Category Ranking

98%

Total Visits

921

Avg Visit Duration

2 minutes

Citations

20

Article Abstract

DNA-binding protein A (DbpA) belongs to the Y-box family of cold shock domain proteins that exert transcriptional and translational activities in the cell via their ability to bind and regulate mRNA. To investigate the role of DbpA in kidney disease, we utilized the murine unilateral ureter obstruction (UUO) model, which recapitulates many features of obstructive nephropathy seen in humans. We observed that DbpA protein expression is induced within the renal interstitium following disease induction. Compared with wild-type animals, obstructed kidneys from -deficient mice are protected from tissue injury, with a significant reduction in the number of infiltrating immune cells as well as in extracellular matrix deposition. RNAseq data from UUO kidneys show that is expressed by activated fibroblasts, which reside within the renal interstitium. Our data support a role for DbpA in orchestrating renal fibrosis and suggest that strategies targeting DbpA may be a therapeutic option to slow disease progression.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10217384PMC
http://dx.doi.org/10.3390/cells12101426DOI Listing

Publication Analysis

Top Keywords

cold shock
8
shock domain
8
protein dbpa
8
kidney disease
8
role dbpa
8
renal interstitium
8
dbpa
6
domain protein
4
dbpa orchestrates
4
orchestrates tubular
4

Similar Publications

Background: Massive hemorrhage is a leading cause of mortality among trauma patients. To date, whole blood (WB) remains the preferred resuscitation fluid on the battlefield and in pre-hospital emergency care. However, components of WB inevitably undergo storage-related damage, and differences in the duration of storage may lead to varying clinical outcomes after transfusion.

View Article and Find Full Text PDF

Background: The cold-shock domain protein YB-1 is overexpressed in pleural mesothelioma (PM) and was shown to contribute to increased cell migration and platinum resistance.

Methods: Phosphorylation of YB-1 at position serine 102 was analysed by immunohistochemistry, immunofluorescence and immunoblotting in PM tissue specimens and cell lines. Intracellular localisation experiments involved immunoblotting, transfection of fluorescent protein-tagged YB-1 and confocal imaging.

View Article and Find Full Text PDF

Plants deploy a diverse array of pattern recognition receptors (PRRs), which perceive microbe-associated molecular patterns to activate immune responses. Leucine-rich repeat receptor-like kinase subgroup XII (LRR-RLK-XII) represents one of the largest PRR families owing to lineage-specific diversification. Through bioinformatics and synthetic biology approaches, we characterized LRR-RLK-XIIs from 285 plant species and identified a receptor, "SCORE," that perceives cold shock protein (CSP) peptides.

View Article and Find Full Text PDF

Rainbow trout(Oncorhynchus mykiss) is a typical cold-water fish often threatened by high summer temperatures. Nano-selenium as a feed additive can improve the antioxidant capacity of the body and relieve stress. In this study, different levels of nano-selenium (0, 5 and 10 mg/kg) were added to the feed of rainbow trout to determine the changes in spleen structure and expression of related genes in rainbow trout at the proper temperature (18℃) and heat stress temperature (24℃).

View Article and Find Full Text PDF

HSP90's Function Under Low Temperature Stress.

Biology (Basel)

August 2025

State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.

Molecular chaperones, especially heat shock proteins (HSPs) have vital functions in cells' responses to stress. Here, we cloned and sequenced the complete complementary DNA encoding HSP90 () from the shrimp . The cDNA comprised 3162 bp, including a 2172 bp coding region encoding a 724 amino acid-protein (predicted molecular mass = 83.

View Article and Find Full Text PDF