Project description:Transcriptional profiling of calpain-6-deficient murine bone marrow-derived macrophages comparing with calpain-6 wild-type macrophages. Total RNA was extracted from the pooled cells. Two-condition experiment, wild-type macrophages vs. calpain-6-deficiennt macrophages. The cells were derived from four mice, and were pooled for analysis.

2016-06-29 | E-GEOD-83815 | biostudies-arrayexpress

Calpain inhibition prevents high-glucose-induced autophagy blockade and mitochondrial fragmentation in endothelial cells and preserves vascular functions in diabetic mice

Project description:Endothelial dysfunction is a major contributor to diabetic vascular complications, yet the mechanisms linking hyperglycemia to impaired endothelial homeostasis remain insufficiently defined. This study identifies calpains as key regulators of endothelial autophagy and mitophagy under diabetic conditions. In HUVECs and primary lung endothelial cells, hyperglycemia activated calpains and induced autophagic flux blockade, characterized by SQSTM1 accumulation, reduced LC3B expression, and impaired mitophagy associated with mitochondrial fragmentation. Pharmacological calpain inhibition or genetic calpastatin overexpression restored autophagic flux and preserved mitochondrial network architecture. Transcriptomic profiling revealed that calpain inhibition counteracted major hyperglycemia‑driven pathways, including oxidative phosphorylation, ROS signaling, and the unfolded protein response. Collectively, our findings demonstrate that calpain overactivation disrupts endothelial autophagy and mitophagy in diabetes, contributing to mitochondrial dysfunction and altered vascular reactivity. Restoring autophagic flux through calpain inhibition emerges as a promising strategy to preserve endothelial homeostasis and limit diabetic vascular complications.

2026-09-01 | GSE339355 | GEO

DEK1 calpain overexpression

Project description:Aim: To understand the role of DEK1 in Arabidopsis development. Background: DEK1 has an essential role during embryogenesis and is involved in the maintenance of the epidermis. Tissues: Comparison of wild-type and ADEK1 calpain-overexpressing line. 9 samples were used in this experiment.

2009-12-09 | E-GEOD-19268 | biostudies-arrayexpress

DEK1 calpain overexpression

2009-12-10 | GSE19268 | GEO

Brain death associated activation of Calpain-Talin axis in donor kidneys underlies podocyte matrix degradation and graft dysfunction in kidney transplantation

Project description:Deceased kidney donation after brain death (DBD) is the main source of transplants, yet these grafts yield inferior transplant outcomes when compared to living donation. In brain death, cerebral injury contributes to systemic biological dysregulation, causing significant cellular stress in donor kidneys that adversely impacts the quality of grafts. Here, we hypothesized that proteolytic processes in DBD kidneys might lead to podocyte damage with subsequent development of post-transplant dysfunction. Using protein topography and migration analysis platform (PROTOMAP), we mapped degradation profiles of cytoskeletal proteins in DBD kidneys. Cytoskeletal proteolytic degradation was further studied by Immunoblotting on a separate cohort of deceased and living donor kidney biopsies. To investigate potential mechanism of kidney cytoskeletal protein degradation, in-vitro human podocytes and ex-vivo precision-cut human kidney slices were employed. We found novel proteolytic profiles of key podocyte cytoskeletal proteins in donor kidneys associated with suboptimal posttransplant function. These were unique to brain-death and were not observed in circulatory-death or living-donor kidneys. Talin-specific protein degradation in DBD kidneys indicated Calpain-1 activation may have a key role in proteolytic processes observed in the dysfunctional kidneys. Investigation of the underlying mechanism suggests that Transforming-Growth Factor-Î² (TGFÎ²) induces Calpain-1 activation, leading to brain-death specific podocyte degradation patterns and dysregulation of actin cytoskeleton; events that were prevented, in-vitro, by Calpain inhibition. Conclusion Our data demonstrate that podocyte protein degradation impacts the quality of DBD kidneys, propose a role of TGFÎ² mediated Calpain-1 proteolytic processing of cytoskeletal Talin-1, suggesting therapeutic opportunities to prevent kidney dysfunction.

2022-08-12 | PXD022074 | Pride

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