Studies On The Distribution Of The Heart Development Related TMP3Protein In Cardiomyocytes

We have been cloned DNA length of zebrafish TMP3in lab, and it proved TMP3is a membrane protein, expressed highly in heart,when knock down TMP3, it will cause cardiac anomalies. At the same time we have prove TMP3with transporters TMPA4interactions. By separating membrane, nuclear, qualitative protein CO-IP experiment, we find it happen in the cytoplasm and nucleus, prompt TMP3protein into the nucleus, the process that its into the nuclear may require TMPA4assistance.Bioinformatics analysis showed that the immune genes encoding proteins size which TMP3mark is about35kd. Immune imprinting experiments show that the size is about57kd, TMP3protein. We speculated that TMP3as membrane proteins may increase the size of the protein through some modification effect. We use adult zebrafish heart, extract the cytoplasm, cell nucleus and cell membrane proteins respectively, detect TMP3protein expression of the distribution. The experimental results show that is35kd and57kd TMP3protein in the cytoplasm and cell membrane, the size of the nucleus of TMP3protein is57kd. Then, we further study the TMP3protein in the distribution of myocardial cells.However, there are often hitches in the process of explicit TMP3other specific bands show. We analyzed amino acid sequence of the TMP3protein size is about35kd, and speculate the modification after translation increases the protein molecular mass, often can up tp57kd. Sometimes accidentally show the35kd and57kd two groups of specific bands specifically. This further evidence we speculate. Moreover, it is interesting to note that the results of the analysis found that cell membrane is the brightest at57kd, the nucleus, cytoplasm is the weakest. And TMP expresses the35kd protein is just the opposite, that is the brightest expressed in the cytoplasm, cell nucleus, expressed in the cell membrane is weakest. The complementary relationship between the above may not be a coincidence, may be a specific modification.Our experimental results show that the protein glycosylation associated with changes of the size of the protein. Bioinformatics analysis found that human TMP3proteins contain a glycosylation site, we built plasmid which TMP3glycosylation sites mutation, transfection H9C2cell immune mark analysis, the size of the test results show that TMP3protein is57kd, TMP3protein changes the size of the relationship between glycosylation is under study.Studies show that the type of protein is associated with the change of protein size, protein size will increase about11kdafter modification of SUMO, this could be another direction in our research. TMP3protein type prediction analysis shows, TMP3may contain a protein sequence to a number of SUMO modification sites. About TMP3protein size changes with the type of relationship is under study.