Specific immuno‐extraction followed by enzymatic detection (SIEFED) of myeloperoxidase and mitochondrial complex I in muscular microbiopsies: preliminary results in endurance horses

Franck, Thierry; Votion, Dominique; Ceusters, Justine; Pouyade, Geoffroy de la Rebière de; Mouithys‐Mickalad, Ange; Niesten, Ariane; Fraipont, Audrey; Erck, Emmanuelle Van; Goachet, A. G.; Robert, Céline; Serteyn, Didier

doi:10.1111/j.2042-3306.2010.00270.x

Cited by 9 publications

(7 citation statements)

References 37 publications

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“…; Franck et al. ) and is then cleaved in the 64‐kDa active subunit of the enzyme. Four other bands below the 30 kDa limit that had never been described before and not found in purified MPO were also observed in these samples.…”

Section: Discussionmentioning

confidence: 99%

“…The overall low MPO activity observed in raw supernatant assays was partly explained by Western blot analyses showing large presence of inactive MPO precursor. Unlike in the human (Klebanoff 2005), the enzyme precursor (86 kDa) is inactive in the equine (Serteyn et al 2003;Franck et al 2010) and is then cleaved in the 64-kDa active subunit of the enzyme. Four other bands below the 30 kDa limit that had never been described before and not found in purified MPO were also observed in these samples.…”

Section: Discussionmentioning

confidence: 99%

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Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

Ponthier

Franck

Parrilla-Hernandez

et al. 2014

Reprod Domestic Animals

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Myeloperoxidase (MPO) is a pro-oxidant enzyme associated with decreased motility in thawed equine semen. This study aimed to describe MPO concentration, activity and subunits in raw and thawed semen and to correlate these data with motilities in raw and thawed semen. Semen samples from five stallions were collected four times. Motilities were assessed in raw and thawed semen. MPO assays were performed in raw seminal plasma, raw sperm-rich pellet and thawed semen. Total and active MPO concentrations were, respectively, assayed by enzyme-linked immunosorbent assay and specific immunological extraction followed by enzymatic detection. MPO subunits present in semen were characterized by Western blot. Purified active MPO was added in saline solution and freezing extender to control its activity during freezing procedure. Differences between medians were determined using Kruskal-Wallis test, and correlations were determined using Spearman's test for nonparametric data. Active MPO concentration was low in seminal plasma and thawed semen, but high in pellet (p = 0.0058), as the opposite relation was observed for total MPO concentration (p < 0.0001). In seminal plasma and post-thaw semen, inactive 86-kDa MPO precursor was mainly observed. Purified MPO activity was decreased in the extender (p = 0.0286). MPO activity in pellet was highly correlated with thawed progressive motility (r = -0.5576, p = 0.0086). Inactive MPO precursor and unknown low molecular weight inactive MPO precursor subunits explain low MPO activity in semen. Major MPO activity was observed in pellet, and post-thaw loss of activity is partially explained by MPO inactivation in extender. Thawed semen motility was negatively correlated with MPO activity in pellet, becoming a potential freezability predictor.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

Ponthier

Franck

Parrilla-Hernandez

et al. 2014

Reprod Domestic Animals

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“…One group produced 3 different studies in Arabian endurance horses using a minimally traumatic muscle ‘microbiopsy’ technique, which allowed collection of enough tissue to evaluate cellular functions in exercised muscle without requiring skin closure or inhibiting further exercise (Franck et al . 2010; Serteyn et al .…”

Section: Muscle Physiology and Biochemistry In Exercisementioning

confidence: 99%

“…Collectively, these studies examined mitochondrial respiratory function (Votion et al . 2010), established normal values for activities of myeloperoxidase and mitochondrial complex 1 in equine muscle tissue (Franck et al . 2010) and also measured neutrophil marker enzymes (myeloperoxidase and elastase) in the blood and muscle of exercised endurance horses to determine their role in exercise‐associated muscle damage (Serteyn et al .…”

Section: Muscle Physiology and Biochemistry In Exercisementioning

confidence: 99%

Muscle physiology and nutrition in exercising horses

McKenzie

2011

Equine Veterinary Journal

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“…This underlines the major role of neutrophil activation [13][14][15][16]. The hypothesis of an involvement of neutrophil-mediated mitochondrial dysfunction was previously observed in muscle micro-biopsies from horses after strenuous exercise [17]. Moreover, in cultured muscle cell lines, it was demonstrated that the potent neutrophil-derived oxidative enzyme myeloperoxidase could enter the cell and disturb the electron transfer system resulting in altered ATP production [18].…”

Section: Introductionmentioning

confidence: 99%

Muscle Mitochondrial Dysfunction in Horses Affected by Acute Laminitis

et al. 2014

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Laminitis is a common and debilitating disease affecting horses and ponies. It often leads to the demise of the animal. Energy deficiency is suspected to entrain the disruption of the hemidesmosomes leading to the failure of the dermal-epidermal interface. The aim of this study was to measure the muscle mitochondrial function by high resolution respirometry. Muscle micro-biopsies were obtained from 11 horses affected by acute metabolic laminitis, 6 horses affected by acute laminitis resulting from a systemic inflammation response syndrome and 28 healthy horses distributed in 2 control groups: 17 horses with a body condition score [BSC, ranging from 0 (emaciated) to 5 (obese)] of 2 to 3 and 11 horses with a BSC of 4 to 5. During the acute phase of laminitis, a significant reduction of the muscle mitochondrial respiration was observed. The muscle mitochondrial dysfunction occurred independently of the etiology (metabolic disorder or systemic inflammation) leading to laminitis. The reduction of the oxidative phosphorylation and of the maximal respiratory capacity (after uncoupling) may induce depletion of the cell's ATP content. If the same mitochondrial alteration occurs in the foot lamina, mitochondria targeting should be considered for the future, not only to better understand the physiopathology of the disease but also to maintain and to support the mitochondrial function before reaching the « mitochondrial dysfunction threshold » that may lead to the failure of the dermal-epidermal interface.

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Specific immuno‐extraction followed by enzymatic detection (SIEFED) of myeloperoxidase and mitochondrial complex I in muscular microbiopsies: preliminary results in endurance horses

Cited by 9 publications

References 37 publications

Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

Muscle physiology and nutrition in exercising horses

Muscle Mitochondrial Dysfunction in Horses Affected by Acute Laminitis

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