scholarly journals Endoplasmic Reticulum Stress (ER Stress) and Unfolded Protein Response (UPR) Occur in a Rat Varicocele Testis Model

2020 ◽  
Vol 2020 ◽  
pp. 1-11 ◽  
Author(s):  
Mahshid Hosseini ◽  
Erfaneh Shaygannia ◽  
Mohsen Rahmani ◽  
Anahita Eskandari ◽  
Aram Ahmadzadeh Golsefid ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Unfolded Protein Response ◽  
Caspase 3 ◽  
Membrane Sensor ◽  
Unfolded Protein ◽  
Jun Kinase ◽  
Induction Of Apoptosis ◽  
Protein Response ◽  
Surgically Induced ◽  
Spliced Variant

Using a surgically induced varicocele rat model, we show here strong evidence that the misfolded/unfolded protein response that is part of the stress response of the endoplasmic reticulum (ER) is activated in the varicocele testis (VCL), leading to the induction of apoptosis. To support this hypothesis, it is observed that the spliced variant of the X-box protein 1 (XBP1s), resulting from the activation of the inositol-requiring enzyme 1 (IRE1) membrane sensor, is significantly more represented in VCL testicular extracts. The activation of the IRE1/XBP1s pathway is also supported by the observation that the VCL testes show an increase phosphorylation of the c-Jun-kinase (JNK) known to be one intermediate of this pathway and an increased level of caspase-3, the terminal apoptotic effector, partly explaining the apoptotic status of the VCL testis.

scholarly journals Uterine Endoplasmic Reticulum Stress and Its Unfolded Protein Response May Regulate Caspase 3 Activation in the Pregnant Mouse Uterus

PLoS ONE ◽  
2013 ◽  
Vol 8 (9) ◽  
pp. e75152 ◽  
Author(s):  
Arvind Suresh ◽  
Kalpana Subedi ◽  
Chandrashekara Kyathanahalli ◽  
Pancharatnam Jeyasuria ◽  
Jennifer C. Condon
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Unfolded Protein Response ◽  
Caspase 3 ◽  
Pregnant Mouse ◽  
Mouse Uterus ◽  
Unfolded Protein ◽  
Protein Response

scholarly journals Uterine endoplasmic reticulum stress-unfolded protein response regulation of gestational length is caspase-3 and -7–dependent

2015 ◽  
Vol 112 (45) ◽  
pp. 14090-14095 ◽  
Author(s):  
Chandrashekara Kyathanahalli ◽  
Kenna Organ ◽  
Rebecca S. Moreci ◽  
Prashanth Anamthathmakula ◽  
Sonia S. Hassan ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Unfolded Protein Response ◽  
Caspase 3 ◽  
Endoplasmic Reticulum Stress Response ◽  
Gestational Length ◽  
Unfolded Protein ◽  
Junction Protein ◽  
Protein Response

We previously identified myometrial caspase-3 (CASP3) as a potential regulator of uterine quiescence. We also determined that during pregnancy, the functional activation of uterine CASP3 is likely governed by an integrated endoplasmic reticulum stress response (ERSR) and is consequently limited by an increased unfolded protein response (UPR). The present study examined the functional relevance of uterine UPR-ERSR in maintaining myometrial quiescence and regulating the timing of parturition. In vitro analysis of the human uterine myocyte hTERT-HM cell line revealed that tunicamycin (TM)-induced ERSR modified uterine myocyte contractile responsiveness. Accordingly, alteration of in vivo uterine UPR-ERSR using a pregnant mouse model significantly modified gestational length. We determined that “normal” gestational activation of the ERSR-induced CASP3 and caspase 7 (CASP7) maintains uterine quiescence through previously unidentified proteolytic targeting of the gap junction protein, alpha 1(GJA1); however, surprisingly, TM-induced uterine ERSR triggered an exaggerated UPR that eliminated uterine CASP3 and 7 tocolytic action precociously. These events allowed for a premature increase in myometrial GJA1 levels, elevated contractile responsiveness, and the onset of preterm labor. Importantly, a successful reversal of the magnified ERSR-induced preterm birth phenotype could be achieved by pretreatment with 4-phenylbutrate, a chaperone protein mimic.

scholarly journals The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane.

1997 ◽  
Vol 8 (9) ◽  
pp. 1805-1814 ◽  
Author(s):  
J S Cox ◽  
R E Chapman ◽  
P Walter
Keyword(s):  
Endoplasmic Reticulum ◽  
Unfolded Protein Response ◽  
Secretory Pathway ◽  
Lipid Synthesis ◽  
Secretory Proteins ◽  
Endoplasmic Reticulum Membrane ◽  
Yeast Saccharomyces Cerevisiae ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

The endoplasmic reticulum (ER) is a multifunctional organelle responsible for production of both lumenal and membrane components of secretory pathway compartments. Secretory proteins are folded, processed, and sorted in the ER lumen and lipid synthesis occurs on the ER membrane itself. In the yeast Saccharomyces cerevisiae, synthesis of ER components is highly regulated: the ER-resident proteins by the unfolded protein response and membrane lipid synthesis by the inositol response. We demonstrate that these two responses are intimately linked, forming different branches of the same pathway. Furthermore, we present evidence indicating that this coordinate regulation plays a role in ER biogenesis.

scholarly journals Class I histone deacetylases localize to the endoplasmic reticulum and modulate the unfolded protein response

2012 ◽  
Vol 26 (6) ◽  
pp. 2437-2445 ◽  
Author(s):  
Soumen Kahali ◽  
Bhaswati Sarcar ◽  
Antony Prabhu ◽  
Edward Seto ◽  
Prakash Chinnaiyan
Keyword(s):  
Endoplasmic Reticulum ◽  
Unfolded Protein Response ◽  
Histone Deacetylases ◽  
Class I ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response
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