Background:p53 gene mutations are associated with human tumors, and are among the most common genetic abnormalities. To understand the relationship between p53 mutations and glycine decarboxylase (GLDC) expression in B cell lymphoma, we established B cell lymphoma animal models to study GLDC expression in B cell lymphoma mice. Materials and Methods: Based on immunohistochemical staining results, BALB/c nude mice were divided into a p53 protein-positive group and a p53 protein-negative group. GLDC mRNA expression was determined by real-time polymerase chain reaction, and GLDC protein expression was determined by Western blot. We designed a GLDC-specific interference fragment siRNA-transfected human B cell lymphoma cell line (Raji) to establish a B cell lymphoma animal model. Results: The results showed both GLDC mRNA and protein expression increased in the B cell lymphoma tissue of the p53 protein-positive group compared with the p53 protein-negative group. The proliferation ability of GLDC siRNA-transfected cells decreased significantly compared with the negative-control siRNA group and the blank control group (p < 0.05), which showed that the GLDC gene can promote cell proliferation in p53-mutated B cell lymphoma. Conclusion: These studies support a direct relationship between p53 mutations and GLDC expression in B cell lymphoma. GLDC can induce dramatic changes in glycolysis and glycine/serine metabolism, leading to changes in pyrimidine metabolism and tumor development.
Calcium-dependent synaptic vesicle exocytosis is mediated by SNARE complex formation. The transition from the Munc18-1/syntaxin-1 complex to the SNARE complex is catalyzed by the Munc13-1 MUN domain and involves at least two conformational changes: opening of the syntaxin-1 linker region and extension of Munc18-1 domain 3a. However, the relationship and the action order of the two conformational changes remain not fully understood. Here, our data show that an open conformation in the syntaxin-1 linker region can bypass the requirement of the MUN NF sequence. In addition, an extended state of Munc18-1 domain 3a can compensate the role of the syntaxin-1 RI sequence. Altogether, the current data strongly support our previous notion that opening of the syntaxin-1 linker region by Munc13-1 is a key step to initiate SNARE complex assembly, and consequently, Munc18-1 domain 3a can extend its conformation to serve as a template for association of synaptobrevin-2 and syntaxin-1.
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