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The protein encoded by SMPD1 is a lysosomal acid sphingomyelinase that converts sphingomyelin to ceramide. Additionally we are shipping Sphingomyelin phosphodiesterase 1, Acid Lysosomal Antibodies (70) and Sphingomyelin phosphodiesterase 1, Acid Lysosomal Kits (25) and many more products for this protein.
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Human SMPD1 Protein expressed in Baculovirus infected Insect Cells - ABIN2003951
Lansmann, Schuette, Bartelsen, Hoernschemeyer, Linke, Weisgerber, Sandhoff: Human acid sphingomyelinase. in European journal of biochemistry / FEBS 2003
results provide evidence that translocated lysosomal V1 H(+)-ATPase (show ATP6AP1 Proteins) contributes to formation of local acid microenvironment to facilitate activation of ASM and consequent membrane raft(MR) aggregation, forming MR redox signalosomes and mediating redox signaling in coronary endothelial cells
Acid sphingomyelinase activation serves as a triggering mechanism, leading to fusion of membrane proximal lysosomes into lipid rafts clusters on the cell membrane of coronary arterial endothelial cells.
Report lysosomal targeting and trafficking of acid sphingomyelinase to lipid raft platforms in coronary endothelial cells.
ASM is a negative regulator of regulatory T Cell development.
We report on an infant with a new frameshift mutation (c.575dupG) of the SMPD1 gene.
Seven novel mutations (c.518-519insT, c.562_563insC, c.792Gdel, c.949G>A, c.1487_1499delACCGTGTGTACCA, c.1495T>C and c.1670T>C) of the SMPD1 gene were identified in four patients. Only one fetus had two mutations of the SMPD1 gene of amniocytes
although ebeta,5alpha,6beta-triol is more specific than 7-KC, it has been found to be significantly elevated in patients with Niemann-Pick type A, a lysosomal storage disorder caused by mutations in the SMPD1 gene
A comprehensive updated review of already reported and newly identified SMPD1 variants of Niemann-Pick Types A and B disease has been presented. (Review)
a conserved haplotype and shared 280 Kb region around the SMPD1 gene was observed in the patients analyzed, indicating that the variant originated from a common ancestor
ASM activation may be involved in the pathophysiology of Kawasaki disease
These results indicate that increased EGR1 (show EGR1 Proteins)/3 and ASMase expression play an important role in cellular ceramide increase by RSV treatment.
The results of this study suggested that disruptive mutations in SMPD1 constitute a risk factor for parkindon disease.
Inhibition of ASM in diabetic CACs improved membrane fluidity and homing of these cells to damaged retinal vessels. Collectively, these findings indicate that selective modulation of sphingolipid metabolism in BM-derived cell populations in diabetes normalizes the reparative/proinflammatory cell balance and can be explored as a novel therapeutic strategy for treating diabetic retinopathy.
Inhibition of the smpd1 by antidepressants prevents stress-induced phosphorylation/activation of p38K indicating that antidepressants indirectly target p38K via the acid sphingomyelinase/ceramide system.
The reduction of membrane sphingomyelin (SM)is due to transcriptional upregulation of neutral sphingomyelinase (show SMPD2 Proteins) (NSM) through active RhoA (show RHOA Proteins).
Intravenous injection of B16F10 melanoma cells into wild-type mice resulted in multiple lung metastases, while Asm-deficient mice (Smpd1(-/-) mice) were protected from pulmonary tumor spread.
Acid sphingomyelinase deficiency reduces S. aureus-induced lung edema.
Ceramide production in M-CSF (show CSF1R Proteins)-deprived macrophages arises from a combination of ASMase activity and de novo synthesis.
aSMase-deficient mouse is the first example in which microglial lipid inclusions are directly related to a loss of retinal function
ASMase deficiency determined resistance to hepatic steatosis mediated by a high fat diet.
results provide the mechanism for dysferlin-mediated repair of skeletal muscle sarcolemma and identify ASM as a potential therapy for dysferlinopathy
Acid sphingomyelinase (ASM) controls autophagy maturation in smooth muscle cells. ASM maintains smooth muscle cell homeostasis and its contractile phenotype. ASM plays a protective role in smooth muscle dysfunction and atherosclerosis.
The protein encoded by this gene is a lysosomal acid sphingomyelinase that converts sphingomyelin to ceramide. The encoded protein also has phospholipase C activity. Defects in this gene are a cause of Niemann-Pick disease type A (NPA) and Niemann-Pick disease type B (NPB). Multiple transcript variants encoding different isoforms have been identified.
, acid sphingomyelinase
, sphingomyelin phosphodiesterase 1, acid lysosomal (acid sphingomyelinase)
, sphingomyelin phosphodiesterase 1, acid lysosomal
, sphingomyelin phosphodiesterase 1
, sphingomyelin phosphodiesterase-like