ABSTRACT
A-kinase anchor protein 12 [AKAP12] is a scaffold protein that participates in mitotic regulation and other signaling processes and probably exerts tumour suppressor function. Acute leukemias are caused by genetic and epigenetic mechanisms involving tumour suppressor genes and oncogenes. Epigenetic regulation plays a key role in the pathogenesis of leukemia. Aberrant DNA methylation patterns are the most frequent molecular alterations detected in AML. Whereas the pathogenetic importance of these changes has begun to emerge, DNA methylation has thus far only played minor role as a biomarker in diagnosis, prognosis prediction and treatment control. The aim of this study was to determine the expression of tumor suppressor gene gravin which belongs to the A kinase anchoring protein family in acute leukaemia patients samples and controls and to explore its possible prognostic importance. In this study, real time quantitative PCR was used to determine gravin gene expression and beta Actin was used as control gene and expression levels were compared with prognostic factors. Gravin gene expression was found to be decreased in 100% of patients as compared with the control group and it was found that there is significant correlation between its expression and laboratory prognostic markers, prognosis and .treatment outcome of acute leukemia patients. Gravin gene expression was found to be decreased in acute leukemias and the degree of its decreased expression has been found to be correlated with poor prognosis
Subject(s)
Acute Disease , Cell Cycle Proteins , Actins/blood , Polymerase Chain Reaction , PrognosisABSTRACT
To analyse the role of native structures of membrane proteins in their structural modifications induced by the elevated intracellular free Ca2+ levels, we have studied the Ca(2+)-mediated effects on membrane skeletal proteins in human erythrocytes that were loaded with Ca2+ using the ionophore A23187 after their pretreatment with the sulphydryl oxidizing agent, diamide. The diamide treatment not only induced polymerization of the major membrane skeletal protein, spectrin, in the erythrocytes, but it also promoted intersubunit crosslinking within the tetramers and dimers of this protein. Loading of these diamide-treated cells with Ca2+ failed to induce significant structural modifications of spectrin as well as polypeptide 4.1, another major membrane skeletal protein, as compared to the erythrocytes that were loaded with Ca2+ without the diamide pretreatment. These results have been interpreted to suggest that the Ca(2+)-induced membrane skeletal protein changes in erythrocytes depend on both the shape and relative orientation of these proteins within the membrane skeleton.