Abstract
The protein quality control (PQC) mechanism is essential for cell function and viability. PQC with proper biological function depends on molecular chaperones and proteases. The hypertonicity-induced protein damage and responses of PQC mechanism in aquatic organisms, however, are poorly understood. In this study, we examine the short-term effects of different hypertonic shocks on the levels of heat shock proteins (HSPs, e.g., HSP70 and HSP90), ubiquitin-conjugated proteins and protein aggregation in gills of the Mozambique tilapia (Oreochromis mossambicus). Following transfer from fresh water (FW) to 20‰ hypertonicity, all examined individuals survived to the end of experiment. Moreover, the levels of branchial HSPs and ubiquitin-conjugated proteins significantly increased at 3 and 24 h post-transfer, respectively. Up-regulation of HSPs and ubiquitin-conjugated proteins was sufficient to prevent the accumulation of aggregated proteins. However, the survival rate of tilapia dramatically declined at 5 h and all fish died within 7 h after direct transfer to 30‰ hypertonicity. We presumed that this result was due to the failed activation of gill PQC system, which resulted in elevating the levels of aggregated proteins at 3 and 4 h. Furthermore, in aggregated protein fractions, the amounts of gill Na+/K+-ATPase (NKA) remained relatively low when fish were transferred to 20‰ hypertonicity, whereas abundant NKA was found at 4 h post-transfer to 30‰ hypertonicity. This study demonstrated that the response of PQC in gills is earlier than observable changes in localization of ion-secreting transport proteins upon hypertonic challenge. To our knowledge, this is the first study to investigate the regulation of PQC mechanism in fish and characterize its important role in euryhaline teleost survival in response to hypertonic stress.
Highlights
Environmental stresses cause numerous perturbations that are detrimental to cellular homeostasis and physiological function
Tilapia did not survive more than 7 h after direct transfer from fresh water (FW) to 30% hypertonicity (30% SW) (Fig. 1; close circle)
It is generally accepted that ion secretion is mediated by apical cystic fibrosis transmembrane conductance regulator (CFTR) Cl2 channel and basolateral Na+/K+/2Cl2 cotransporter (NKCC) in gill mitochondrion-rich (MR) cells of fish acclimated to a hypertonic environment [8,9,22,23,24,25]
Summary
Environmental stresses cause numerous perturbations that are detrimental to cellular homeostasis and physiological function. Compensatory responses induced by diverse stresses are essential for cell survival under adverse conditions. The mechanisms of induced cellular responses are regulated by many molecular processes that aid cell adaptation to various stresses [1]. Proteins are the molecules possess the biological function to carry out diverse mechanisms responsible for cellular function. The expression and maintenance of functional proteins depends on more than transcription and translation [2]. Chaperones and proteases mediate protein quality control (PQC), prevent protein aggregation, and maintain cell viability in many species under stressful conditions, from unicellular organisms to plants and animals [2,3,4,5]
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