Questions+I'd+like+to+know+the+answer+to+1-19-12


 * Why do normal people have antibodies against their own proteins (if this is actually true)?
 * Kathy mentioned that maybe one can have antibodies against their own proteins, but it doesn't cause any harm unless a threshold is passed.
 * I wonder if it's possible that the immune system can recognize patterns of proteins presented on cells. For example, maybe a cancer cell can express 3 normal self proteins together that would never be expressed together in a normal cell. Does the immune system have the capability of recognizing patterns like this? If it could, the immune system would be smarter than we think it is.
 * I think Kathy mentioned this to me before when she reasoning why can't we depleted all VP30 protein from the ASFV serum. Here is how how I wrote in my thesis: antibodies against conjugated proteins. -Alan
 * I think we are both talking about two different things here. You are talking about recognizing a modified protein from an unmodified one, and I am talking about the immune system recognizing something like 3 normal unmodified proteins that should not be together in one cell. -Kurt
 * Also, can the immune system recognize over-expression or under-expression of a protein? I think so, any over-expressed protein is potentially a threat to our immune system. There should be some established theories about this, we might need to check the immunology book. -Alan
 * Yeah I would think that the immune system can. Like you said, there must be some information about this somewhere like our immunology book. -Kurt
 * I think one reason antibodies could decrease to one epitope in a protein and increase to another epitope in a protein could be that these epitopes are located on more than one protein in the body. The body reuses many protein domains to make different proteins. Therefore, there is a very good possibility that the same protein domain is found in different proteins. Let's say there are antibodies against the GAD diabetes protein. Some antibodies increase in the disease against epitopes in one domain of the GAD protein. However, let's say there is some other protein in the body that the antibodies decrease against in the disease, but the epitope for these antibodies is located in a domain that is also in the GAD protein. In this situation, you would see antibodies increase against some epitopes in GAD and decrease against other epitopes in GAD.
 * Shen mentioned several ideas
 * Perhaps various B cells are undergoing tolerance suppression while others are not
 * A different isotype of antibody could increase in affinity for the epitope, and therefore would not be detected on the array
 * Perhaps the amount of other proteins in the blood change, and these proteins block the peptides.
 * Chronic inflammation causes cancer, but exercise causes inflammation and it is very good for health. Why is this the case?