Mesh : Amino Acid Sequence Animals Base Sequence Cloning, Molecular Conserved Sequence DNA Primers DNA, Complementary Databases, Factual Humans Membrane Glycoproteins / chemistry genetics Mice Molecular Sequence Data Polymerase Chain Reaction Pregnancy Proteins / chemistry genetics Proteins / chemistry genetics Rabbits Repetitive Sequences, Nucleic Acid Sequence Homology, Amino Acid Tumor Necrosis Factor-alpha / chemistry genetics Urochordata / chemistry genetics Vitronectin / chemistry genetics

来  源:   DOI:10.1016/0305-0491(95)00025-4   PDF(Sci-hub)

Abstract:
Mammalian tumor necrosis factor (TNF)-alpha degenerate polymerase chain reaction (PCR) primers were used to amplify a probe from Botryllus schlosseri (colonial ascidian) allogeneic rejection-cDNA library. A PCR product (269 bp) was cloned and sequenced encoding an open reading frame (ORF) of 89 amino acids (aa). This clone, which revealed no similarity to TNF-alpha, but a substantial similarity to mammalian proteins featuring short consensus repeats (SCRs) of the complement control superfamily, was used to probe the rejection-cDNA library. Two partial cDNA clones were isolated and sequenced (Bs.1, 846 bp; Bs.2, 712 bp). The longest ORF in clone Bs.1 (which lacks the 5\' end of the cDNA) predicts a protein of 251 aa, which differs from Bs.2 at six nucleotides and four aa. We compare the aa similarity (up to 50.5%) of Bs.1 with the SCR-region of mammalian complement factor H, apolipoprotein H, selectins, and complement receptors type 1 and type 2. A somatomedin B-like domain at the C-terminus of Bs.1 deduced protein was also recorded. We propose that this mosaic and polymorphic botryllid sequence, featuring mammalian-like SCRs, might be an ancestral molecule in the evolution of the chordate\'s complement-control protein superfamily.
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