In vivo sulfation of the contact site A glycoprotein of Dictyostelium discoideum.

摘要: Abstract During the development of Dictyostelium discoideum from growth phase to aggregation stage, a glycoprotein with an apparent mol. wt. 80 kd is known be expressed on cell surface. This glycoprotein, referred as contact site A, has been implicated in formation species-specific, EDTA-stable contacts aggregating cells. When developing cells were labeled vivo [35S]sulfate, 80-kd was found most prominently sulfated protein. Another strongly protein had 130 and was, like developmentally regulated associated particulate fraction The [35S]sulfate incorporated into 130-kd proteins not present tyrosine-O-sulfate, modified amino acid many mammalian D. incubated presence tunicamycin, inhibitor N-glycosylation, produced 66-kd that reacted monoclonal antibodies raised against but no longer contained [35S]sulfate. These results suggest sulfation occurred carbohydrate residues. possible importance for role adhesion discussed.