CYB5B

Last update 08 May 2025

Basic Info

Synonyms

CYB5-M, CYB5B, CYB5M

+ [3]

Introduction

Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.

100 Clinical Results associated with CYB5B

100 Translational Medicine associated with CYB5B

0 Patents (Medical) associated with CYB5B

Literatures (Medical) associated with CYB5B

01 Apr 2025·Oral Diseases

Benzylurea Protects hPDLFs Against LPS‐Induced Mitochondrial Dysfunction Through MTCH2

Article

Author: Wang, Jiyun ; Chang, Hong ; Liu, Li ; Yang, Pengfei ; Bai, Jing ; Hui, Xuancheng ; Yin, Dong ; Fan, Junheng

ABSTRACTObjectiveThe aim of this study is to explore the mechanism of benzylurea in the inflammatory injury of human periodontal ligament fibroblasts (hPDLFs).MethodsAn inflammation model of hPDLFs was established using LPS. Nuclear transport of nuclear transcription factor‐κB (NF‐κB), secretion of cytokines, and the morphology and distribution of F‐actin were determined. Mitochondrial function was assessed by measuring mitochondrial membrane potential (MMP), mitochondrial permeability transition pore (mPTP), and reactive oxygen species (ROS) levels. The expression of mitochondrial carrier homolog 2 (MTCH2) and Cytochrome b5 type B (CYB5B) was detected.ResultsBenzylurea alleviated the effects of lipopolysaccharide (LPS) on the proliferation and apoptosis of hPDLFs. It reduced the release of inflammatory cytokines and inhibited NF‐κB nuclear translocation. Benzylurea improved mitochondrial function by regulating MMP and preventing excessive mPTP opening. Furthermore, LPS elevated the expression of MTCH2 and reduced the expression of CYB5B in hPDLFs. However, these effects can be inhibited by benzylurea. The altered expression of MTCH2 directly affected CYB5B expression, the release of inflammatory cytokines, and the activation of nuclear translocation of NF‐κB.ConclusionCYB5B may act as an effector of MTCH2, with benzylurea enhancing mitochondrial function and protecting hPDLFs from LPS‐induced injury through MTCH2.

01 Nov 2024·Cell Reports

Defects in CYB5A and CYB5B impact sterol-C4 oxidation in cholesterol biosynthesis and demonstrate regulatory roles of dimethyl sterols

Article

Author: Zhu, Wen-Zhuo ; Ma, Mei-Yan ; Deng, Gang ; Jiang, Lu-Yi ; Liu, Yuan-Bin ; Guo, Lin ; Li, Wei-Hui ; Song, Bao-Liang ; Sun, Ming ; Zhao, Xiaolu

Cytochrome b5 (CYB5) is a hemoprotein crucial for electron transfer to oxygenases. Although microsomal CYB5A is required for sterol C4-demethylation in vitro, cholesterol biosynthesis remains intact in Cyb5a knockout mice. Here, we show that knockout of mitochondrial CYB5B, rather than CYB5A, blocks cholesterol biosynthesis at the sterol-C4 oxidation step in HeLa cells, causing an accumulation of testis meiosis-activating sterol (T-MAS) and dihydro-T-MAS. Surprisingly, liver-specific Cyb5b knockout (L-Cyb5b^-/-) mice exhibit normal cholesterol metabolism. Further knockdown of Cyb5a in L-Cyb5b^-/- (L-Cyb5b^-/-/short hairpin [sh]Cyb5a) mice leads to a marked accumulation of T-MAS and dihydro-T-MAS, indicating that either CYB5A or CYB5B is required for sterol C4-demethylation. The L-Cyb5b^-/-/shCyb5a mice are largely normal, with lower sterol regulatory element-binding protein (SREBP)-target gene expression during refeeding and higher liver triglyceride levels while fasting, as T-MAS and dihydro-T-MAS inhibit the SREBP pathway and activate the PPARγ pathway. In summary, CYB5A and CYB5B compensate for sterol C4-demethylation, and T-MAS and dihydro-T-MAS can modulate the SREBP and PPARγ pathways.

01 Apr 2024·Chemosphere

Actinomycetota, a central constituent microbe during long-term exposure to diazinon, an organophosphorus insecticide

Article

Author: Kim, Songhwa ; Cho, Gyeongjun ; Riu, Myoungjoo ; Song, Jaekyeong ; Jeon, Je-Seung

Microbial biodegradation is a primary pesticide remediation pathway. Despite diazinon is one of the most frequently used organophosphate insecticides worldwide, its effect on soil microbial community remains obscure. We hypothesize that diazinon exposure reshapes microbial community, among them increased microbes may play a crucial role in diazinon degradation. To investigate this, we collected soil from an organic farming environment, introduced diazinon, cultivated it in a greenhouse, and then assessed its effects on soil microbiomes at three distinct time points: 20, 40, and 270 days after treatment (DAT). Results from HPLC showed that the level of diazinon was gradually degraded by 98.8% at 270 DAT when compared with day zero, whereas 16S rRNA gene analysis exhibited a significant reduction in the bacterial diversity, especially at the early two time points, indicating that diazinon may exert selection pressure to the bacteria community. Here, the relative abundance of phylum Actinomycetota increased at 20 and 40 DATs. In addition, the bacterial functional gene profile employing PICRUSt2 prediction also revealed that diazinon exposure induced the genomic function related to xenobiotics biodegradation and metabolism in soil, such as CYB5B, hpaC, acrR, and ppkA. To validate if bacterial function is caused by increased relative abundance in diazinon enriched soil, further bacteria isolation resulted in obtaining 25 diazinon degradation strains out of 103 isolates. Notably, more than 70% (18 out of 25) isolates are identified as phylum Actinomycetota, which empirically confirms and correlates microbiome and PICRUSt2 results. In conclusion, this study provides comprehensive information from microbiome analysis to obtaining several bacteria isolates responsible for diazinon degradation, revealing that the phylum Actinomycetota is as a key taxon that facilitates microbial biodegradation in diazinon spoiled soil. This finding may assist in developing a strategy for microbial detoxification of diazinon, such as using an Actinomycetota rich synthetic community (SynCom).

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

CYB5B

Basic Info

Related

Analysis