Mammalian recombinant coagulation proteins: structure and function. Transfus Sci 1998 Jun;19(2):177-89
Date
05/07/1998Pubmed ID
10187042DOI
10.1016/s0955-3886(98)00027-7Scopus ID
2-s2.0-0031788456 (requires institutional sign-in at Scopus site) 14 CitationsAbstract
Recombinant DNA technology has permitted the production of synthetic proteins which are potentially free of human infectious agents. Despite production in foreign cells, these proteins are structurally and functionally comparable to the native proteins. Recombinant clotting factors VIII, IX, VIIa, and von Willebrand factor have the same primary sequence as their plasma counterparts. The secondary and tertiary structures are similar, Post-translational modifications, including proteolytic processing, disulfide bonding, addition and processing of N- and O-linked glycans, gamma-carboxylation of glutamic acid residues, beta-hydroxylation of aspartic acid residues, sulfation of tyrosine residues, and phosphorylation of serine residues, are similar but not always identical, In some instances. these differences may cause significant functional differences. For example, reduced tyrosine sulfation and serine phosphorylation of recombinant factor IX have been correlated with reduced recovery following intravenous infusion. The specific clotting activity of the recombinant factors, an indication of their coagulant function, is equivalent to that of the plasma factors. Finally, these proteins have been used clinically and shown to correct clinical deficiencies of these proteins in a manner that is similar to replacement with plasma factors. All in all, the promise of recombinant DNA technology for coagulation and other disorders remains bright.
Author List
White GC 2nd, Pickens EM, Liles DK, Roberts HRAuthor
Gilbert C. White MD Professor in the Medicine department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBlood Coagulation Factors
Humans
Mammals
Recombinant Proteins
Structure-Activity Relationship
