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Volume 272, Number 9, Issue of February 28, 1997 pp. 5627-5634
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Human Factor H-related Protein 4 (FHR-4)
A NOVEL SHORT CONSENSUS REPEAT-CONTAINING PROTEIN IS ASSOCIATED WITH HUMAN TRIGLYCERIDE-RICH LIPOPROTEINS

(Received for publication, June 12, 1996, and in revised form, December 3, 1996)

Christine Skerka , Jens Hellwage , Wilfried Weber , Anne Tilkorn , Friedrich Buck ^§ , Thomas Marti , Eva Kampen , Ulrike Beisiegel and Peter F. Zipfel

From the Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Strasse 74, 20359 Hamburg, the  Medical Clinic, University Hospital Eppendorf, Martinistrasse 52, 20246 Hamburg, and the ^§ Institute for Cell Biology and Clinical Neurobiology, University of Hamburg, Süderfeldstrasse 24, 20246 Hamburg, Germany

A novel apoprotein of an apparent molecular mass of 86 kDa in its unreduced form was identified in human triglyceride-rich lipoproteins. This protein was purified and the amino acid sequence of six proteolytic fragments was found to overlap with that of the factor H-related proteins. In parallel we identified the cDNA encoding a new complement factor H-related protein, termed FHR-4. The sequences of the new apoprotein overlapped with that of the FHR-4 protein. Similar to the previously described factor H-related proteins, FHR-4 contains a hydrophobic signal sequence followed by a stretch of five repetitive elements termed short consensus repeats. Recombinant FHR-4 protein was expressed in the baculovirus system and has an apparent molecular mass of 42 kDa. In addition a 84-kDa dimeric form of the recombinant FHR-4 was detected. Using an immunoaffinity column with antibodies raised against the recombinant FHR-4, we isolated a 86-kDa protein from human plasma. The different molecular mass of the recombinant FHR-4 and the dimeric FHR-4 in plasma is due to different carbohydrate moieties. The 86-kDa plasma protein and the novel apolipoprotein had identical mobility on SDS-polyacrylamide gel electrophoresis analysis and reacted with antisera raised against the reFHR-4 and the purified apoprotein. In conclusion, we have identified a novel factor H-related protein, FHR-4, in human plasma and demonstrate that this protein is present in triglyceride-rich lipoproteins in a dimeric form. This observation provides an intriguing new aspect on possible function(s) of this novel protein and the other factor H-related proteins.

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