Disease relevance of Sgpl1

• Sphingosine-1-phosphate lyase is involved in the differentiation of F9 embryonal carcinoma cells to primitive endoderm [1].
• Inhibition of C. elegans sphingosine phosphate lyase expression by RNA interference causes accumulation of phosphorylated and unphosphorylated long-chain bases and leads to poor feeding, delayed growth, reproductive abnormalities, and intestinal damage similar to the effects seen with exposure to Bacillus thuringiensis toxin [2].
• Sphingosine-1-phosphate lyase potentiates apoptosis via p53- and p38-dependent pathways and is down-regulated in colon cancer [3].
• In contrast, nonactivated nylon wool-nonadherent spleen cells ( NWT ) or unfractionated spleen cells (Spl) and cells of the P815 mastocytoma, the Meth A fibrosarcoma, and the T cell lymphomas Ly 5178 Eb and ESb did not stimulate cytotoxic responses at these cell concentrations [4].
• Knocking-down of Spl expression by small inhibitory RNA led to decreased IGF-IR expression and attenuated growth and metastasis of gastric cancer cells [5].

High impact information on Sgpl1

• In contrast, the responses of lymph node (LN) and spleen (Spl) cells to this mitogen were shown by the same techniques to rely upon resident populations of mature T lymphocytes in these peripheral lymphoid organs [6].
• Lysis of B cells with anti-mouse gamma globulin or anti-mouse IgM antisera had no significant effect on either Spl or BM blastogenesis in response to this lectin [6].
• One of these binding sites probably interacts with Spl, while the second interacts with an uncharacterized protein [7].
• A vibrissa-related pattern began to emerge in trigeminal nucleus principalis and subnucleus interpolaris (Spl) by embryonic day (E-) 19 and appeared fully developed by the day of birth (P-0) [8].
• The immune modulator FTY720 inhibits sphingosine-1-phosphate lyase activity [9].

Biological context of Sgpl1

• Our results show that sphingosine phosphate lyase is an essential gene in C. elegans and suggest that the sphingolipid degradative pathway plays a conserved role in regulating animal development [2].
• Promoter analysis indicates tissue-specific and developmental regulation of sphingosine phosphate lyase gene expression [2].
• Identification of an Spl-like element within the immunoglobulin kappa 3' enhancer necessary for maximal enhancer activity [10].
• One region, found immediately 5' to the mouse and human ACE genes, is a GC rich segment that contains a "TATA box" and several potential Spl binding sites [11].
• The promoter region was found to lack TATA and CAAT boxes but contains Spl binding sites, which are indicators of typical housekeeping genes [12].

Anatomical context of Sgpl1

• Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5'-phosphate binding domain exposed to the cytosol [13].
• Cytolysis of T cells with anti-theta (anti-Thy 1), anti-thymocyte, or anti-brain antisera abolished the PHA responses of LN and Spl, but had no appreciable effect on the BM PHA response [6].
• Proliferative responses of thymus and lymph node cells from anti-mu suppressed mice to RCS, mitomycin-treated syngeneic spleen cells (M. Spl.) Con A, and PHA were entirely normal [14].
• In contrast, none of the vehicle-treated allogeneic BM/Spl chimeras survived more than 43 days after bone marrow transplantation (BMT) [15].
• Mitogen-induced proliferation of rabbit lymphocytes from the thymus (Thy), spleen (Spl) and lymph node (LN) was measured by [3H]thymidine incorporation [16].

Associations of Sgpl1 with chemical compounds

• Intracellular levels of sphingosine 1-phosphate are tightly regulated by the actions of sphingosine kinase, which is responsible for its synthesis and sphingosine-1-phosphate phosphatase and sphingosine phosphate lyase, the two enzymes responsible for its catabolism [2].
• Sphingosine-phosphate lyase enhances stress-induced ceramide generation and apoptosis [17].
• But at high concentrations GT11 provoked an accumulation of sphingosine-1-phosphate and especially of dihydrosphingosine-1-phosphate, suggesting a decreased activity of sphingosine-1-phosphate lyase [18].

References