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Complement component C8γ is expressed in human fetal and adult kidney independent of C8α
Author(s) -
Trojer Patrick,
Wojnar Petra,
Merschak Petra,
Redl Bernhard
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00228-8
Subject(s) - complementary dna , complement system , microbiology and biotechnology , complement factor i , recombinant dna , biology , northern blot , thymosin , lipocalin , western blot , chemistry , gene , biochemistry , antibody , genetics
Human complement component C8γ is an unusual complement factor since it shows no homology to other complement proteins but is a member of the lipocalin superfamily. So far, it has been found exclusively in plasma, covalently linked to C8α by disulfide bridging. We have used dot blot and Northern blot analyses of a large number of different human tissues to survey systematically the expression pattern of C8γ. Our experiments clearly showed that besides in liver, this gene is also expressed in fetal and adult kidney. Renal expression of C8γ is not dependent on C8α expression, since we could not detect C8α expression in kidney. Thus its physiological function is not restricted to a specific action in association with complement components. As a prerequisite for further characterization of the structure and binding activities of the uncomplexed C8γ, we have expressed the encoding cDNA in Escherichia coli . To increase the probability for proper folding of the characteristic intramolecular disulfide bridge the recombinant protein was produced by secretion to the periplasm.