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1.
Food Chem ; 368: 130768, 2022 Jan 30.
Artigo em Inglês | MEDLINE | ID: mdl-34392120

RESUMO

Apoptosis plays a critical role in sea cucumber autolysis. To investigate the ultraviolet (UV)-induced apoptosis, sea cucumbers with and without injection of BAPTA-AM (cytosolic calcium chelator) were exposed to UV (15 W/m2) for 30 min. The results showed that UV irradiation caused several changes in sea cucumber coelomocytes, including calcium imbalance, abnormal morphology of endoplasmic reticulum, upregulation of pro-apoptotic proteins CRT, CHOP, and caspases 9 and 3, and downregulation of anti-apoptotic protein Bcl-2. A comparison between the two groups showed that injection of the calcium chelator into sea cucumbers helped maintain coelomocyte intracellular calcium homeostasis and suppressed other abnormal changes caused by ER stress, indicating apoptosis in sea cucumbers is mediated by calcium imbalance and follows the activation of the ER stress pathway. Therefore, this study broadens understanding of the apoptotic mechanism involved in sea cucumber autolysis, which is helpful in developing preservative agents for sea cucumbers.


Assuntos
Pepinos-do-Mar , Stichopus , Animais , Autólise , Cálcio , Homeostase
2.
Int J Mol Sci ; 21(3)2020 Feb 04.
Artigo em Inglês | MEDLINE | ID: mdl-32033098

RESUMO

Salmonella typhimurium (S. typhimurium) is a common foodborne pathogen that not only causes diseases and contaminates food, but also causes considerable economic losses. Therefore, it is necessary to find effective and feasible methods to control S. typhimurium. In this study, changes in S. typhimurium after treatment with benzyl isothiocyanate (BITC) were detected by transcriptomics to explore the antibacterial effect of BITC at subinhibitory concentration. The results showed that, in contrast to the control group (SC), the BITC-treated group (SQ_BITC) had 197 differentially expressed genes (DEGs), of which 115 were downregulated and 82 were upregulated. We screened out eight significantly downregulated virulence-related genes and verified gene expression by quantitative Real-time Polymerase Chain Reaction (qRT-PCR). We also selected motility and biofilm formation to observe the effects of BITC on the other virulence related factors of S. typhimurium. The results showed that both swimming and swarming were significantly inhibited. BITC also had a significant inhibitory effect on biofilm formation, and showed an effect on bacterial morphology. These results will be helpful for understanding the mechanism of the antibacterial action of BITC against S. typhimurium and other foodborne pathogens.


Assuntos
Antibacterianos/farmacologia , Biofilmes/efeitos dos fármacos , Isotiocianatos/farmacologia , Salmonella typhimurium/efeitos dos fármacos , Transcriptoma/efeitos dos fármacos , Transcriptoma/genética , Perfilação da Expressão Gênica/métodos , Testes de Sensibilidade Microbiana/métodos , Salmonella typhimurium/genética , Virulência/efeitos dos fármacos , Virulência/genética , Fatores de Virulência/genética
3.
Molecules ; 21(11)2016 Nov 16.
Artigo em Inglês | MEDLINE | ID: mdl-27854344

RESUMO

We aimed to explore the differences of thermal behaviors between insoluble collagen fibrils (ICFs) and pepsin-solubilized collagens (PSCs) from sea cucumber Stichopus japonicus. The unfolding/refolding sequences of secondary structures of ICFs and PSCs during the heating and cooling cycle (5 → 70 → 5 °C) were identified by Fourier transform infrared spectrometry combined with curve-fitting and 2D correlation techniques. ICFs showed a higher proportion of α-helical structures and higher thermostability than PSCs, and thus had more-stable triple helical structures. The sequences of changes affecting the secondary structures during heating were essentially the same between ICFs and PSCs. In all cases, α-helix structure was the most important conformation and it disappeared to form a ß-sheet structure. In the cooling cycle, ICFs showed a partially refolding ability, and the proportion of ß-sheet structure rose before the increasing proportion of α-helix structure. PSCs did not obviously refold during the cooling stage.


Assuntos
Colágeno/química , Redobramento de Proteína , Desdobramento de Proteína , Pepinos-do-Mar/química , Espectroscopia de Infravermelho com Transformada de Fourier , Aminoácidos , Animais , Desnaturação Proteica , Termodinâmica
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