Ficolins and FIBCD1: Soluble and membrane bound pattern recognition molecules with acetyl group selectivity

Thomsen, Theresa; Schlosser, Anders; Holmskov, Uffe; Sørensen, Grith Lykke

doi:10.1016/j.molimm.2010.09.019

Cited by 71 publications

(42 citation statements)

References 127 publications

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“…X-ray crystallography analysis of L-ficolin suggests that ligand binding is likely to involve a number of sites (see Fig. S1 to S4 in the supplemental material) simultaneously, with the S3 site being responsible for binding acetylated structures and the S2 site having an affinity for galactose and GlcNAc (22)(23)(24).…”

Section: Discussionmentioning

confidence: 99%

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

et al. 2013

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Aspergillus species are saprophytic molds causing life-threatening invasive fungal infections in the immunocompromised host. Innate immune recognition, in particular, the mechanisms of opsonization and complement activation, has been reported to be an integral part of the defense against fungi. We have shown that the complement component ficolin-A significantly binds to Aspergillus conidia and hyphae in a concentration-dependent manner and was inhibited by N-acetylglucosamine and N-acetylgalactosamine. Calcium-independent binding to Aspergillus fumigatus and A. terreus was observed, but binding to A. flavus and A. niger was calcium dependent. Ficolin-A binding to conidia was increased under low-pH conditions, and opsonization led to enhanced binding of conidia to A549 airway epithelial cells. In investigations of the lectin pathway of complement activation, ficolin-A-opsonized conidia did not lead to lectin pathway-specific C4 deposition. In contrast, the collectin mannose binding lectin C (MBL-C) but not MBL-A led to efficient lectin pathway activation on A. fumigatus in the absence of ficolin-A. In addition, ficolin-A opsonization led to a modulation of the proinflammatory cytokine interleukin-8. We conclude that ficolin-A may play an important role in the innate defense against Aspergillus by opsonizing conidia, immobilizing this fungus through enhanced adherence to epithelial cells and modulation of inflammation. However, it appears that other immune pattern recognition molecules, i.e., those of the collectin MBL-C, are involved in the Aspergillus-lectin complement pathway activation rather than ficolin-A.

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Section: Discussionmentioning

confidence: 99%

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

et al. 2013

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“…The members of this protein family include fibrinogen, MFAP4, angiopoietin, tachylectins, tenascins, fibroleukin, FIBCD1 and ficolins [15,16]. These proteins are up-regulated following exogenous immuno-stimulation and could bind to pathogens to eliminate foreign invaders.…”

Section: Introductionmentioning

confidence: 99%

Characteristic and functional analysis of a ficolin-like protein from the oyster Crassostrea hongkongensis

Xiang

Wang

et al. 2014

Fish & Shellfish Immunology

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“…4 MFAP4, known as 36-kDa microfibril-associated glycoprotein (MAGP36) 5 in other species, was first identified as a protein with a resemblance to tenascin in its amino acid composition and localization to the ECM in arteries. [6][7][8][9][10] MAGP36 is known to interact directly with ECM fibers, including elastin, collagen, and calvasculin.…”

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confidence: 99%

MFAP4 Promotes Vascular Smooth Muscle Migration, Proliferation and Accelerates Neointima Formation

Schlosser¹,

Pilecki²,

Hemstra³

et al. 2016

ATVB

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101

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V ascular smooth muscle cell (VSMC) activation and phenotypic switching are critical for remodeling processes in vascular proliferative disorders, including intimal hyperplasia. Both the migratory and proliferative activities of VSMCs, as well as the interplay between the extracellular matrix (ECM) and integrin receptors essentially, contribute to neointimal hyperplasia and restrictive remodeling processes in the vessels.1 Among integrins, the particular role of integrin α V β 3 in the induction of VSMC responses has been shown both in vivo and in vitro.

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Ficolins and FIBCD1: Soluble and membrane bound pattern recognition molecules with acetyl group selectivity

Cited by 71 publications

References 127 publications

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species

Characteristic and functional analysis of a ficolin-like protein from the oyster Crassostrea hongkongensis

MFAP4 Promotes Vascular Smooth Muscle Migration, Proliferation and Accelerates Neointima Formation

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