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Identification and structural analysis of four serine proteases in a monotreme, the platypus, Ornithorhynchus anatinus
MOLECULAR IMMUNOLOGY, LARS HELLMAN. Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
2000 (English)In: Immunogenetics, ISSN 0093-7711, E-ISSN 1432-1211, Vol. 52, no 1-2, 19-28 p.Article in journal (Refereed) Published
Abstract [en]

To study the emergence of the major subfamilies of serine proteases during vertebrate evolution, we present here the primary structure of four serine proteases expressed in the spleen of a monotreme, the platypus, Ornithorhynchus anatinus. Partial cDNA clones for four serine proteases were isolated by a PCR-based strategy. This strategy is based on the high level of sequence identity between various members of the large gene family of trypsin-related serine proteases, over two highly conserved regions, those of the histidine and the serine of the catalytic triad. The partial cDNA clones were used to isolate full-length or almost full-length cDNA clones for three of these proteases from a platypus spleen cDNA library. By phylogenetic analysis, these three clones were identified as being the platypus homologues of human coagulation factor X, neutrophil elastase, and a protease distantly related to the T-cell granzymes. The remaining partial clone was found to represent a close homologue of human complement factor D (adipsin). The isolation of these four clones shows that several of the major subfamilies of serine proteases had evolved as separate subfamilies long before the radiation of the major mammalian lineages of today, the monotremes, the marsupials, and the placental mammals. Upon comparison of the corresponding proteases of monotremes and eutherian mammals, the coagulation and complement proteases were shown to display a higher degree of conservation compared to the hematopoietic proteases N-elastase and the T-cell granzymes. This latter finding indicates a higher evolutionary pressure to maintain specific functions in the complement and coagulation enzymes compared to many of the hematopoietic serine proteases.

Place, publisher, year, edition, pages
SPRINGER-VERLAG , 2000. Vol. 52, no 1-2, 19-28 p.
Keyword [en]
serine protease, platypus, hematopoiesis, evolution, human haptoglobin cdna, cathepsin-G, mast-cell, granzyme-B, molecular-cloning, gene, proteinase-3, distinct, sequence, expression
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Natural Sciences
Identifiers
URN: urn:nbn:se:uu:diva-38152DOI: 10.1007/s002510000246PubMedID: 11132153OAI: oai:DiVA.org:uu-38152DiVA: diva2:66051
Note
Addresses: Hellman L, Univ Uppsala, Biomed Ctr, Dept Cell & Mol Biol, Box 596, S-75124 Uppsala, Sweden. Univ Uppsala, Biomed Ctr, Dept Cell & Mol Biol, S-75124 Uppsala, Sweden. Univ Tasmania, Sch Biomed Sci, Launceston, Tas, Australia.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2017-12-06Bibliographically approved

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