Results 181 to 190 of about 7,922 (214)

Ficolins in complement activation

Molecular Immunology, 2013
Ficolins are a group of multimeric lectins made up of single subunits each of which is composed of a collagen-like domain and a fibrinogen-like domain. Most of the ficolins identified to date bind to acetylated compounds such as N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc).
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Collectins and Ficolins

Protein-carbohydrate interactions are utilized by the immune system for several defense activities. Collectins and ficolins have a key role in maintaining the balance of surfactants in the lungs and supporting the immune system in the lungs, respectively. This chapter provides an extensive description of two soluble pattern recognition receptors (PRRs),
Hajra, Gupta, Ann Mary, Joseph, Mughair, Abdul Aziz, Faryal, Saeed, Rekha, Kumari, Khaled, Masmoudi, Uday, Kishore, Taruna, Madan   +7 more
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Ficolins and the lectin complement pathway

Immunological Reviews, 2001
Summary:Ficolins, found in various tissues, are a group of proteins containing both a collagen‐like and a fibrinogen‐like domain. Recently, it was shown that ficolins present in serum are lectins with a common binding specificity for N‐acetylglucosamine (GlcNAc). The fibrinogen‐like domain is responsible for the carbohydrate binding.
M, Matsushita, T, Fujita
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The ficolin response to LPS-challenge in mice

Molecular Immunology, 2018
The ficolins belong to an important family of pattern recognition molecules, which contributes to complement activation via the lectin pathway. How the ficolins respond to inflammatory stimuli remains only partly understood. In the present study, we investigated the ficolin A and ficolin B expression and protein distribution patterns in a mouse model ...
Ida Jarlhelt, Ninette Genster, Nikolaj Kirketerp-Møller, Mikkel-Ole Skjoedt, Peter Garred   +4 more
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Can ficolin‐2 (L‐ficolin) insufficiency be established by a single serum protein measurement?

International Journal of Immunogenetics, 2015
SummarySerum ficolin‐2 was measured in multiple (2‐27) samples from 68 paediatric sepsis patients. Fourteen individuals (21%) gave values that included a change in status from ‘normal’ to ‘insufficient’ or vice versa. Therefore, if possible, ficolin‐2 concentration should be determined in samples obtained when a disease is inactive.
D C, Kilpatrick, A S, Świerzko, M, Sobociński, W, Krajewski, K, Chojnacka, J, Szczapa, M, Cedzyński   +6 more
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Characterization of Ficolins as Novel Elastin-Binding Proteins and Molecular Cloning of Human Ficolin-1

Journal of Biochemistry, 1996
A novel elastin-binding protein, EBP-37, was recently identified and purified from human plasma. Its partial amino acid sequences showed significant homology to porcine ficolins, which were originally purified from porcine uterus membranes as multimeric proteins with fibrinogen- and collagen-like domains.
S, Harumiya, K, Takeda, T, Sugiura, Y, Fukumoto, H, Tachikawa, K, Miyazono, D, Fujimoto, H, Ichijo   +7 more
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L-ficolin (ficolin-2) insufficiency is associated with combined allergic and infectious respiratory disease in children

Molecular Immunology, 2009
We previously reported an association between relative L-ficolin deficiency and recurrent respiratory infections co-existing with allergic disorders in children. To confirm and extend this preliminary finding, we performed a prospective study on children of a similar age (mean 8.9 years) designed to establish whether the principal relationship was with
Maciej Cedzynski, Anna St Swierzko, Agnieszka Szala   +2 more
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Comparative study of the human ficolins reveals unique features of Ficolin-3 (Hakata antigen)

Molecular Immunology, 2008
The ficolins and mannose-binding lectin (MBL) are collagen-like defence proteins that serve as recognition molecules in lectin complement pathway. Differential features that may indicate diverse functions of these proteins are poorly understood. In this study we compared important biological features of the ficolins and MBL.
Hummelshoj, Tina, Fog, Lea Munthe, Madsen, Hans O, Sim, Robert B, Garred, Peter   +4 more
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Histidine-regulated activity of M-ficolin

Biochemical Journal, 2008
Human M-ficolin is a pathogen-associated molecular recognition molecule in the innate immune system, and it binds to some sugars, such as GlcNAc (N-acetylglucosamine), on pathogen surfaces. From previous structural and functional studies of the FD1 (M-ficolin fibrinogen-like domain), we proposed that the ligand-binding region of FD1 exists in a ...
Michikazu, Tanio, Toshiyuki, Kohno
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Activation of the lectin complement pathway by ficolins

International Immunopharmacology, 2001
Mannose-binding lectin (MBL), a serum lectin specific for mannose or N-acetylglucosamine (GlcNAc), which contains both a collagen-like domain and a carbohydrate-recognition domain (CRD), plays a role in innate immunity by acting as an opsonin and activating complement in association with MBL-associated serine protease (MASP) via the lectin pathway ...
M, Matsushita, Y, Endo, N, Hamasaki, T, Fujita   +3 more
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