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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 (zeige HAS2 Proteine)
nSMase2 activation is required for the development of infection-induced diaphragm calpain activation and muscle weakness.
These results suggest that OTC (zeige OTC Proteine) is a potent stimulant of nSMase-2 expression and that there may be unanticipated complications of OTC (zeige OTC Proteine) supplementation.
Src (zeige SRC Proteine) and p38 mitogen-activated protein kinase (zeige MAPK14 Proteine) 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 (zeige AKT1 Proteine) 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 (zeige RARA Proteine), but this is independent of previously identified transcriptional regulators of nSMase2 (Sp1 (zeige PSG1 Proteine), Sp3, Runx2 (zeige RUNX2 Proteine)) and is not through increased promoter activity.
Overexpression of Smpd3 induced cytodifferentiation of HPDL (zeige HPDL Proteine) 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 (zeige HPDL Proteine) cells. Together, these findings suggest that Smpd3 plays an important role in the osteoblastic differentiation of HPDL (zeige HPDL Proteine) cells.
low oxLDL concentration triggers sprouting angiogenesis that involves ROS (zeige ROS1 Proteine)-induced activation of the neutral sphingomyelinase-2/sphingosine kinase-1 (zeige SPHK1 Proteine) pathway, and is effectively inhibited by GW4869.
nSMase2 is a novel p53 (zeige TP53 Proteine) 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 (zeige SMPD2 Proteine) in skeletal muscle that is essential for TNF (zeige TNF Proteine)-stimulated oxidant activity.
This is the first report on the critical role of ceramide generated by nSMase2 in stem cell ciliogenesis and differentiation.
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.
sphingomyelin phosphodiesterase 3, neutral membrane (neutral sphingomyelinase II)
, neutral sphingomyelinase 2
, neutral sphingomyelinase II
, sphingomyelin phosphodiesterase 3
, confluent 3Y1 cell-associated 1
, confluent 3Y1 cell-associated protein 1
, neutral sphingomyelin phosphodiesterase 3