Photodynamic modification of proteins in human red blood cell membranes, induced by protoporphyrin.
Illumination of erythrocytes or erythrocyte membranes with visible light in the presence of protoporphyrin causes photodynamic damage of the cell membrane. This process is reflected a.o. by a mutilated ultrastructure and changes of the physical properties of the membrane proteins. Illumination in the presence of protoporphyrin causes association of membrane proteins, leading to blurring of the protein bands in electropheretograms, disappearance of bands and the appearance of protein aggregates on top of the gels. The formation of large protein aggregates is also indicated by Sephadex gel filtration of the solubilized membrane proteins. In kinetic studies it appeared that spectrin and the bands 2.1, 2.2, 2.3 and 6 are most susceptible and that band 3 is least susceptible to this cross-linking reaction. Experimental results indicate that this cross-linking is caused by direct photooxidation of membrane proteins. Peroxidation of unsaturated fatty acids is not involved in the process. The significance of this process for studies on membrane structure and on photodynamic membrane damage is discussed.
D001797:Blood Protein Electrophoresis; D001798:Blood Proteins / Q000378:metabolism / Q000528:radiation effects*; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008027:Light; D011166:Porphyrins / Q000494:pharmacology*; D011524:Protoporphyrins / Q000494:pharmacology*
D001798:Blood Proteins; D011166:Porphyrins; D011524:Protoporphyrins