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Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine.
The enzymes involved in sphingolipid metabolism are expressed abnormally in B cells from lupus-prone mice. TLR signaling induced the abnormal expression of sphingomyelin phosphodiesterase 3 (SMPD3). TLR signaling also induced the transport of SMPD3 from the Golgi apparatus. Furthermore, the dysfunction of SMPD3 enhanced TLR-induced inflammatory response of B cells and macrophages in turn.
SMPD3 in the regulation of the protein vesicular secretory pathway may become a diagnostic target in the etiology of unknown forms of juvenile growth and developmental inhibition.
Study provides evidence that Smpd3 expression in both chondrocytes and osteoblasts is required for normal endochondral bone development.
these results highlight the role of nSMase2 in apoptosis evoked by nutrient starvation that could contribute to the delayed apoptosis of hypertrophic chondrocytes in the growth plate, and emphasize the antiapoptotic properties of HAS2 (show HAS2 Proteins)
nSMase2 activation is required for the development of infection-induced diaphragm calpain activation and muscle weakness.
These results suggest that OTC (show OTC Proteins) is a potent stimulant of nSMase-2 expression and that there may be unanticipated complications of OTC (show OTC Proteins) supplementation.
Src (show SRC Proteins) and p38 mitogen-activated protein kinase (show MAPK14 Proteins) activities are critical for regulating nSMase2 phosphorylation.
Smpd3 was identified as a redox-sensitive enzyme, whose basal activity mediated changes in its oligomeric state.
Data confirms a crucial pro-survival role for SMPD3 during embryonic development.
Smpd3/nSMase2-ceramide-Akt (show AKT1 Proteins) signaling axis negatively regulates BMP-induced chondrocyte maturation.
The enzymes involved in sphingolipid metabolism are expressed abnormally in B cells from SLE patients. TLR signaling induced the abnormal expression of sphingomyelin phosphodiesterase 3 (SMPD3). TLR signaling also induced the transport of SMPD3 from the Golgi apparatus. Furthermore, the dysfunction of SMPD3 enhanced TLR-induced inflammatory response of B cells and macrophages in turn.
ATRA regulates nSMase2 transcriptionally through the retinoic acid receptor-alpha (show RARA Proteins), but this is independent of previously identified transcriptional regulators of nSMase2 (Sp1 (show PSG1 Proteins), Sp3, Runx2 (show RUNX2 Proteins)) and is not through increased promoter activity.
Overexpression of Smpd3 induced cytodifferentiation of HPDL (show HPDL Proteins) cells, which could be suppressed by an inhibitor of its protein product, nSMase2. In addition,Smpd3 harboring a SNP (rs145616324) showed no activity and failed to induce cytodifferentiation of HPDL (show HPDL Proteins) cells. Together, these findings suggest that Smpd3 plays an important role in the osteoblastic differentiation of HPDL (show HPDL Proteins) cells.
low oxLDL concentration triggers sprouting angiogenesis that involves ROS (show ROS1 Proteins)-induced activation of the neutral sphingomyelinase-2/sphingosine kinase-1 (show SPHK1 Proteins) pathway, and is effectively inhibited by GW4869.
nSMase2 is a novel p53 (show TP53 Proteins) target gene, regulated by the DNA damage pathway to induce cell growth arrest.
nSMase2 involvement in cellular processes including inflammatory signaling, exosome generation, cell growth, and apoptosis, which in turn play important roles in pathologies such as cancer metastasis, Alzheimer's disease
SMPD3 plays an important role in the release of microRNAs into extracellular spaces.
The data shows that nSMase3 acts as a signaling nSMase (show SMPD2 Proteins) in skeletal muscle that is essential for TNF (show TNF Proteins)-stimulated oxidant activity.
This is the first report on the critical role of ceramide generated by nSMase2 in stem cell ciliogenesis and differentiation.
This study establishes NSMase2 as a pivotal enzyme in the onset of endothelial endoplasmic reticulum stress-mediated vascular dysfunction.
Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Acts as a regulator of postnatal development and participates in bone and dentin mineralization. Overexpression enhances cell death, suggesting that it may be involved in apoptosis control. May be involved in IL-1-beta-induced JNK activation in hepatocytes. May act as a mediator in transcriptional regulation of NOS2/iNOS via the NF- kappa-B activation under inflammatory conditions.
, neutral sphingomyelinase 2
, neutral sphingomyelinase II
, sphingomyelin phosphodiesterase 3
, confluent 3Y1 cell-associated 1
, confluent 3Y1 cell-associated protein 1
, neutral sphingomyelin phosphodiesterase 3