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Research Article Free access | 10.1172/JCI118515

The molecular basis of hereditary complement factor I deficiency.

T J Vyse, B J Morley, I Bartok, E L Theodoridis, K A Davies, A D Webster, and M J Walport

Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

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Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

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Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

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Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

Find articles by Theodoridis, E. in: JCI | PubMed | Google Scholar

Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

Find articles by Davies, K. in: JCI | PubMed | Google Scholar

Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

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Department of Medicine, RPMS, Hammersmith Hospital, London, United Kingdom.

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Published February 15, 1996 - More info

Published in Volume 97, Issue 4 on February 15, 1996
J Clin Invest. 1996;97(4):925–933. https://doi.org/10.1172/JCI118515.
© 1996 The American Society for Clinical Investigation
Published February 15, 1996 - Version history
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Abstract

The molecular basis of hereditary complement factor I deficiency is described in two pedigrees. In one pedigree, there were two factor I-deficient siblings, one of whom was asymptomatic and the other suffered from recurrent pyogenic infections. Their factor I mRNA was analyzed by reverse transcription of fibroblast RNA followed by amplification using the polymerase chain reaction. Both siblings were homozygous for the same transversion (adenine to thymine) at nucleotide 1282 in the cDNA. This mutation causes histidine-400 to be replaced by leucine. The altered histidine is a semi-conserved residue within the serine proteinase family, although no function has been ascribed to it. The proband of the second pedigree studied was found to be a compound heterozygote. One allele had the same mutation as the first family, the second allele had a donor splice site mutation that resulted in the deletion of the mRNA encoded in the fifth exon (a low-density lipoprotein receptor domain) from its transcript.

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  • Version 1 (February 15, 1996): No description

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