Publications by authors named "I Kalvins"

Protein disulfide isomerases (PDIs) are involved in many intracellular and extracellular processes, including cell adhesion and cytoskeletal reorganisation, but their contribution to the regulation of fenestrations in liver sinusoidal endothelial cells (LSECs) remains unknown. Given that fenestrations are supported on a cytoskeleton scaffold, this study aimed to investigate whether endothelial PDIs regulate fenestration dynamics in primary mouse LSECs. PDIA3 and PDIA1 were found to be the most abundant among PDI isoforms in LSECs.

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In this study, we report a series of newly synthesised sulphonamides of aziridine-2-carboxylic acid (Az-COOH) ester and amide analogues as potent protein disulphide isomerase (PDI, EC 5.3.4.

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Article Synopsis
  • Protein disulphide isomerases (PDIs) are crucial in cancer progression, but their specific roles in tumor formation are still unclear.
  • In a study of 22 cancer cell lines, PDIA1 and PDIA3 were found to be the most abundant isoforms, while PDIA17 showed varying expression levels across different cell lines.
  • Inhibition of PDIA1 and PDIA3 led to significant anti-proliferative effects in breast cancer cells, with the most notable effects seen in hormone-sensitive MCF-7 cells, suggesting potential strategies for targeted cancer therapies.
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Background: Platelet-derived protein disulfide isomerase 1 (PDIA1) regulates thrombus formation, but its role in the regulation of platelet function is not fully understood.

Aims: The aim of this study was to characterize the role of PDIA1 in human platelets.

Methods: Proteomic analysis of PDI isoforms in platelets was performed using liquid chromatography tandem mass spectometry, and the expression of PDIs on platelets in response to collagen, TRAP-14, or ADP was measured with flow cytometry.

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Cancer cell cross-talk with the host endothelium plays a crucial role in metastasis, but the underlying mechanisms are still not fully understood. We studied the involvement of protein disulphide isomerase A1 (PDIA1) in human breast cancer cell (MCF-7 and MDA-MB-231) adhesion and transendothelial migration. For comparison, the role of PDIA1 in proliferation, migration, cell cycle and apoptosis was also assessed.

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