| UBIAD1, the synthetase for both Vitamin K2 and Co Q10, which are two important molecules in human body, is not only related to the occurrence and development of many tumors, but also acts as an antioxidant to protect cardiovascular by regulating the cholesterol metabolism directly or indirectly. Meanwhile, the mutation of conservative amino acids in transmembrance domain of UBIAD1 can lead the occurrence of SCCD, a rare genetic disease. More of its physiological and pathological functions are still being found. UBIAD1 is a vital multifunctional protein in organism, and there’s always a heated dispute for its subcellular localization. The existing researches show that the subcellular localizations of UBIAD1 in different cell lines is different.In this essay, we use immunofluorescence staining, expressing fusion plasmid, MTT test, flow cytometry and so on to testify the express distribution and grow inhibition in both normal human cell HEK293 T and tumor cells T24. The results show that, in HEK293 T and T24, the exogenous UBIAD1 protein distributes in both endoplasmic reticulum and golgi apparatus, and the protein aggregates in Golgi apparatus. However, this aggregation in Golgi apparatus for endogenous UBIAD1 is not obvious, but it evenly distribute in endoplasmic reticulum. LAY, from 71 to 73 amino acid in N-terminal of UBIAD1 protein, is the vital sequence for the retention in endoplasmic reticulum. When mutating RPWS, the retention signal of UBIAD1 in golgi apparatus, the mutants don’t diffuse but specifically remain in endoplasmic apparatus. Both wild UBIAD1 and its mutants, whose signal for remaining in endoplasmic reticulum has been mutated, can lead to the growth inhibition of bladder cancer cells T24, but not normal cells HEK293 T. Adding VK2 can obviously promote the growth inhibition of T24 by UBIAD1 mutants, whose retention signal for endoplasmic reticulum is mutated. |
