Binding and covalent processing of fibrinogen by hepatocytes and endothelial cells.
In contrast to most plasma glycoproteins, asialofibrinogen and aglycofibrinogen manifest relatively normal in vivo survivals, suggesting that molecular determinants other than the carbohydrate may be involved in their catabolism. To analyse the metabolic properties of fibrinogen further, we analysed the interaction of normal fibrinogen with suspensions of rabbit hepatocytes or human umbilical vein endothelial cells. In so doing, we identified a novel type of fibrinogen - cell interaction which has the distinguishing characteristic of involving covalent transglutaminase-mediated fibrinogen cross-linking. In this report, we highlight some of the major distinguishing characteristics of this novel type of transglutaminase-mediated fibrinogen - cell interaction.
Barsigian
C
C
Cardeza Foundation for Hematologic Research, Department of Medicine, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107.
Martinez
J
J
D000818:Animals; D037263:Asialoglycoprotein Receptor; D001212:Asialoglycoproteins / Q000378:metabolism; D004730:Endothelium, Vascular / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000166:cytology / Q000378:metabolism*; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism*; D011108:Polymers; D011485:Protein Binding; D011817:Rabbits; D011971:Receptors, Immunologic / Q000378:metabolism; D011503:Transglutaminases / Q000037:antagonists & inhibitors / Q000378:metabolism
D037263:Asialoglycoprotein Receptor; D001212:Asialoglycoproteins; D010980:Platelet Membrane Glycoproteins; D011108:Polymers; D011971:Receptors, Immunologic; C032692:asialofibrinogen; D005340:Fibrinogen; D011503:Transglutaminases