The impact of the endoplasmic reticulum protein-folding environment on cancer development

2014 ◽  
Vol 14 (9) ◽  
pp. 581-597 ◽  
Author(s):  
Miao Wang ◽  
Randal J. Kaufman
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Cancer Development ◽  
Endoplasmic Reticulum Protein ◽  
The Impact

scholarly journals Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum

2006 ◽  
Vol 396 (1) ◽  
pp. 173-182 ◽  
Author(s):  
Karin Osibow ◽  
Sasa Frank ◽  
Roland Malli ◽  
Rudolf Zechner ◽  
Wolfgang F. Graier
Keyword(s):  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Lipoprotein Lipase ◽  
Chinese Hamster ◽  
Protein Levels ◽  
Dependent Activity ◽  
Dependent Protein ◽  
The Impact ◽  
Reversible Reduction

Considering the physiological Ca2+ dynamics within the ER (endoplasmic reticulum), it remains unclear how efficient protein folding is maintained in living cells. Thus, utilizing the strictly folding-dependent activity and secretion of LPL (lipoprotein lipase), we evaluated the impact of ER Ca2+ content and mitochondrial contribution to Ca2+-dependent protein folding. Exhaustive ER Ca2+ depletion by inhibition of sarcoplasmic/endoplasmic reticulum Ca2+-ATPases caused strong, but reversible, reduction of cell-associated and released activity of constitutive and adenovirus-encoded human LPL in CHO-K1 (Chinese-hamster ovary K1) and endothelial cells respectively, which was not due to decline of mRNA or intracellular protein levels. In contrast, stimulation with the IP3 (inositol 1,4,5-trisphosphate)-generating agonist histamine only moderately and transiently affected LPL maturation in endothelial cells that paralleled a basically preserved ER Ca2+ content. However, in the absence of extracellular Ca2+ or upon prevention of transmitochondrial Ca2+ flux, LPL maturation discontinued upon histamine stimulation. Collectively, these data indicate that Ca2+-dependent protein folding in the ER is predominantly controlled by intraluminal Ca2+ and is largely maintained during physiological cell stimulation owing to efficient ER Ca2+ refilling. Since Ca2+ entry and mitochondrial Ca2+ homoeostasis are crucial for continuous Ca2+-dependent protein maturation in the ER, their pathological alterations may result in dysfunctional protein folding.

Synthetic Substrates for an Endoplasmic Reticulum Protein-Folding Sensor, UDP-Glucose: Glycoprotein Glucosyltransferase

2005 ◽  
Vol 117 (48) ◽  
pp. 8164-8168 ◽  
Author(s):  
Kiichiro Totani ◽  
Yoshito Ihara ◽  
Ichiro Matsuo ◽  
Hiroyuki Koshino ◽  
Yukishige Ito
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Endoplasmic Reticulum Protein

scholarly journals miR-1307 promotes hepatocarcinogenesis by CALR-OSTC-endoplasmic reticulum protein folding pathway

iScience ◽  
2021 ◽  
pp. 103271
Author(s):  
Sijie Xie ◽  
Xiaoxue Jiang ◽  
Rushi Qin ◽  
Shuting Song ◽  
Yanan Lu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Folding Pathway ◽  
Endoplasmic Reticulum Protein

Synthetic Substrates for an Endoplasmic Reticulum Protein-Folding Sensor, UDP-Glucose: Glycoprotein Glucosyltransferase

2005 ◽  
Vol 44 (48) ◽  
pp. 7950-7954 ◽  
Author(s):  
Kiichiro Totani ◽  
Yoshito Ihara ◽  
Ichiro Matsuo ◽  
Hiroyuki Koshino ◽  
Yukishige Ito
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Endoplasmic Reticulum Protein

Abstracts of the 11th Winternational Symposium of the CSBMCB / Résumés du 11e symposium internationeige de la SCBBMC

2001 ◽  
Vol 79 (5) ◽  
pp. 637-679
Author(s):  
Abstracts / Résumés
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Molecular Machines ◽  
Canadian Society ◽  
Endoplasmic Reticulum Protein ◽  
Intracellular Organelles

Seventy-nine abstracts are presented from the Canadian Society of Biochemistry and Molecular & Cellular Biology's 11th Winternational Symposium on "Dynamics of Intracellular Organelles and Molecular Machines". The abstracts are representative of the symposium's wide-ranging discussions encompassing topics such as endoplasmic reticulum, protein folding and degradation, protein machines and organelle dynamics, and diseases associated with protein folding and trafficking.

scholarly journals Iminosugar antivirals: the therapeutic sweet spot

2017 ◽  
Vol 45 (2) ◽  
pp. 571-582 ◽  
Author(s):  
Dominic S. Alonzi ◽  
Kathryn A. Scott ◽  
Raymond A. Dwek ◽  
Nicole Zitzmann
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Antiviral Activity ◽  
Broad Spectrum ◽  
Antiviral Effect ◽  
Sweet Spot ◽  
Future Prospects ◽  
Wide Range ◽  
Viral Glycoproteins ◽  
Endoplasmic Reticulum Protein

Many viruses require the host endoplasmic reticulum protein-folding machinery in order to correctly fold one or more of their glycoproteins. Iminosugars with glucose stereochemistry target the glucosidases which are key for entry into the glycoprotein folding cycle. Viral glycoproteins are thus prevented from interacting with the protein-folding machinery leading to misfolding and an antiviral effect against a wide range of different viral families. As iminosugars target host enzymes, they should be refractory to mutations in the virus. Iminosugars therefore have great potential for development as broad-spectrum antiviral therapeutics. We outline the mechanism giving rise to the antiviral activity of iminosugars, the current progress in the development of iminosugar antivirals and future prospects for this field.

Sign in / Sign up

Export Citation Format

Share Document