Rola albuminy w diagnostyce. Wiązanie jonów i kompleksów metali

• Autorzy: Trynda-Lemiesz L. , Wiglusz K. , Mucha I.

Warianty tytułu

EN

The role of albumin in the diagnostics. Binding of ions and metal complexes

• Języki publikacji: PL

Abstrakty

EN

Human serum albumin (HSA), the most prominent protein in plasma, binds different classes of ligands at multiple sites. HSA provides a depot for many compounds, affects pharmacokinetics of many drugs, holds some ligands in a strained orientation providing their metabolic modification, renders potential toxins harmless transporting them to disposal sites, accounts for most of the antioxidant capacity of human serum, and acts as a NO-carrier. Transport of metal ions is another prominent function of HSA. Metal ions carried by HSA include physiological Ca2+, Zn2+, Co2+ and Cu2+, toxic Cd2+ and Ni2+, and drug-derived Au+ and Pt2+. This broad specificity is due to the presence of distinct binding sites on HSA surface. The N-terminal binding site (in brief NTS, alternatively labeled as ATCUN motif) was the earliest to be identified. It is composed of the first three amino-acid residues of the HSA sequence, Asp-Ala-His. Another specific binding site for metal ions in HSA is located at the interface of domains I and II of the protein molecule. This site, labeled multimetal binding site (MBS), the coordination of metal ions at MBS is provided by His67, His247, Asn99 and Asp249. Cys34 provides the sole thiol group of HSA which is not engaged in intramolecular disulfide bridges. The Cys34 side chain is located at the bottom of a crevice, what results in a limited accessibility and elevated specificity in metal ion interactions. Cys34 was proposed to be the major site of Pt2+ and Au+ complexes interaction. HSA had been indicated to be a physiological carrier of Co2+ ions a long time ago. The interest in the binding of Co(II) ions to HSA has surged recently due to a proposal by Bar-Or et al. [1] of a new rapid clinical assay for myocardial ischemia. This assay (ACB test) is based on an interaction of Co(II) ions with HSA derived from blood serum, followed by DTT treatment. This test is based on an assumption that the clipping of two first residues of HSA is related to ischemia. The proposed molecular mechanism for this test is based on a further assumption of NTS is the primary binding site for Co2+ ions. However, several questions regarding the ACB test are still open, and the molecular mechanism is not clear. Recent studies strongly suggest that the primary binding sites of Co(II) are sites A and B and not the N-terminus. In the field of MR imaging, there is a considerable interest in contrast agents that target serum albumin because they are retained in the vascular space for longer periods of time than low molecular weight MR agents and also have an enhanced water relaxivity due to slower rotation when bound to the large protein. Albumin in this case serves two purposes, to enhance the sensitivity of the contrast agent by slowing its rotation and to slow diffusion of the agent from blood vessels into the spaces between cells. Both features are useful for imaging of blood vessels (MR angiography). Simple aliphatic chains are sufficient to facilitate binding to HSA. A derivative of Gd-DOTMP bearing an 11-carbon chain, was found to bind at a minimum of five fatty acid binding sites on HSA molecule.

Słowa kluczowe

PL

albumina ludzka; wiązanie metali przez albuminę; markery biochemiczne; albumina modyfikowana niedokrwieniem

EN

human albumin; albumin metal binding; biochemical markers; ischemia modified albumin

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Wiadomości Chemiczne
• Rocznik: 2010
• Tom: [Z] 64, 1-2
• Strony: 81--104
• Opis fizyczny: bibliogr. 65 poz., wykr.

Twórcy

autor

Trynda-Lemiesz L.

autor

Wiglusz K.

autor

Mucha I.

• Akademia Medyczna im. Piastów Śląskich, Katedra i Zakład Chemii Analitycznej ul. Szewska 38, 50-139 Wrocław,

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