ABSTRACT
Prolin-rich Akt substrate of 40 kD (PRAS40) is firstly identified as a partner of 14-3-3 protein and a substrate of Akt kinase by Roth et al in 2003. Accumulated evidence shows that PRAS40 is mainly activated by phosphorylate modification at different sites. PRAS40 may be involved in various of signaling pathways, such as mammalian target of rapamycin complex 1 (mTORC1), protein kinase B (Akt), NF-κB and ribosomal protein L11 (RPL11) etc, which can regulate cell proliferation, senescence, autophagy, apoptosis and exosome secretion.
Subject(s)
Humans , Adaptor Proteins, Signal Transducing , Metabolism , Mechanistic Target of Rapamycin Complex 1 , Metabolism , Phosphorylation , Proto-Oncogene Proteins c-akt , Metabolism , TOR Serine-Threonine Kinases , MetabolismABSTRACT
OBJECTIVE@#To investigate the ubiquitin expression in laryngeal squamous cell carcinoma (LSCC) whether along with local lymph node metastasis, and further study its correlation with local lymph node metastasis and other clinicopathological parameters in laryngeal squamous cell carcinoma.@*METHOD@#We detected the different expression level of ubiquitin in paraffin specimens between 19 cases of LSCC associated with cervical lymph node metastasis LSCC(N+) and 20 cases of LSCC not associated with cervical lymph node metastasis LSCC(N-) by immunohistochemical staining combined with stereology image analysis system. Statistics were analyzed by student test, variance analysis and ROC curve.@*RESULT@#Ubiquitin expression in LSCC(N+) was significantly higher than LSCC(N-) (P < 0.01); their expression level was not correlated with age,history of tobacco, alcohol addiction, clinical stage and primary site,etc.@*CONCLUSION@#Ubiquitin was significantly up-expressed in LSCC(N+) than ILSCC (N-), which may imply that it is one of the important elements in mechanism of lymph node metastasis in LSCC.