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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Osibow, K; Frank, S; Malli, R; Zechner, R; Graier, WF.
Mitochondria maintain maturation and secretion of lipoprotein lipase in the endoplasmic reticulum.
Biochem J. 2006; 396(1): 173-182.
Doi: 10.1042/BJ20060099
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- Führende Autor*innen der Med Uni Graz
- Graier Wolfgang
- Osibow Karin
- Co-Autor*innen der Med Uni Graz
- Frank Sasa
- Malli Roland
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- Abstract:
- 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.
- Find related publications in this database (using NLM MeSH Indexing)
- Adenoviridae - genetics
- Animals -
- CHO Cells - metabolism
- Calcium - physiology
- Calcium Signaling -
- Calcium-Transporting ATPases - antagonists and inhibitors
- Clonazepam - analogs and derivatives Clonazepam - pharmacology
- Cricetinae -
- Cricetulus -
- Endoplasmic Reticulum - metabolism
- Endothelial Cells - metabolism
- Genetic Vectors -
- Histamine - pharmacology
- Humans -
- Hydroquinones - pharmacology
- Inositol 1,4,5-Trisphosphate - agonists
- Lipoprotein Lipase - biosynthesis Lipoprotein Lipase - chemistry Lipoprotein Lipase - secretion
- Mitochondria - physiology
- Protein Folding -
- Protein Processing, Post-Translational -
- Recombinant Fusion Proteins - metabolism
- Thiazepines - pharmacology
- Find related publications in this database (Keywords)
- Ca2+-dependent protein folding
- endoplasmic reticulum
- intraluminal Ca2+
- lipoprotein lipase
- mitochondrion