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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Ficoline</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><p><b>Ficoline</b> sind eine Gruppe von <a href="Protein" title="Protein">Proteinen</a> des <a href="Komplementsystem" title="Komplementsystem">Komplementsystems</a>, die als <a href="Lektin" class="mw-redirect" title="Lektin">Lektine</a> <a href="N-Acetylglucosamin" title="N-Acetylglucosamin">N-Acetylglucosamin</a> binden.<sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup>
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<div class="mw-heading mw-heading2"><h2 id="Eigenschaften">Eigenschaften</h2></div>
<p>Ficoline besitzen, je nach <a href="Proteindom%C3%A4ne" title="Proteindomäne">Proteindomäne</a>, strukturelle <a href="Homologie_(Genetik)" title="Homologie (Genetik)">Homologien</a> zu <a href="Kollagen" class="mw-redirect" title="Kollagen">Kollagen</a> und <a href="Fibronectin" class="mw-redirect" title="Fibronectin">Fibronectin</a>. Unter den Fibronectin-verwandten Proteindomänen besitzen die der Ficoline die höchste Mutationsrate.<sup id="cite_ref-2" class="reference"><a href="#cite_note-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Wie auch die verwandten Collectine, z. B. <a href="Mannan" class="mw-disambig" title="Mannan">Mannan</a>-bindendes Lektin (MBL), bindet Ficolin als <a href="Pattern-Recognition_Receptor" class="mw-redirect" title="Pattern-Recognition Receptor">Pattern-Recognition Receptor</a> an <a href="Kohlenhydrat" class="mw-redirect" title="Kohlenhydrat">Kohlenhydrate</a> und aktiviert dann den Lektin-Weg des Komplementsystems.<sup id="cite_ref-3" class="reference"><a href="#cite_note-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> Ficoline bilden <a href="Multimer" title="Multimer">Multimere</a> aus zwölf Untereinheiten (Dodecamere) mit einer Masse von 400 <a href="Atomare_Masseneinheit" title="Atomare Masseneinheit">Kilodalton</a> aus.<sup id="cite_ref-4" class="reference"><a href="#cite_note-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup>
</p><p>Im Menschen wurden drei Ficoline beschrieben, FCN1 (synonym <i>M-Ficolin</i>),<sup id="cite_ref-5" class="reference"><a href="#cite_note-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> FCN2 (synonym <i>L-Ficolin</i>)<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> und FCN3 (synonym <i>H-Ficolin</i>).<sup id="cite_ref-7" class="reference"><a href="#cite_note-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup>
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<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text">M. Matsushita: <i>Ficolins: complement-activating lectins involved in innate immunity.</i> In: <i>Journal of Innate Immunity.</i> Band 2, Nummer 1, 2010, S.&nbsp;24–32, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1159/000228160">10.1159/000228160</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/20375620?dopt=Abstract">PMID 20375620</a>.</span>
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<li id="cite_note-2"><span class="mw-cite-backlink"><a href="#cite_ref-2">↑</a></span> <span class="reference-text">R. F. Doolittle, K. McNamara, K. Lin: <i>Correlating structure and function during the evolution of fibrinogen-related domains.</i> In: <i>Protein Science&nbsp;: a publication of the Protein Society.</i> Band 21, Nummer 12, Dezember 2012, S.&nbsp;1808–1823, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1002/pro.2177">10.1002/pro.2177</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/23076991?dopt=Abstract">PMID 23076991</a>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575912/">PMC&nbsp;3575912</a> (freier Volltext).</span>
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<li id="cite_note-3"><span class="mw-cite-backlink"><a href="#cite_ref-3">↑</a></span> <span class="reference-text">M. Cedzynski, A. S. Swierzko, D. C. Kilpatrick: <i>Factors of the lectin pathway of complement activation and their clinical associations in neonates.</i> In: <i>Journal of Biomedicine &amp; Biotechnology.</i> Band 2012, 2012, S.&nbsp;363246, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1155/2012%2F363246">10.1155/2012/363246</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/22619494?dopt=Abstract">PMID 22619494</a>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3348535/">PMC&nbsp;3348535</a> (freier Volltext).</span>
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<li id="cite_note-4"><span class="mw-cite-backlink"><a href="#cite_ref-4">↑</a></span> <span class="reference-text">D. C. Kilpatrick, J. D. Chalmers: <i>Human L-ficolin (ficolin-2) and its clinical significance.</i> In: <i>Journal of Biomedicine &amp; Biotechnology.</i> Band 2012, 2012, S.&nbsp;138797, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1155/2012%2F138797">10.1155/2012/138797</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/22500076?dopt=Abstract">PMID 22500076</a>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3303570/">PMC&nbsp;3303570</a> (freier Volltext).</span>
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<li id="cite_note-5"><span class="mw-cite-backlink"><a href="#cite_ref-5">↑</a></span> <span class="reference-text">J. Lu, P. N. Tay, O. L. Kon, K. B. Reid: <i>Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9.</i> In: <i><a href="Biochemical_Journal" title="Biochemical Journal">Biochemical Journal</a>.</i> Band 313 (Pt 2), Januar 1996, S.&nbsp;473–478, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8573080?dopt=Abstract">PMID 8573080</a>. <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1216931/">PMC&nbsp;1216931</a> (freier Volltext).</span>
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<li id="cite_note-6"><span class="mw-cite-backlink"><a href="#cite_ref-6">↑</a></span> <span class="reference-text">Y. Endo, Y. Sato, M. Matsushita, T. Fujita: <i>Cloning and characterization of the human lectin P35 gene and its related gene.</i> In: <i>Genomics.</i> Band 36, Nummer 3, September 1996, S.&nbsp;515–521, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1006/geno.1996.0497">10.1006/geno.1996.0497</a></span>. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8884275?dopt=Abstract">PMID 8884275</a>.</span>
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<li id="cite_note-7"><span class="mw-cite-backlink"><a href="#cite_ref-7">↑</a></span> <span class="reference-text">R. Sugimoto, Y. Yae, M. Akaiwa, S. Kitajima, Y. Shibata, H. Sato, J. Hirata, K. Okochi, K. Izuhara, N. Hamasaki: <i>Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family.</i> In: <i><a href="The_Journal_of_Biological_Chemistry" class="mw-redirect" title="The Journal of Biological Chemistry">The Journal of Biological Chemistry</a>.</i> Band 273, Nummer 33, August 1998, S.&nbsp;20721–20727, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/9694814?dopt=Abstract">PMID 9694814</a>.</span>
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