Protective effect of catechin in type I Gaucher disease cells by reducing endoplasmic reticulum stress

Background and Objective: This study investigated whether rapamycin has a protective effect on the testis of diabetic rats by regulating autophagy, endoplasmic reticulum stress, and oxidative stress. Methods: Thirty male Sprague-Dawley rats were randomly divided into three groups: control, diabetic, and diabetic treated with rapamycin, which received gavage of rapamycin (2mg.kg-1.d-1) after induction of diabetes. Diabetic rats were induced by intraperitoneal injection of streptozotocin (STZ, 65mg.Kg-1). All rats were sacrificed at the termination after 8 weeks of rapamycin treatment. The testicular pathological changes were determined by hematoxylin and eosin staining. The protein or mRNA expression of autophagy-related proteins (Beclin1, microtubule-associated protein light chain 3 (LC3), p62), ER stress marked proteins (CCAAT/enhancer-binding protein (C/EBP) homologous protein (CHOP), caspase-12), oxidative stress-related proteins (p22phox, nuclear factor erythroid2-related factor 2 (Nrf2)) and apoptosis-related proteins (Bax, B cell lymphoma-2 (Bcl-2)) were assayed by western blot or real-time fluorescence quantitative PCR. Results: There were significant pathological changes in the testes of diabetic rats. The expression of Beclin1, LC3, Nrf2, Bcl-2 were significantly decreased and p62, CHOP, caspase12, p22phox, and Bax were notably increased in the testis of diabetic rats (P <0.05). However, rapamycin treatment for 8 weeks significantly reversed the above changes in the testis of diabetic rats (P <0.05). Conclusion: Rapamycin appears to produce a protective effect on the testes of diabetic rats by inducing the expression of autophagy and inhibiting the expression of ER-stress, oxidative stress, and apoptosis.

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Protective effect of butanol extracts of skin of Anguilla japonica against endoplasmic reticulum stress-induced insulin resistance via the AMPK pathway in L6 myotubes

Food Science and Biotechnology ◽

10.1007/s10068-015-0137-5 ◽

2015 ◽

Vol 24 (3) ◽

pp. 1069-1075

Author(s):

Min Kyun Na ◽

Yong-Tae Jeong ◽

Xian Li ◽

Fansi Jin ◽

Seung-Lark Hwang ◽

...

Keyword(s):

Insulin Resistance ◽

Endoplasmic Reticulum ◽

Endoplasmic Reticulum Stress ◽

Protective Effect ◽

Anguilla Japonica ◽

Ampk Pathway ◽

L6 Myotubes

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An essential dimer-forming subregion of the endoplasmic reticulum stress sensor Ire1

Biochemical Journal ◽

10.1042/bj20050640 ◽

2005 ◽

Vol 391 (1) ◽

pp. 135-142 ◽

Cited By ~ 27

Author(s):

Daisuke Oikawa ◽

Yukio Kimata ◽

Masato Takeuchi ◽

Kenji Kohno

Keyword(s):

Endoplasmic Reticulum ◽

Recombinant Protein ◽

Endoplasmic Reticulum Stress ◽

Transmembrane Protein ◽

Type I ◽

Unfolded Protein ◽

The Unfolded Protein Response ◽

Protein Response ◽

Recombinant Fragments ◽

Made In

The luminal domain of the type I transmembrane protein Ire1 senses endoplasmic reticulum stress by an undefined mechanism to up-regulate the signalling pathway for the unfolded protein response. Previously, we proposed that the luminal domain of yeast Ire1 is divided into five subregions, termed subregions I–V sequentially from the N-terminus. Ire1 lost activity when internal deletions of subregion II or IV were made. In the present paper, we show that partial proteolysis of a recombinant protein consisting of the Ire1 luminal domain suggests that subregions II–IV are tightly folded. We also show that a recombinant protein of subregions II–IV formed homodimers, and that this homodimer formation was impaired by an internal deletion of subregion IV. Furthermore, recombinant fragments of subregion IV exhibited a self-binding ability. Therefore, although its sequence is little conserved evolutionarily, subregion IV plays an essential role to promote Ire1 dimer formation.

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