Summary
As we all know that the glycosylation of proteins is a very important process for modifying proteins. It can regulate the function of proteins. Here we will introduce a new method to detect the proteins glycosylation sites.
N-terminus linked with glycosylation is an important biological process posttranslational modification. But now the glycosylated protein found is not much. Here we are selecting a method---filter aided sample preparation (FASP). Whereby glycosylated polypeptides can be enriched to filter paper containing lectins, and then using high-precision mass spectrometry found 6367 glycosylation sites from four mice tissues and 2352 plasma proteins. And the amount among these sites take 74% of 830 glycosylation sites, which were found with the help of Swissport server. And other 5753 sites are the first time to be discovered. These sites are presented with "N- P- [S | T] -!! P (P is not proline!)" and some rare or non-conserved sequence motif NXC.
According to the FASP and subcellular glycosylation sites, we can find that these sites generally toward to the extracellular domain or the ER lumen, Golgi apparatus, lysosomes or peroxisomes. Those proteins, which are connecting with the specific organ function, development or disease-related aspect, have too many glycosylation sites.
This study found contributed a lot to the proteomics field. Because, its result will help people understand the physiological and biochemical processes in the human body. In addition, it is also working well in studying disease mechanisms.
Scientists have been studying on the cell's proteins modification, which sites are associated with diseases, such as Alzheimer-related protein glycosylation. We have found that the N- glycosylation plays a very important role in the development of Alzheimer’s. So this research result has a profound learning about the diseases mechanisms.
This is a new method for Glycosylation Analysis of Protein. We believe that this will affect the proteomics field a lot.
As we all know that the glycosylation of proteins is a very important process for modifying proteins. It can regulate the function of proteins. Here we will introduce a new method to detect the proteins glycosylation sites.
N-terminus linked with glycosylation is an important biological process posttranslational modification. But now the glycosylated protein found is not much. Here we are selecting a method---filter aided sample preparation (FASP). Whereby glycosylated polypeptides can be enriched to filter paper containing lectins, and then using high-precision mass spectrometry found 6367 glycosylation sites from four mice tissues and 2352 plasma proteins. And the amount among these sites take 74% of 830 glycosylation sites, which were found with the help of Swissport server. And other 5753 sites are the first time to be discovered. These sites are presented with "N- P- [S | T] -!! P (P is not proline!)" and some rare or non-conserved sequence motif NXC.
According to the FASP and subcellular glycosylation sites, we can find that these sites generally toward to the extracellular domain or the ER lumen, Golgi apparatus, lysosomes or peroxisomes. Those proteins, which are connecting with the specific organ function, development or disease-related aspect, have too many glycosylation sites.
This study found contributed a lot to the proteomics field. Because, its result will help people understand the physiological and biochemical processes in the human body. In addition, it is also working well in studying disease mechanisms.
Scientists have been studying on the cell's proteins modification, which sites are associated with diseases, such as Alzheimer-related protein glycosylation. We have found that the N- glycosylation plays a very important role in the development of Alzheimer’s. So this research result has a profound learning about the diseases mechanisms.
This is a new method for Glycosylation Analysis of Protein. We believe that this will affect the proteomics field a lot.