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Purification of properoxinectin, a myeloperoxidase homologue and its activation to a cell adhesion molecule
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
2007 (English)In: Biochimica et Biophysica Acta - General Subjects, ISSN 0304-4165, E-ISSN 1872-8006, Vol. 1770, no 1, 87-93 p.Article in journal (Refereed) Published
Abstract [en]

Peroxidases are important mediators of innate immune reactions throughout the animal kingdom. In many arthropods a myeloperoxidase homologue, peroxinectin, is known to function as a cell adhesion factor and an opsonin. Here, we report in the freshwater crayfish Pacifastacus leniusculus the isolation of properoxinectin, inactive in cell adhesion, and we also show that properoxinectin is produced in the mature blood cells whereas the hematopoietic tissue contains very little of this protein. Both properoxinectin and peroxinectin are catalytically active as peroxidases, at least when using low molecular weight substrates. The extracellular processing of properoxinectin into an active cell adhesion protein was found to involve proteolytic steps shared with the prophenoloxidase activating system to yield catalytically active phenoloxidase. Thus, the regulation of activities by two ancient metalloproteins, both potentially producing highly toxic substances aimed at pathogens, is carried out by limited proteolysis. The proteolytic processing is triggered in the presence of microbial compounds such as beta-glucans or lipopolysaccharide after the release of properoxinectin and prophenoloxidase activating serine proteinases from the blood cells.

Place, publisher, year, edition, pages
2007. Vol. 1770, no 1, 87-93 p.
Keyword [en]
peroxidase, prophenoloxidase, serine proteinase, hemocyte
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:uu:diva-83242DOI: 10.1016/j.bbagen.2006.06.018ISI: 000243631600012PubMedID: 16934940OAI: oai:DiVA.org:uu-83242DiVA: diva2:111149
Available from: 2008-06-09 Created: 2008-06-09 Last updated: 2017-12-14

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Lin, XionghuiCerenius, LageSöderhäll, Kenneth

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