Scholarlink

<p>Arsenic occurs extensively in the environment and is classified as a potent carcinogenic substance in humans. Prolonged intake of water contaminated with arsenic results in the development of arsenicosis. In the present study, a toxicoproteomic approach was employed to elucidate arsenic-induced alterations in lens proteins using a fish model. Juveniles of <i>Labeo rohita</i> were exposed to sodium meta-arsenite (NaAsO<sub>2</sub>) at concentrations of 5, 10, 15, and 20&#xa0;ppm for a period of 10&#xa0;days in triplicate experimental groups. Soluble lens proteins were analyzed using one- and two-dimensional gel electrophoresis, immunoblotting of αA-crystallin and MALDI-TOF mass spectrometry. Cataract development was observed at arsenic concentrations ≥ 15&#xa0;ppm. Proteomic analyses revealed concentration-dependent alterations in lens protein abundance, including significant reductions in βB1, βB2, and βA2b-crystallin, small heat shock protein and skeletal α-actin (<i>p</i> &lt; 0.05). In addition, αA, βA2, and βA2a-crystallin exhibited reduced abundance trends, although these changes were not statistically significant. Two-dimensional immunoblotting revealed 15 distinct αA-crystallin isoforms in control lenses, several of which showed a progressive decrease with increasing arsenic exposure, culminating in complete degradation at 20&#xa0;ppm. These findings demonstrate that arsenic exposure is associated with substantial alterations in lens crystallins and other proteins involved in structural organization and protein homeostasis, coinciding with cataract development at higher exposure concentrations. The identified proteins may serve as potential toxicoproteomic biomarkers of lens damage in aquatic organisms and provide a foundation for future studies investigating the molecular mechanisms of arsenic-induced lens toxicity.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Toxicoproteomic analysis reveals arsenic-induced alterations in eye lens proteins of Labeo rohita

  • 期刊论文

  • 发表日期：

    2026年8月3日

查看全文
  • Soma Bhattacharjee,
  • Manoj Kumar Pati,
  • Kampan Bisai,
  • Bimal Prasanna Mohanty

摘要

Arsenic occurs extensively in the environment and is classified as a potent carcinogenic substance in humans. Prolonged intake of water contaminated with arsenic results in the development of arsenicosis. In the present study, a toxicoproteomic approach was employed to elucidate arsenic-induced alterations in lens proteins using a fish model. Juveniles of Labeo rohita were exposed to sodium meta-arsenite (NaAsO2) at concentrations of 5, 10, 15, and 20 ppm for a period of 10 days in triplicate experimental groups. Soluble lens proteins were analyzed using one- and two-dimensional gel electrophoresis, immunoblotting of αA-crystallin and MALDI-TOF mass spectrometry. Cataract development was observed at arsenic concentrations ≥ 15 ppm. Proteomic analyses revealed concentration-dependent alterations in lens protein abundance, including significant reductions in βB1, βB2, and βA2b-crystallin, small heat shock protein and skeletal α-actin (p < 0.05). In addition, αA, βA2, and βA2a-crystallin exhibited reduced abundance trends, although these changes were not statistically significant. Two-dimensional immunoblotting revealed 15 distinct αA-crystallin isoforms in control lenses, several of which showed a progressive decrease with increasing arsenic exposure, culminating in complete degradation at 20 ppm. These findings demonstrate that arsenic exposure is associated with substantial alterations in lens crystallins and other proteins involved in structural organization and protein homeostasis, coinciding with cataract development at higher exposure concentrations. The identified proteins may serve as potential toxicoproteomic biomarkers of lens damage in aquatic organisms and provide a foundation for future studies investigating the molecular mechanisms of arsenic-induced lens toxicity.