Transbilayer movement of phosphatidylserine in erythrocytes: inhibition of transport and preferential labeling of a 31,000-dalton protein by sulfhydryl reactive reagents.
A series of labeled thiolation reagents were synthesized on the basis of the parent structure pyridyldithioethylamine (PDA). These compounds specifically and reversibly inhibit the active intrabilayer transport of phosphatidylserine (PS) in human red blood cells. The binding of PDA to cells can be quantified since the thiol-disulfide exchange reaction yields a chromophore. In addition, the presence of a primary amine makes it amenable to derivatization with a variety of compounds. An iodinated derivative of PDA preferentially labeled a 31,000-dalton red blood cell peptide. The labeled component, which may represent the PS transporter, comigrated with integral membrane protein band 7.
Connor
J
J
Department of Cell Biology, University of Texas M. D. Anderson Hospital and Tumor Institute, Houston 77030.
Schroit
A J
AJ
D002352:Carrier Proteins / Q000097:blood*; D004220:Disulfides / Q000138:chemical synthesis / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008051:Lipid Bilayers; D008565:Membrane Proteins; D008970:Molecular Weight; D010718:Phosphatidylserines / Q000097:blood*; D049294:Phospholipid Transfer Proteins; D011725:Pyridines / Q000138:chemical synthesis / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D013439:Sulfhydryl Reagents / Q000138:chemical synthesis / Q000494:pharmacology*
D002352:Carrier Proteins; D004220:Disulfides; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010718:Phosphatidylserines; D049294:Phospholipid Transfer Proteins; D011725:Pyridines; D013439:Sulfhydryl Reagents; C055639:pyridyldithioethylamine