Studies on the binding of complement factor C4 in human platelets. Complement activation by means of cold agglutinins.
Normal human platelets were investigated by immunofluorescence techniques for the natural occurrence of and uptake capacity for complement factor C4. Fractions of human platelets were found to carry none or very little C4. Activated C4 was readily taken up by the majority of platelets in vitro. Complement could be activated with pathological cold agglutinins (CA) of mono- or polyclonal types, all with specificity for the I antigen. Complement activation seen in normal human sera was probably due to naturally occurring CA with anti-I specificity. Thrombin potentiated the complement-activating capacity of CA, and complement factor C1 enhanced and stabilized the binding of CA to platelets.
D000373:Agglutinins / Q000276:immunology; D001792:Blood Platelets / Q000378:metabolism*; D003080:Cold Temperature; D003167:Complement Activation; D003181:Complement C4 / Q000378:metabolism*; D015935:Complement C4b; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding
D000373:Agglutinins; D003181:Complement C4; D010446:Peptide Fragments; D015935:Complement C4b; C032261:complement C4d