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

Soma Bhattacharjee; Manoj Kumar Pati; Kampan Bisai; Bimal Prasanna Mohanty

doi:10.1007/s10695-026-01762-5

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

Soma Bhattacharjee·Manoj Kumar Pati·Kampan Bisai·Bimal Prasanna Mohanty

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Abstract

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.

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Animals Lens, Crystalline Water Pollutants, Chemical Proteomics Crystallins Cyprinidae Arsenic Fish Proteins Arsenites Sodium Compounds Electrophoresis, Gel, Two-Dimensional Cataract Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization 2D gel electrophoresis Arsenic toxicity Lens crystallins MALDI-TOF MS Toxicoproteomics Journal Article

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Soma Bhattacharjee, Manoj Kumar Pati, Kampan Bisai, Bimal Prasanna Mohanty. 2026-08-03. Toxicoproteomic analysis reveals arsenic-induced alterations in eye lens proteins of Labeo rohita.. https://doi.org/10.1007/s10695-026-01762-5

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