Complement component C3: molecular basis of the C3*S025 variant and evidence for molecular heterogeneity of other variants |
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Authors: | Thomas Höhler Marina Botto Christian Rittner Peter M Schneider Karl-Hermann Meyer zum Büschenfelde |
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Institution: | (1) I. Med Klinik and Poliklinik, Johannes Gutenberg University Mainz, Langenbeckstrasse 1, 55101 Mainz, Germany;(2) Rheumatology Department, Royal Postgraduate Medical School,Hammersmith Hospital, London, UK;(3) Institute of Legal Medicine, Johannes Gutenberg University, Mainz, Germany |
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Abstract: | Complement component 3 (C3) is the central molecule of the complement system. It displays a number of polymorphic variants with, as yet, unclear functional consequences. We have investigated a number of rare C3 variants by PCR-SSCP (polymerase chain reaction-single strand conformation polymorphism) analysis and could identify the molecular basis of a C3*S025 variant. The decreased electrophoretic mobility of this protein is caused by the exchange of a neutral serine residue to an arginine residue (positively charged). This exchange is unlikely to have functional consequences as it maps to the C-terminus of the -chain. C3 variants appear to have originated from various independent mutations as we could not detect this mutation in different allotypes. |
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