CPVL

Last update 23 Jan 2025

Basic Info

Synonyms

carboxypeptidase vitellogenic like, carboxypeptidase WUG, carboxypeptidase, vitellogenic-like

+ [7]

Introduction

May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation.

100 Clinical Results associated with CPVL

100 Translational Medicine associated with CPVL

0 Patents (Medical) associated with CPVL

598

Literatures (Medical) associated with CPVL

01 Mar 2025·International Journal of Biological Macromolecules

SCPL48 regulates the vessel cell programmed cell death during xylem development in Arabidopsis thaliana

Article

Author: Lu, Hai ; Sun, Leiqian ; Xu, Yaoming ; Li, Hui ; Fan, Yawei ; Sun, Yu ; Shen, Mengxiao ; Zhang, Chong

Secondary cell wall (SCW) deposition is tightly coordinated with programmed cell death (PCD) during xylem development and plays a crucial role in plant stress responses. In this study, we characterized a serine carboxypeptidase-like gene, SCPL48, which exhibits xylem cell-specific expression patterns in stem xylem during vascular development. The scpl48 plants exhibited reduced stem xylem cell numbers, particularly vessel cells, accompanied by delayed organelle degradation during PCD and increased secondary wall thickness in xylem vessel cells. In contrast, SCPL48 overexpression resulted in increased vessel cell abundance and accelerated degradation of vessel cell contents, suggesting its critical role in xylem vessel cell differentiation. Notably, SCPL48 expression was significantly up-regulated in response to ABA treatment and drought stress, with SCPL48 overexpression lines demonstrating enhanced drought resistance. Further molecular analyses revealed that SCPL48 was directly targeted and transcriptionally activated by key SCW regulators VND6, and MYB46. Furthermore, the expression of PCD-related protease genes, including XCP1, XSP1, RNS3, MC9, γVPE, and CEP1, showed compensatory changes in both scpl48 mutants and SCPL48 overexpression lines. Collectively, our findings demonstrate that SCPL48 functions as a key regulator in xylem vessel cell differentiation, PCD and drought stress responses.

07 Jan 2025·Proceedings of the National Academy of Sciences

VCP controls KCC2 degradation through FAF1 recruitment and accelerates emergence from anesthesia

Article

Author: Chen, Peng ; Song, Xue-Jun ; Liu, Yuexin ; Hu, Jiang-Jian ; Cao, Boxu

Ubiquitin-proteasomal degradation of K + /Cl − cotransporter 2 (KCC2) in the ventral posteromedial nucleus (VPM) has been demonstrated to serve as a common mechanism by which the brain emerges from anesthesia and regains consciousness. Ubiquitin-proteasomal degradation of KCC2 during anesthesia is driven by E3 ligase Fbxl4. However, the mechanism by which ubiquitinated KCC2 is targeted to the proteasome has not been elucidated. We report in cultured neuro-2a cells that the valosin-containing protein (VCP) transported ubiquitinated KCC2 to the proteasome and in mice in vivo experiments that inhibition of VCP restored KCC2 expression in the VPM and enhanced the effects of anesthesia. In cultured neuro-2a cells, propofol-induced degradation of KCC2 was inhibited by VCP inhibitor DBeQ and VCP knockout plasmid sgRNA(VCP). Propofol-induced enhanced interaction between VCP and KCC2 was inhibited by knockout of Fbxl4 or Fas-associated factor 1 (FAF1). In in vivo studies, pharmacological or genetic inhibition of VCP in the VPM significantly prevented KCC2 degradation and enhanced propofol anesthesia; these effects were abrogated by a KCC2 antagonist VU0463271. These results demonstrate that the VCP controls ubiquitin-proteasomal degradation of KCC2 dependent on FAF1 recruitment and serves as a mechanism for the ubiquitin-proteasomal degradation of KCC2, which is responsible for the subsequent emergence from anesthesia.

01 Jan 2025·Histology and histopathology

NRF3 suppresses the metastasis of triple-negative breast cancer cells by inhibiting ERK activation in a ROS-dependent manner.

Article

Author: Zheng, Zhibao ; Li, Jin ; Pan, Yue ; Lin, Bangyi ; Chen, Qi ; Zheng, Chenhui

PURPOSEOur previous study demonstrated that NRF3 (NFE2L3, Nuclear Factor-erythroid 2-related factor 3) could suppress cell metastasis and proliferation in breast cancer. In this study, we investigated the mechanisms underlying its function in breast cancer.METHODSIn the present study, NRF3 expression and its clinical characteristics in breast cancer were analyzed using public datasets and clinical specimens. After breast cancer cells were overexpressed NRF3, FACS was used to detect the intracellular ROS levels. The migration and invasion activities of NRF3-ectopic expressed breast cancer cells were determined by transwell assay. To validate the role of ROS/ERK axis in the inhibitory effect of NRF3 in cell metastasis, ROS scavenger NAC was also included.RESULTSWe found that NRF3 mRNA was highly expressed, while NRF3 protein was extremely lowly expressed in breast cancer tissues compared with their normal counterparts, and low level NRF3 was associated with poorer prognosis in patients with triple negative breast cancer (TNBC). More interestingly, overexpression of NRF3 protein significantly increased cellular ROS production and dramatically decreased p-ERK level and cell migration in TNBC cells. Mechanistically, NRF3 protein was found to be mutually regulated by valosin-containing protein (VCP). Strikingly, VCP-knockdown dramatically increased NRF3 protein expression, but NRF3-knockin also decreased VCP expression in return. Moreover, antioxidant NAC treatment effectively increased the level of p-ERK and VCP expression, as well as cell migration and invasion abilities of TNBC cells.CONCLUSIONNRF3, a tumor suppressor downregulated by VCP, could attenuate cell metastasis in TNBC cells by increasing cellular ROS accumulation and subsequently inhibiting the ERK phosphorylation.

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