Ficoline

Ficoline sind eine Gruppe von Proteinen des Komplementsystems, die als Lektine N-Acetylglucosamin binden.[1]

Ficoline sind eine Gruppe von Proteinen des Komplementsystems, die als Lektine N-Acetylglucosamin binden.[1]

Eigenschaften

Ficoline besitzen, je nach Proteindomäne, strukturelle Homologien zu Kollagen und Fibronectin. Unter den Fibronectin-verwandten Proteindomänen besitzen die der Ficoline die höchste Mutationsrate.[2] Wie auch die verwandten Collectine, z. B. Mannan-bindendes Lektin (MBL), bindet Ficolin als Pattern-Recognition Receptor an Kohlenhydrate und aktiviert dann den Lektin-Weg des Komplementsystems.[3] Ficoline bilden Multimere aus zwölf Untereinheiten (Dodecamere) mit einer Masse von 400 Kilodalton aus.[4]

Im Menschen wurden drei Ficoline beschrieben, FCN1 (synonym M-Ficolin),[5] FCN2 (synonym L-Ficolin)[6] und FCN3 (synonym H-Ficolin).[7]

Einzelnachweise

  1. ↑ M. Matsushita: Ficolins: complement-activating lectins involved in innate immunity. In: Journal of Innate Immunity. Band 2, Nummer 1, 2010, S. 24–32, doi:10.1159/000228160. PMID 20375620.
  2. ↑ R. F. Doolittle, K. McNamara, K. Lin: Correlating structure and function during the evolution of fibrinogen-related domains. In: Protein Science : a publication of the Protein Society. Band 21, Nummer 12, Dezember 2012, S. 1808–1823, doi:10.1002/pro.2177. PMID 23076991. PMC 3575912 (freier Volltext).
  3. ↑ M. Cedzynski, A. S. Swierzko, D. C. Kilpatrick: Factors of the lectin pathway of complement activation and their clinical associations in neonates. In: Journal of Biomedicine & Biotechnology. Band 2012, 2012, S. 363246, doi:10.1155/2012/363246. PMID 22619494. PMC 3348535 (freier Volltext).
  4. ↑ D. C. Kilpatrick, J. D. Chalmers: Human L-ficolin (ficolin-2) and its clinical significance. In: Journal of Biomedicine & Biotechnology. Band 2012, 2012, S. 138797, doi:10.1155/2012/138797. PMID 22500076. PMC 3303570 (freier Volltext).
  5. ↑ J. Lu, P. N. Tay, O. L. Kon, K. B. Reid: Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9. In: Biochemical Journal. Band 313 (Pt 2), Januar 1996, S. 473–478, PMID 8573080. PMC 1216931 (freier Volltext).
  6. ↑ Y. Endo, Y. Sato, M. Matsushita, T. Fujita: Cloning and characterization of the human lectin P35 gene and its related gene. In: Genomics. Band 36, Nummer 3, September 1996, S. 515–521, doi:10.1006/geno.1996.0497. PMID 8884275.
  7. ↑ R. Sugimoto, Y. Yae, M. Akaiwa, S. Kitajima, Y. Shibata, H. Sato, J. Hirata, K. Okochi, K. Izuhara, N. Hamasaki: Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family. In: The Journal of Biological Chemistry. Band 273, Nummer 33, August 1998, S. 20721–20727, PMID 9694814.

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