Extracellular glutathione peroxidase and ascorbic acid in aqueous humor and serum of patients operated on for cataract

Huang, Wuqing; Koralewska-Makár, Anna; Bauer, Birgitta; Åkesson, Björn

doi:10.1016/s0009-8981(97)06520-0

Cited by 35 publications

(22 citation statements)

References 39 publications

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“…The glutathione peroxidase family has at least four member enzymes, but little is known about their physiological function. Extracellular glutathione peroxidase is the predominant form in plasma and is mainly produced in the kidney (Avissar et al, 1989;Huang & A Ê kesson, 1993;Avissar et al, 1994;Huang, 1996), and it is also found in milk (Avissar et al, 1991) and aqueous humor (Huang et al, 1997). It is also the major 75 Se-substituted protein secreted by human thyrocytes incubated with ( 75 Se)selenite, and it was hypothesized that it may be a regulator of thyroid hormone synthesis (Howie et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

et al. 1998

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Objective: To study the relationships between ®sh intake and different markers of selenium status and thyroid hormone function. Design: Cross-sectional study. Setting and subjects: Sixty-eight men (age 24±79 years) were recruited among coastal ®shermen and inland subjects from Latvia. None of the subjects was on selenium medication or had any known endocrine disease. Main outcome measures: Correlations between ®sh intake, plasma levels of selenium, selenoprotein P, glutathione peroxidase, organic mercury in erythrocytes and TSH in serum. Results: Selenium in plasma ranged from 0.30 to 1.56 mmola1, selenoprotein P from 0.54 to 2.21 arbitrary units relative to pooled plasma, and glutathione peroxidase from 1.20 to 5.73 mga1. The number of ®sh meals per month was correlated with plasma selenium, selenoprotein P and glutathione peroxidase (r 0.63, r 0.62 and r 0.50, respectively; P`0.001). Plasma selenium was correlated with selenoprotein P and glutathione peroxidase (r 0.88 and r 0.67, respectively; P`0.001), and also selenoprotein P and glutathione peroxidase were correlated (r 0.63, P`0.001). The mean plasma selenium level in those with a high ®sh intake (21±50 ®sh mealsamonth), was 81% higher than in those with lowest ®sh intake. TSH in serum was inversely correlated with plasma selenium and selenoprotein P. Thyroid hormone levels were not correlated with plasma selenium, selenoproteins or ®sh intake. Conclusions: In this study group, selenium from ®sh intake had a marked impact on all variables studied on selenium status. No impact of selenium status on T3 and T4 levels was observed. The slightly negative correlation of selenium status with TSH levels might indicate a higher TSH secretion at low selenium status.

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Section: Discussionmentioning

confidence: 99%

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

et al. 1998

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“…For example, though the exact role of Glutathione Peroxidase in the AH is unclear, it is known to protect cells and other proteins from oxidative damage and most likely serves a similar function in the AH [32]. Prostaglandin-H2 D-isomerase is thought to be involved in maintenance of intraocular pressure as well as development and maintenance of the blood-aqueous barrier [33].…”

Section: Discussionmentioning

confidence: 99%

Multidimensional Protein Identification Technology

Berri-Trapero¹,

Villar-Moreno²

2006

Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine

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Aqueous humor (AH) supports avascular tissues in the anterior segment of the eye, maintains intraocular pressure, and potentially influences the pathogenesis of ocular diseases. Nevertheless, the AH proteome is still poorly defined despite several previous efforts, which were hindered by interfering high abundance proteins, inadequate animal models, and limited proteomic technologies. To facilitate future investigations into AH function, the AH proteome was extensively characterized using an advanced proteomic approach. Samples from patients undergoing cataract surgery were pooled and depleted of interfering abundant proteins and thereby divided into two fractions: albumin-bound and albumin-depleted. Multidimensional Protein Identification Technology (MudPIT) was utilized for each fraction; this incorporates strong cation exchange chromatography to reduce sample complexity before reversed-phase liquid chromatography and tandem mass spectrometric analysis. Twelve proteins had multi-peptide, high confidence identifications in the albumin-bound fraction and 50 proteins had multi-peptide, high confidence identifications in the albumin-depleted fraction. Gene ontological analyses were performed to determine which cellular components and functions were enriched. Many proteins were previously identified in the AH and for several their potential role in the AH has been investigated; however, the majority of identified proteins were novel and only speculative roles can be suggested. The AH was abundant in antioxidant and immunoregulatory proteins as well as anti-angiogenic proteins, which may be involved in maintaining the avascular tissues. This is the first known report to extensively characterize and describe the human AH proteome and lays the foundation for future work regarding its function in homeostatic and pathologic states.The aqueous humor (AH) is a clear fluid that fills the anterior segment of the eye and bathes the lens, iris, and corneal endothelium [1]. It is secreted by the ciliary body and functions to provide nutrients and remove waste from avascular tissues [2], as well as create the intraocular pressure that maintains the convex shape of the cornea. The AH has antioxidant properties and purported immune response roles during inflammation and infection [3,4]. However, the proteins that are responsible for carrying out these functions are largely unknown. The protein content of the AH has been studied extensively [5][6][7][8][9][10][11][12]; however, due to limitations in technology, an extensive and definitive description of human AH proteins has yet to be provided. Furthermore, proteins in the AH are thought to be involved in development of several eye diseases [13,14], and investigating the AH proteome will facilitate generation of new hypotheses regarding the etiology of such pathologies. Thus our goal in this study was to investigate the AH proteome and determine its protein constituents with high confidence using an advanced proteomic approach.

