Hemoglobin components from trout (Salmo irideus): determination of their peroxidative activity

Fedeli, Donatella; Tiano, Luca; Gabbianelli, Rosita; Caulini, G; Woźniak, Michał; Falcioni, Giancarlo

doi:10.1016/s1096-4959(01)00471-7

Cited by 15 publications

(12 citation statements)

References 16 publications

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“…The inability to produce heme degradation products by met‐Hb with H 2 O 2 , was explained by the reaction of oxoferrylHb with H 2 O 2 with the production of met‐Hb and oxygen instead of superoxide anion [8]. Our data performed, at pH 5.4, in the presence of H 2 O 2 and guaiacol (as reductant) indicate a larger peroxidase activity of HbIV, with respect to HbI, in line with a previous work [5]. However, these results show a decrease of the peroxidase activity in the order: iron(II)‐HbIV > met‐HbIV > met‐HbI > iron(II)‐HbI.…”

Section: Discussionsupporting

confidence: 92%

“…Trout HbIV and HbI are also characterized by different peroxidative activities [4,5], which are dependent from the pH of the medium and/or the iron oxidation state. In fact, it is known that the hemoglobin molecules present peroxidative properties [5–7], which may be important for the life span of red blood cells (RBCs), continuously exposed to extracellular and intracellular sources of reactive oxygen species (ROS), which are a potential cause of oxidative injury and could have a role in erythrocytes senescence [7].…”

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confidence: 99%

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Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs

Gabbianelli¹,

Zolese²,

Bertoli³

et al. 2004

European Journal of Biochemistry

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Circular dichroism (CD) spectra of two major hemoglobin components (Hb), HbI and HbIV, from Oncorhyncus mykiss (formerly Salmo irideus) trout were evaluated in the range 250-600 nm. HbI is characterized by a complete insensitivity to pH changes, while HbIV presents the Root effect. Both reduced [iron(II) or oxy] and oxidized (met) forms of the two proteins were studied at different pHs, 7.8 and 6.0, to obtain information about the pH effects on the structural features of these hemoglobins. Data obtained show that oxy and met-HbI are almost insensitive to pH decrease, remaining in the R conformational state also at low pH. On the contrary, the pH decrease induces similar structural changes, characteristics of ligand dissociation and R fi T transition, both in the reduced and in the oxidized HbIV. The structural changes, monitored by CD, are compared with the peroxidative activity of iron(II)-Hb and met-Hb forms and with the superoxide anion scavenger capacity of the proteins.

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Section: Discussionsupporting

confidence: 92%

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confidence: 99%

Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs

Gabbianelli¹,

Zolese²,

Bertoli³

et al. 2004

European Journal of Biochemistry

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“…Trout IV Hb autooxidized more rapidly compared to trout I Hb at pH 7 and 30 ëC (Fedeli et al, 2001). Trout IV also autooxidized more rapidly compared to trout I at pH 6.3 and 2 ëC (Richards et al, 2005).…”

Section: Autooxidation Of Different Hbsmentioning

confidence: 86%

Heme proteins and oxidation in fresh and processed meats

Richards

2010

Oxidation in Foods and Beverages and Antioxidant Applications

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“…This could explain the stimulation of angiogenesis, a response that is often linked to regional hypoxia (Maxwell and Ratcliffe, 2002). While there is no evidence that mitochondrial gene expression is directly sensitive to oxygen levels, erythrocytes have important antioxidant roles and may be an important element of peripheral antioxidant defense by metabolizing ROS (Gabbianelli et al, 1998;Aoshiba et al, 1999;Fedeli et al, 2001). While the antioxidant capacities of erythrocytes do not deteriorate with cell age (e.g.…”

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Muscle remodeling in relation to blood supply: implications for seasonal changes in mitochondrial enzymes

McClelland

Dalziel

Fragoso

et al. 2005

Journal of Experimental Biology

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SUMMARY We investigated if seasonal changes in rainbow trout muscle energetics arise in response to seasonal changes in erythrocyte properties. We assessed if skeletal muscle mitochondrial enzymes changed (1) acutely in response to changes in erythrocyte abundance, or (2) seasonally when we altered the age profile of erythrocytes. Rainbow trout were treated with pheynylhydrazine,causing a 75% reduction in hematocrit within 4 days. After erythropoiesis had returned hematocrit to normal, treated and control fish were subjected to a seasonal cold acclimation regime to assess the impact of erythrocyte age on skeletal muscle remodeling. Anemia (i.e. phenylhydrazine treatment) did not alter the specific activities (U g-1 tissue) of mitochondrial enzymes in white or red muscle. Anemic pretreatment did not alter the normal pattern of cold-induced mitochondrial proliferation in skeletal muscle,suggesting erythrocyte age was not an important influence on seasonal remodeling of muscle. Anemia and cold acclimation both induced a 25–30%increase in relative ventricular mass. The increase in relative ventricular mass with phenylhydrazine treatment was accompanied by a 35% increase in DNA content (mg DNA per ventricle), suggesting an increase in number of cells. In contrast, the increase in ventricular mass with cold temperature acclimation occurred without a change in DNA content (mg DNA per ventricle), suggesting an increase in cell size. Despite the major increases in relative ventricular mass, neither anemia nor seasonal acclimation had a major influence on the specific activities of a suite of mitochondrial enzymes in heart. Collectively, these studies argue against a role for erythrocyte dynamics in seasonal adaptive remodeling of skeletal muscle energetics.

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Hemoglobin components from trout (Salmo irideus): determination of their peroxidative activity

Cited by 15 publications

References 16 publications

Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs

Correlation between functional and structural changes of reduced and oxidized trout hemoglobins I and IV at different pHs

Heme proteins and oxidation in fresh and processed meats

Muscle remodeling in relation to blood supply: implications for seasonal changes in mitochondrial enzymes

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