Standard

Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells. / Шишкова, Дарья; Лобов, Арсений Андреевич; Репкин, Егор Алексеевич; Маркова, Виктория; Маркова, Юлия; Синицкая, Анна Викторовна; Синицкий, Максим; Кондратьев, Егор; Торгунакова, Евгения ; Кутихин, Антон.

в: Journal of Cardiovascular Development and Disease, Том 11, № 1, 5, 2024.

Результаты исследований: Научные публикации в периодических изданияхстатьяРецензирование

Harvard

Шишкова, Д, Лобов, АА, Репкин, ЕА, Маркова, В, Маркова, Ю, Синицкая, АВ, Синицкий, М, Кондратьев, Е, Торгунакова, Е & Кутихин, А 2024, 'Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells', Journal of Cardiovascular Development and Disease, Том. 11, № 1, 5. https://doi.org/10.3390/jcdd11010005

APA

Шишкова, Д., Лобов, А. А., Репкин, Е. А., Маркова, В., Маркова, Ю., Синицкая, А. В., Синицкий, М., Кондратьев, Е., Торгунакова, Е., & Кутихин, А. (2024). Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells. Journal of Cardiovascular Development and Disease, 11(1), [5]. https://doi.org/10.3390/jcdd11010005

Vancouver

Шишкова Д, Лобов АА, Репкин ЕА, Маркова В, Маркова Ю, Синицкая АВ и пр. Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells. Journal of Cardiovascular Development and Disease. 2024;11(1). 5. https://doi.org/10.3390/jcdd11010005

Author

Шишкова, Дарья ; Лобов, Арсений Андреевич ; Репкин, Егор Алексеевич ; Маркова, Виктория ; Маркова, Юлия ; Синицкая, Анна Викторовна ; Синицкий, Максим ; Кондратьев, Егор ; Торгунакова, Евгения ; Кутихин, Антон. / Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells. в: Journal of Cardiovascular Development and Disease. 2024 ; Том 11, № 1.

BibTeX

@article{8d1a37b472d3440fafa66542a98c3842,
title = "Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells",
abstract = "Calciprotein particles (CPPs) are indispensable scavengers of excessive Ca2+ and PO43− 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, Ca2+-dependent events, and apoptosis in cytosolic and nuclear proteomes; (2) H+ and Ca2+ 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.",
author = "Дарья Шишкова and Лобов, {Арсений Андреевич} and Репкин, {Егор Алексеевич} and Виктория Маркова and Юлия Маркова and Синицкая, {Анна Викторовна} and Максим Синицкий and Егор Кондратьев and Евгения Торгунакова and Антон Кутихин",
year = "2024",
doi = "10.3390/jcdd11010005",
language = "English",
volume = "11",
journal = "Journal of Cardiovascular Development and Disease",
issn = "2308-3425",
publisher = "MDPI AG",
number = "1",

}

RIS

TY - JOUR

T1 - Calciprotein particles induce cellular compartment-specific proteome alterations in human arterial endothelial cells

AU - Шишкова, Дарья

AU - Лобов, Арсений Андреевич

AU - Репкин, Егор Алексеевич

AU - Маркова, Виктория

AU - Маркова, Юлия

AU - Синицкая, Анна Викторовна

AU - Синицкий, Максим

AU - Кондратьев, Егор

AU - Торгунакова, Евгения

AU - Кутихин, Антон

PY - 2024

Y1 - 2024

N2 - Calciprotein particles (CPPs) are indispensable scavengers of excessive Ca2+ and PO43− 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, Ca2+-dependent events, and apoptosis in cytosolic and nuclear proteomes; (2) H+ and Ca2+ 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.

AB - Calciprotein particles (CPPs) are indispensable scavengers of excessive Ca2+ and PO43− 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, Ca2+-dependent events, and apoptosis in cytosolic and nuclear proteomes; (2) H+ and Ca2+ 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.

UR - https://www.mendeley.com/catalogue/2f747633-72ee-30bc-bdcf-71cf48d3da33/

U2 - 10.3390/jcdd11010005

DO - 10.3390/jcdd11010005

M3 - Article

VL - 11

JO - Journal of Cardiovascular Development and Disease

JF - Journal of Cardiovascular Development and Disease

SN - 2308-3425

IS - 1

M1 - 5

ER -

ID: 115264571