“…Published data show that molecules of heparin [5], lectins [3], integrins [4], and γ-globulin contain bound metals [3]. Metal-binding sites are formed in native and aggregated IgG [4,[10][11][12]. Conformational and functional reconstruction of biological macromolecules is determined by binding or donating of cations.…”

Section: Resultsmentioning

confidence: 99%

Activity of human lymphocytes in the presence of carbohydrate-containing compounds

Чекнев

Babaeva

2004

Bull Exp Biol Med

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Treatment with chelating agent abolished stimulation of human lymphocyte blast transformation observed in the presence of native microbial glycoproteins. Heparin passed through a column packed with aluminum hydroxide inhibited cytotoxic activity in natural killer cells. We discuss the possibility of regulation of cell functions via modulation of the vector of transport and exchange of metal cations in cell microenvironment and the role of macromolecular compounds containing carbohydrate components in this process.

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Antibody constant region: Potential to bind metal and nucleic acid

Cited by 10 publications

References 48 publications

Biphasic Interaction of γ-Globulin with Copper Cations

Biphasic Interaction of γ-Globulin with Copper Cations

Regulation ofin vitro human lymphocyte blast transformation associated with γ-globulin fraction containing a carbohydrate component

Activity of human lymphocytes in the presence of carbohydrate-containing compounds

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