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SPTLC2 encodes a long chain base subunit of serine palmitoyltransferase. Additionally we are shipping serine Palmitoyltransferase, Long Chain Base Subunit 2 Antibodies (82) and serine Palmitoyltransferase, Long Chain Base Subunit 2 Kits (7) and many more products for this protein.
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2 families had late-onset autosomal dominant HSAN1C caused by a new variant in SPTLC2, c.547C>T, p.(Arg183Trp). The variant changed a conserved amino acid.
The activities of the hLCB2a mutants were measured in the presence of ssSPTa and ssSPTb and was found that all decrease enzyme activity.
Mutations in SPTLC2 are associated with increased deoxySL formation causing hereditary sensory and autonomic neuropathy type 1 (HSANI) in a familial study.
Mutations in the SPTLC2 subunit of serine palmitoyltransferase cause hereditary sensory and autonomic neuropathy type I.
results suggest that SPTLC2 mutations are not a common cause for genetic sensory neuropathies.
Results suggest that functional serine palmitoyltransferase is not a dimer, but a higher organized complex, composed of three distinct subunits (SPTLC1 (show SPTLC1 Proteins), SPTLC2 and SPTLC3 (show SPTLC3 Proteins)) with a molecular mass of 480 kDa.
discovery of 2 proteins, ssSPTa and ssSPTb, which each interacts with both hLCB1 (show SPTLC1 Proteins) and hLCB2, suggesting that there are 4 distinct human SPT (show AGXT Proteins) isozymes.
The expression of SPT2 was stronger in vascular smooth muscle cells and neointima of carotid arteries from knock-out mice compared to wild-type.
Data suggest that overexpression of serine palmitoyltransferase (Sptlc1 (show SPTLC1 Proteins) and Sptlc2, serine palmitoyltransferase long chain base subunit 1 (show SPTLC1 Proteins)/2) to elevate de novo sphingolipid biosynthesis induces autophagy in the liver.
SPTLC2 knockout mice showed decreased ceramide levels in the epidermis, which impaired water-holding capacity and barrier function.
Ldlr (show LDLR Proteins) gene knockout mice with myeloid cell-specific Sptlc2 haploinsufficiency exhibited significantly less atherosclerosis than controls.
Data show that LCAT (show LCAT Proteins) activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2)+/- and sphingomyelin synthase 2 (Sms2 (show SGMS2 Proteins))-/- mice, but markedly lower in ApoE (show APOE Proteins)-/- and Ldlr (show LDLR Proteins)-/- mice.
results suggest that Sptlc2-mediated de novo ceramide synthesis is an essential source of C18 (show BBS9 Proteins):0 and very long chain, but not of shorter chain, ceramides in the heart
Inflammatory response elicited by lipopolysaccharide increases serine palmitoyltransferase activity via upregulation of Sptlc2 in macrophages.
Deficiency of Sptlc2 induces necrotic lesions in gastrointestinal cells followed by atrophic change of the tissue in short term.
Both Sptlc1 (show SPTLC1 Proteins) and Sptlc2 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.
This gene encodes a long chain base subunit of serine palmitoyltransferase. Serine palmitoyltransferase, which consists of two different subunits, is the key enzyme in sphingolipid biosynthesis. It catalyzes the pyridoxal-5-prime-phosphate-dependent condensation of L-serine and palmitoyl-CoA to 3-oxosphinganine. Mutations in this gene were identified in patients with hereditary sensory neuropathy type I.
, SPT 2
, long chain base biosynthesis protein 2a
, serine palmitoyltransferase 2
, serine palmitoyltransferase, subunit II
, serine-palmitoyl-CoA transferase 2
, serine palmitoyltransferase, long chain base subunit 2
, serine palmitoyltransferase 2-like
, long chain base biosynthesis protein 2
, protein-O-mannosyltransferase 2
, Long chain base biosynthesis protein 2
, Long chain base biosynthesis protein 2a
, Serine-palmitoyl-CoA transferase 2