Cell biology related question

Viewing 10 reply threads
  • Author
    Posts
    • #12039
      Nesreena
      Participant

      Hello Biologists.
      This is a question that I thought and read to answer but I feel like it is not that specific 😕
      anyway the question is as follows, you have proteins on a cell membrane, how can you tell that one of them was modified by the same cell and came out of it, while the other will enter for modification and the other might send a signal to that cell? and how can you tell that some of these proteins aren’t related to that cell?
      my tries to answer was that we apply Fluorescence and watch their functions, however, my teacher told me that would be true if the cell is alive. so how could I solve this in case the cell is not functioning or not alive.? I then thought it could be related to the structure of the protein itself, so I am saying that the protein if it is to enter for modification it will not be phosphorylated and so it will bind to some kind of receptor to be phosphorylated and that this can happen for the signaling protein which should be binding to a receptor in order to make the cell respond to it, therefore these kinds of protein will be related to that cell. however other proteins wont have any attachment to that cell. tell me what do you think of my predictions, your critisises are welcome, anytips or predictions are as well.

      ——–
      one of my friends told me about the bioinformatics but I do not know about it I have some books that do not have this technique, if you think it might help could you give me a good Ebook that I can read about it. Thank you

    • #93841
      JackBean
      Participant

      So, you wish to determine, whether the protein stays in the cell, where is it produced or whether it passes to another cell?

    • #93860
      Nesreena
      Participant

      Hi there Jackbean, thank you for replying. Yes this is it

    • #93871
      JackBean
      Participant

      So, I guess, that if the protein travels from one cell to another, you should found it also outside of the cell, shouldn’t you?
      Or, theoretically, you could pick up one cell and add it to anothers under a microscope a wath, what will happen, whether the fluorescence stays in one cell or spread around.

      But I don’t have experiences with these, so there is probably something more elegant 🙂

    • #93900
      kolean
      Participant

      I would also look at the glysolation of the protein also: http://www.biomedcentral.com/1471-2105/9/500

      I just remember that depending on what the protein’s function (and destination) is to be, the Golgi apparatus will modify the protein, usually by glycosylation and phosphorylation, for its purpose.

    • #93904
      Nesreena
      Participant

      Hello,
      Thanks vor the replys guys:) appreciate it really. That is it, tomorrow I am going to tell the answer, I hafe a good feeling about my answer which is " the affinity between ligands=proteins in this case and the receptor on that cell" …tell me what do you think untill tomorrow when I’ll be back and tell you what happened with my teacher:) …I hope I got it right..

    • #93914
      JackBean
      Participant
      quote kolean:

      I would also look at the glysolation of the protein also: http://www.biomedcentral.com/1471-2105/9/500

      I just remember that depending on what the protein’s function (and destination) is to be, the Golgi apparatus will modify the protein, usually by glycosylation and phosphorylation, for its purpose.

      Glycosylation does not have to mean export from cell 😉 Also intracellular proteins can be glycosylated
      And phosphorylation, in my opinion, is always only on intracellular proteins, isn’t it?

    • #93948
      kolean
      Participant

      No, it does not have to mean export from a cell. But there are certain patterns to the glycosylation of a protein that can tell you if the protein is for export or import (location), signaling or binding (function), and structure(function).
      Glycobiology has become increasingly popular as diseases are becoming evident from mutations in gylcosylation of proteins.
      Personally, I did not know exactly what info this person was looking for. I just put in some info of my own that pertained to proteins and identification.

    • #93985
      JackBean
      Participant

      BTW if is protein glycosylated and once exported, can it be imported again?
      Maybe some signal predictions could help more 😉

    • #94012
      kolean
      Participant

      If the protein is glycosylated and enclosed in a vesicle that is bound for exocytosis. Once exported, then the glycosylated protein is free to interact with any signal it is receptive to, and can be imported. Is that what you mean?

    • #94019
      JackBean
      Participant

      Kind of

Viewing 10 reply threads
  • You must be logged in to reply to this topic.