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Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. Additionally we are shipping serine Palmitoyltransferase, Long Chain Base Subunit 1 Antibodies (108) and serine Palmitoyltransferase, Long Chain Base Subunit 1 Kits (4) and many more products for this protein.
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Findings indicate that AtORM1 and AtORM2 mediation of serine palmitoyltransferase (SPT) activity differentially regulates functionally distinct ceramide synthase activities as part of a broader sphingolipid homeostatic regulatory network.
The roles of the LCB2a (show SPTLC2 Proteins) and LCB2b (show SPTLC3 Proteins) subunits in sphingolipid biosyntesis in A. thaliana were studied.
Therefore, SPT (show AGXT Proteins) may be an attractive therapeutic anti-cancer drug target for which compound-2 may be a promising new drug.
Hereditary sensory and autonomic neuropathy type 1 mutations in SPTLC1 have distinct biochemical properties, which allowed for the prediction of the clinical symptoms on the basis of the plasma sphingoid base profile.
This study describe aberrant morphology of SPTLC1C133W Dorsal Root Ganglia characterized by increased neurite growth, branching, and expression of p-ERM (show ETV5 Proteins) at neuronal growth cones.
A novel SPTLC2 (show SPTLC2 Proteins)-S384F variant in 2 unrelated HSAN1 families resulted in elevated plasma 1-deoxySL levels. Expression of this mutant in HEK293 cells increased 1-deoxySL formation. The substrate specificity is affected by phosphorylation at this position.
Therefore, Ser331 in SPTLC1 is a crucial amino acid, which characterizes the Hereditary sensory and autonomic neuropathy type I phenotype
SPTLC1 mutations cause mitochondrial abnormalities and ER stress in HSN1 cells.
Endoplasmic reticulum-resident human protein serine palmitoyltransferase long chain-1 (SPTLC1) is phosphorylated at Tyr (show TYR Proteins)(164) by the tyrosine kinase ABL.
The p.CYS133Trp mutation in SPTLC1 is the most common cause of hereditary and autonomic neuropathy in the United Kingdom population.
SPTLC1 mutations p.S331F and p.A352V result in a reduction of serine palmitoyltransferase activity in vitro and are associated with increased levels of the deoxysphingoid in patients' plasma samples.
Hereditary sensory neuropathy type 1 is caused by a gain of function mutation in SPTLC1 which causes the accumulation of two neurotoxic sphingolipids
mice with an adipocyte-specific deletion of Sptlc1 show that de novo sphingolipid biosynthesis is required for adipocyte cell viability and normal metabolic function and that reduced de novo sphingolipid biosynthesis within adipocytes is associated with adipocyte death, adipose tissue remodeling, and metabolic dysfunction
Data suggest that overexpression of serine palmitoyltransferase (Sptlc1, serine palmitoyltransferase long chain base subunit 1) to elevate de novo sphingolipid biosynthesis induces autophagy in the liver.
Both Sptlc1 and Sptlc2 (show SPTLC2 Proteins) interactions are necessary for Serine palmitoyl-CoA transferase (SPT (show AGXT Proteins)) activity in vivo and SPT (show AGXT Proteins) activity directly influences plasma sphingolipid levels
The expression and activities of SPT (show AGXT Proteins) in mouse liver increased significantly following fumonisin B1 treatment
Physical interaction of ABCA1 (show ABCA1 Proteins) and SPTLC1 results in reduction of ABCA1 (show ABCA1 Proteins) activity and that inhibition of this interaction produces enhanced cholesterol efflux.
Sptlc1 deficient mice absorb less cholesterol.
Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl-CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. The product of this gene is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in this gene were identified in patients with hereditary sensory neuropathy type 1. Alternatively spliced variants encoding different isoforms have been identified.
Serine palmitoyltransferase 1
, LCB 1
, SPT 1
, long chain base biosynthesis protein 1
, serine C-palmitoyltransferase
, serine palmitoyltransferase 1
, serine-palmitoyl-CoA transferase 1
, serine palmitoyltransferase subunit 1
, Long chain base biosynthesis protein 1
, Serine-palmitoyl-CoA transferase 1
, serine palmitoyltransferase LCB1 subunit