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“…Ензим глутатуон пероксидаза или мРНК за синтезу овог ензима је доказана у многим органима хуманог организма: бубрезима, плућима, плаценти, тироидној жлезди, а главни извор овог ензима у хуманој плазми су бубрези (108). Такође, мРНК за синтезу глутатуон пероксидазе је детектована у хуманом цилијарном епителу одакле се секретује у очну водицу (148).…”

Section: глутатион пероксидазаunclassified

“…Сличне податке о активности глутатион пероксидазе у плазми пацијената оболелих од сенилне катаракте објавили су и други истраживачи. Наиме, Huang и сарадници (108) су објавили да је код испитаника са нуклеарном, кортикалном, субкапсуларном и мешовитом катарактом активност глутатион пероксидазе у плазми слична.…”

Section: активност антиоксидационих ензима у плазми пацијената са сенunclassified

“…Наиме, глутатион пероксидаза има кључну улогу у разградњи водоник пероксида и детоксикацији липидних хидропероксида и у условима смањене активности поменуте пероксидазе повећава се концентрација продуката пероксидације липида у плазми (108). Ензим глутатион пероксидаза или мРНК за његову синтезу, пронађени су у многим ткивима хуманог организма, као што су бубрези, плућа, тироидеа, плазма, а претпоставља се, да су бубрези главни извор глутатион пероксидазе у плазми код човека.…”

Section: активност антиоксидационих ензима у плазми пацијената са сенunclassified

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Oxidative stress and antioxidant defense elements in the genesis of cataracts

Kisić¹

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Introduction. The immediate cause for the occurrence of cataract is unknown, but oxidative damage and effects of reactive oxygen species are considered important in its etiopathogenesis. Aim. The study was aimed at testing the products oxidative stress and antioxidant protection factors in serum and corticonuclear lenses blocks of patients with different types and different degrees of maturity of agerelated cataract. Material and Methods. Patients. Clinical and biochemical researches were carried out in 101 patients with age-related cataract, 46 women and 55 men. The average age of the group was 72.5 (SD ± 7.98). According to the cataract maturity degree the patients were classified into two groups as follows: cataract senilis incipiens (N=41) and cataract senilis matura (N=60). Serum samples and corticonuclear lenses blocks were obtained to detect the products of lipid peroxidation: conjugated diene, fluorescent lipid peroxidation products and malondialdehyde and activities antioxidative enzymes: superoxide dismutase, catalase, glutathione peroxidase, glutathione reductase and glutathione S-transferase. Results. Significantly higher concentration of diene conjugation in corticonuclear lenses blocks was measured in the patients with cataract senilis incipiens (p<0.001) as well as the intensity of fluorescent iminopropens (p<0.001). Significantly higher concentration of malondialdehyde in corticonuclear lenses blocks (p<0.001) was measured in the patients with cataracta senilis matura. Conclusion. Based on the found lipid peroxidation products measuring results in corticonuclear lenses blocks in the patients with cataract diagnosis, it can be concluded that the lens structure changes caused by lipid peroxidation can, with other risk factors present, influence occurrence and development of cataract. Some cataract types show different lipid peroxidation intensity with the most distinct changes in the cataract wich started as nuclear. Кључне речиОксидациони стрес, катаракта, липидна пероксидација, антиоксидантни ензими.

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Extracellular glutathione peroxidase and ascorbic acid in aqueous humor and serum of patients operated on for cataract

Cited by 35 publications

References 39 publications

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

Plasma levels of selenium, selenoprotein P and glutathione peroxidase and their correlations to fish intake and serum levels of thyrotropin and thyroid hormones: A study on Latvian fish consumers

Multidimensional Protein Identification Technology

Oxidative stress and antioxidant defense elements in the genesis of cataracts

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