<p>Prophenoloxidase (proPO) is a key enzyme for generation of melanin and is activated by the proPO activating enzyme (ppA) to its active form, PO. The active ppA was purified and cloned from crayfish hemocytes and it is a typical serine proteinase containing a clip, a proline-rich, and a glycine-rich domain. A recombinant protein containing the clip-domain, with homology to horseshoe crab big defensin and mammalian â-defensin, had antibacterial activity <i>in vitro</i> against gram-positive bacteria.</p><p>The proPO activating system (proPO system) is triggered by lipopolysaccharides (LPS) or â-1,3-glucans. An LPS and â-1,3-glucan binding protein (LGBP) was characterized from crayfish hemocytes. The results of an LGBP antibody inhibition assay suggest that LGBP is directly involved in the proPO system.</p><p>The primary structure of a crayfish masquerade-like (mas) protein has homology to serine proteinases except for a substitution within the catalytic triad, which renders it without proteinase activity. The crayfish mas-like protein has also binding activity to various gram-negative bacteria and yeast. When the mas-like protein binds to microorganisms, it is processed by a proteolytic enzyme. The mas-like protein exhibited cell adhesion and opsonic activities suggesting that it plays a role in defense against parasites.</p>
| Identifer | oai:union.ndltd.org:UPSALLA/oai:DiVA.org:uu-623 |
| Date | January 2001 |
| Creators | So Young, Lee |
| Publisher | Uppsala University, Department of Evolutionary Biology, Uppsala : Acta Universitatis Upsaliensis |
| Source Sets | DiVA Archive at Upsalla University |
| Language | English |
| Detected Language | English |
| Type | Doctoral thesis, comprehensive summary, text |
| Relation | Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, 1104-232X ; 613 |
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