Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells
Calciprotein particles (CPPs) are indispensable scavengers of excessive Ca<sup>2+</sup> and PO<sub>4</sub><sup>3−</sup> ions in blood, being internalised and recycled by liver and spleen macrophages, monocytes, and endothelial cells (ECs). Here, we performed a pat...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-12-01
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| Series: | Journal of Cardiovascular Development and Disease |
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| Online Access: | https://www.mdpi.com/2308-3425/11/1/5 |
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| author | Daria Shishkova Arseniy Lobov Egor Repkin Victoria Markova Yulia Markova Anna Sinitskaya Maxim Sinitsky Egor Kondratiev Evgenia Torgunakova Anton Kutikhin |
| author_facet | Daria Shishkova Arseniy Lobov Egor Repkin Victoria Markova Yulia Markova Anna Sinitskaya Maxim Sinitsky Egor Kondratiev Evgenia Torgunakova Anton Kutikhin |
| author_sort | Daria Shishkova |
| collection | DOAJ |
| description | Calciprotein particles (CPPs) are indispensable scavengers of excessive Ca<sup>2+</sup> and PO<sub>4</sub><sup>3−</sup> ions in blood, being internalised and recycled by liver and spleen macrophages, monocytes, and endothelial cells (ECs). Here, we performed a pathway enrichment analysis of cellular compartment-specific proteomes in primary human coronary artery ECs (HCAEC) and human internal thoracic artery ECs (HITAEC) treated with primary (amorphous) or secondary (crystalline) CPPs (CPP-P and CPPs, respectively). Exposure to CPP-P and CPP-S induced notable upregulation of: (1) cytokine- and chemokine-mediated signaling, Ca<sup>2+</sup>-dependent events, and apoptosis in cytosolic and nuclear proteomes; (2) H<sup>+</sup> and Ca<sup>2+</sup> transmembrane transport, generation of reactive oxygen species, mitochondrial outer membrane permeabilisation, and intrinsic apoptosis in the mitochondrial proteome; (3) oxidative, calcium, and endoplasmic reticulum (ER) stress, unfolded protein binding, and apoptosis in the ER proteome. In contrast, transcription, post-transcriptional regulation, translation, cell cycle, and cell–cell adhesion pathways were underrepresented in cytosol and nuclear compartments, whilst biosynthesis of amino acids, mitochondrial translation, fatty acid oxidation, pyruvate dehydrogenase activity, and energy generation were downregulated in the mitochondrial proteome of CPP-treated ECs. Differentially expressed organelle-specific pathways were coherent in HCAEC and HITAEC and between ECs treated with CPP-P or CPP-S. Proteomic analysis of mitochondrial and nuclear lysates from CPP-treated ECs confirmed bioinformatic filtration findings. |
| first_indexed | 2024-03-08T10:45:59Z |
| format | Article |
| id | doaj.art-19643740034d41aab0fc2380524e852f |
| institution | Directory Open Access Journal |
| issn | 2308-3425 |
| language | English |
| last_indexed | 2024-03-08T10:45:59Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Cardiovascular Development and Disease |
| spelling | doaj.art-19643740034d41aab0fc2380524e852f2024-01-26T17:04:44ZengMDPI AGJournal of Cardiovascular Development and Disease2308-34252023-12-01111510.3390/jcdd11010005Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial CellsDaria Shishkova0Arseniy Lobov1Egor Repkin2Victoria Markova3Yulia Markova4Anna Sinitskaya5Maxim Sinitsky6Egor Kondratiev7Evgenia Torgunakova8Anton Kutikhin9Department of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaLaboratory of Regenerative Biomedicine, Institute of Cytology of the RAS, 4 Tikhoretskiy Prospekt, 194064 St. Petersburg, RussiaCentre for Molecular and Cell Technologies, St. Petersburg State University, Universitetskaya Embankment, 7/9, 199034 St. Petersburg, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaDepartment of Experimental Medicine, Research Institute for Complex Issues of Cardiovascular Diseases, 6 Sosnovy Boulevard, 650002 Kemerovo, RussiaCalciprotein particles (CPPs) are indispensable scavengers of excessive Ca<sup>2+</sup> and PO<sub>4</sub><sup>3−</sup> ions in blood, being internalised and recycled by liver and spleen macrophages, monocytes, and endothelial cells (ECs). Here, we performed a pathway enrichment analysis of cellular compartment-specific proteomes in primary human coronary artery ECs (HCAEC) and human internal thoracic artery ECs (HITAEC) treated with primary (amorphous) or secondary (crystalline) CPPs (CPP-P and CPPs, respectively). Exposure to CPP-P and CPP-S induced notable upregulation of: (1) cytokine- and chemokine-mediated signaling, Ca<sup>2+</sup>-dependent events, and apoptosis in cytosolic and nuclear proteomes; (2) H<sup>+</sup> and Ca<sup>2+</sup> transmembrane transport, generation of reactive oxygen species, mitochondrial outer membrane permeabilisation, and intrinsic apoptosis in the mitochondrial proteome; (3) oxidative, calcium, and endoplasmic reticulum (ER) stress, unfolded protein binding, and apoptosis in the ER proteome. In contrast, transcription, post-transcriptional regulation, translation, cell cycle, and cell–cell adhesion pathways were underrepresented in cytosol and nuclear compartments, whilst biosynthesis of amino acids, mitochondrial translation, fatty acid oxidation, pyruvate dehydrogenase activity, and energy generation were downregulated in the mitochondrial proteome of CPP-treated ECs. Differentially expressed organelle-specific pathways were coherent in HCAEC and HITAEC and between ECs treated with CPP-P or CPP-S. Proteomic analysis of mitochondrial and nuclear lysates from CPP-treated ECs confirmed bioinformatic filtration findings.https://www.mdpi.com/2308-3425/11/1/5calciprotein particlesmineral stressendothelial cellsproteomic profilingcytosolnuclei |
| spellingShingle | Daria Shishkova Arseniy Lobov Egor Repkin Victoria Markova Yulia Markova Anna Sinitskaya Maxim Sinitsky Egor Kondratiev Evgenia Torgunakova Anton Kutikhin Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells Journal of Cardiovascular Development and Disease calciprotein particles mineral stress endothelial cells proteomic profiling cytosol nuclei |
| title | Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells |
| title_full | Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells |
| title_fullStr | Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells |
| title_full_unstemmed | Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells |
| title_short | Calciprotein Particles Induce Cellular Compartment-Specific Proteome Alterations in Human Arterial Endothelial Cells |
| title_sort | calciprotein particles induce cellular compartment specific proteome alterations in human arterial endothelial cells |
| topic | calciprotein particles mineral stress endothelial cells proteomic profiling cytosol nuclei |
| url | https://www.mdpi.com/2308-3425/11/1/5 |
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