Cited by 197Endoplasmic Reticulum Stress and DiseaseIon Channels and ReceptorsRNA and protein synthesis mechanisms

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Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

Brostrom, Margaret A, Brostrom, Charles O·2003·Cell Calcium

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Abstract

The endoplasmic reticulum (ER) possesses the structural and functional features expected of an organelle that supports the integration and coordination of major cellular processes. Ca(2+) sequestered within the ER sustains lumenal protein processing while providing a reservoir of the cation to support stimulus-response coupling in the cytosol. Release of ER Ca(2+) sufficient to impair protein processing promotes ER stress and signals the "unfolded protein response" (UPR). The association of the UPR with an acute suppression of mRNA translational initiation and a longer term up-regulation of ER chaperones and partial translational recovery is discussed. Regulatory sites in mRNA translation and the mechanisms responsible for the early and later phases of the UPR are reviewed. The regulatory significance of GRP78/BiP, a multifunctional, broad-specificity ER chaperone, in the coordination of ER protein processing with mRNA translation during acute and chronic ER stress is addressed. The relationship of ER stress to protein misfolding in the cytoplasm is examined. Translational alterations in embryonic cardiomyocytes during treatments with various Ca(2+)-mobilizing, growth-promoting stimuli are described. The importance of ER Ca(2+) stores, ER chaperones, and cytosolic-free Ca(2+) in translational control and growth promotion by these stimuli is assessed. Some perspectives are provided regarding Ca(2+) as an integrating factor in the generation or diversion of metabolic energy. Circumstances impacting upon cellular adaptability during exposure to growth stimuli or during stressful conditions that require rapid adjustments in ATP for continued viability are considered.

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Retracted
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[Retracted] Piezo1 protein induces the apoptosis of human osteoarthritis‑derived chondrocytes by activating caspase‑12, the signaling marker of ER stress
Li, X., Zhang, Z., Chen, Z.-K., Cui, Z.-W., & Zhang, H. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3918 · Cited by 32
Retracted
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Authors: Brostrom, M. A., & Brostrom, C. O.
Corresponding author: Brostrom, Margaret A
Venue: Cell Calcium
Publisher: Elsevier BV
Published: 2003-10
Volume: 34
Issue: 4-5
Pages: 345-363
ISSN: 0143-4160 (ISSN-L)
DOI: 10.1016/s0143-4160(03)00127-1
OpenAlex: W2038563918
Cited by: 197
References: 124
Citations by year: 2026: 3 · 2025: 5 · 2024: 4 · 2023: 3 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 12 · 2018: 5 · 2017: 16 · 2016: 5 · 2015: 9 · 2014: 10 · 2013: 12 · 2012: 13
FWCI: 0.48
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cell Calcium (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: endoplasmic reticulum calcium, ER calcium stores, unfolded protein response, endoplasmic reticulum stress, protein synthesis regulation, translational regulation, GRP78, ER chaperones, cytosolic free calcium, protein misfolding, embryonic cardiomyocytes, cell growth, ATP metabolism, mRNA translation regulation
MeSH terms: Endoplasmic Reticulum Chaperone BiP, Adenosine Triphosphate, Animals, Calcium, Carrier Proteins, Cell Division, Endoplasmic Reticulum, Gene Expression Regulation, Heat-Shock Proteins, Hormones, Humans, Hypertrophy, Models, Biological, Protein Processing, Post-Translational, Sarcoplasmic Reticulum, Protein Biosynthesis, Vasopressins, Eukaryotic Initiation Factor-2, Molecular Chaperones, Calcium Signaling, Myocytes, Cardiac

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Calcium dynamics and endoplasmic reticular function in the regulation of protein synthesis: implications for cell growth and adaptability

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