Electron spin resonance study of the copper(II) complexes of human and dog serum albumins and some peptide analogs

Rakhit, Gopa; Sarkar, Bibudhendra

doi:10.1016/s0162-0134(00)80158-0

Cited by 36 publications

(28 citation statements)

References 20 publications

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“…6A). Similar EPR signals from Cu(II)-albumin have been described previously as the complex of Cu(II) ion coordinated to four in-plane nitrogen atoms, one of which is the imidazole group of histidine (17). The spectra recorded at room temperature (298 K) and at liquid-nitrogen temperature (77 K) were similar, but they had slightly different paramagnetic parameters: g II ϭ 2.173, A II ϭ 17.5 mT at 298 K, and g II ϭ 2.193, A II ϭ 19.2 mT at 77 K, respectively (Fig.…”

Section: Effects Of Free Fatty Acids On Copper Binding/redox Activitysupporting

confidence: 77%

“…These changes may be related to the occupancy of the second Cu-binding site on albumin. Indeed, earlier work has indicated that bovine serum albumin has two distinct Cu-binding sites (differing in the affinity for Cu), which are represented by two different signals in the EPR spectrum (17). Similarly, hSA also has high-affinity and low-affinity binding sites; the EPR signal of the latter becomes detectable only when the Cu/albumin ratio exceeds 1/1.…”

Section: Effects Of Free Fatty Acids On Copper Binding/redox Activitymentioning

confidence: 98%

“…Conditions for analysis are those described by Rakit and Sarkar (17) with the exception that measurements were made at room temperature because we have established that low-temperature EPR is not required for resolution of these signals (g II ϭ 2.173, A II ϭ 17.5 mT at room temperature compared to g II ϭ 2.193, A II ϭ 19.2 under liquid nitrogen). The spectra of Cu(II)/albumin were recorded as follows: 315 mT, center field; 10 mW, power; 150 mT, sweep width; 9.078 GHz, frequency; 4 min, sweep time.…”

Section: Epr Measurements Of the Cu(ii)/albumin Complexesmentioning

confidence: 99%

See 2 more Smart Citations

Mishandling of Copper by Albumin: Role in Redox-Cycling and Oxidative Stress in Preeclampsia Plasma

Kagan

Tyurin

Borisenko

et al. 2001

Hypertension in Pregnancy

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Section: Effects Of Free Fatty Acids On Copper Binding/redox Activitysupporting

confidence: 77%

Section: Effects Of Free Fatty Acids On Copper Binding/redox Activitymentioning

confidence: 98%

Section: Epr Measurements Of the Cu(ii)/albumin Complexesmentioning

confidence: 99%

See 1 more Smart Citation

Mishandling of Copper by Albumin: Role in Redox-Cycling and Oxidative Stress in Preeclampsia Plasma

Kagan

Tyurin

Borisenko

et al. 2001

Hypertension in Pregnancy

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“…The EPR spectra of Cu II -Ab40 and Cu-HSA are quite different [20,[53][54][55] (Figure 1 be followed by the appearance of a negative peak at 3445 Gauss ( Figure 1) present in Cu II -HSA but not in Cu-Ab40. The development of this peak increased steadily in intensity up to the addition of one equivalent of HSA, where a plateau is reached (Figure 1, inset).…”

Section: Cumentioning

confidence: 97%

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

Perrone¹,

Mothes²,

Vignes³

et al. 2009

ChemBioChem

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Amyloid-beta peptides (Abeta) and the protein human serum albumin (HSA) interact in vivo. They are both localised in the blood plasma and in the cerebrospinal fluid. Among other functions, HSA is involved in the transport of the essential metal copper. Complexes between Abeta and copper ions have been proposed to be an aberrant interaction implicated in the development of Alzheimer's disease, where Cu is involved in Abeta aggregation and production of reactive oxygen species (ROS). In the present work, we studied copper-exchange reaction between Abeta and HSA or the tetrapeptide DAHK (N-terminal Cu-binding domain of HSA) and the consequence of this exchange on Abeta-induced ROS production and cell toxicity. The following results were obtained: 1) HSA and DAHK removed Cu(II) from Abeta rapidly and stoichiometrically, 2) HSA and DAHK were able to decrease Cu-induced aggregation of Abeta, 3) HSA and DAHK suppressed the catalytic HO(.) production in vitro and ROS production in neuroblastoma cells generated by Cu-Abeta and ascorbate, 4) HSA and DAHK were able to rescue these cells from the toxicity of Cu-Abeta with ascorbate, 5) DAHK was more potent in ROS suppression and restoration of neuroblastoma cell viability than HSA, in correlation with an easier reduction of Cu(II)-HSA than Cu-DAHK by ascorbate, in vitro. Our data suggest that HSA is able to decrease aberrant Cu(II)-Abeta interaction. The repercussion of the competition between HSA and Abeta to bind Cu in the blood and brain and its relation to Alzheimer's disease are discussed.

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“…In the albumin from dog and swine, the His residue at the third position is replaced by Tyr [11][12][13]. The replacement of His by Tyr resulted in a low affinity of Cu(II) by the model peptide study.…”

Section: Introductionmentioning

confidence: 99%

Transport of Cu(II) from an albumin mimic peptide, GlyGlyHisGly, to histidine and penicillamine

Hanaki¹,

Odani

2007

Journal of Inorganic Biochemistry

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Electron spin resonance study of the copper(II) complexes of human and dog serum albumins and some peptide analogs

Cited by 36 publications

References 20 publications

Mishandling of Copper by Albumin: Role in Redox-Cycling and Oxidative Stress in Preeclampsia Plasma

Mishandling of Copper by Albumin: Role in Redox-Cycling and Oxidative Stress in Preeclampsia Plasma

Copper Transfer from Cu–Aβ to Human Serum Albumin Inhibits Aggregation, Radical Production and Reduces Aβ Toxicity

Transport of Cu(II) from an albumin mimic peptide, GlyGlyHisGly, to histidine and penicillamine

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