Results 171 to 180 of about 3,647 (206)

Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins

Genomics, 2004
Ficolin is a collagenous lectin which plays a crucial role in innate immunity. Three and two ficolins have been identified in human and mice, respectively. To identify the mouse homologue of human H-ficolin and to elucidate the orthology between mouse ficolins A/B and human L-/M-ficolins, the gene structures were explored.
Kazuko Kanno, Minoru Takahashi, Misao Matsushita   +2 more
exaly   +3 more sources

The Role of Ficolins in Innate Immunity

Immunobiology, 2002
Ficolins are a group of proteins containing both a collagen-like domain and a fibrinogen-like domain and are found in varying tissues. Ficolins present in sera have a lectin activity toward N-acetylglucosamine through their fibrinogen-like domains. The domain organizations between ficolins and mannose-binding lectin (MBL) are very similar in that both ...
Teizo Fujita
exaly   +3 more sources

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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.
Teizo Fujita
exaly   +3 more sources

Structure and Function of Ficolins

2007
Ficolins are proteins that consist mainly of two domains: an N-terminal collagen- like domain and a C-terminal fibrinogen-like domain. This domain structure is related to MBL or C1q, a subcomponent of the complement C1 complex in having a collagenous stalk.
Yuichi, Endo, Yu, Liu, Teizo, Fujita
openaire   +2 more sources

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 ...
Naotaka Hamasaki, Teizo Fujita
exaly   +3 more sources

Carbohydrate-binding specificities of mouse ficolin A, a splicing variant of ficolin A and ficolin B and their complex formation with MASP-2 and sMAP

Immunogenetics, 2005
Ficolins are a group of proteins mainly consisting of collagen-like and fibrinogen-like domains and are thought to play a role in innate immunity via their carbohydrate-binding activities. Two types of ficolins have been identified in mice, ficolin A, and ficolin B. However, their structure and function are not fully understood.
Y, Endo, N, Nakazawa, Y, Liu, D, Iwaki, M, Takahashi, T, Fujita, M, Nakata, M, Matsushita   +7 more
openaire   +2 more sources

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
openaire   +2 more sources

Ficolin A and ficolin B are expressed in distinct ontogenic patterns and cell types in the mouse

Molecular Immunology, 2005
Ficolins are a group of proteins characterized by the presence of collagen-like and fibrinogen-like domains. Two of three human ficolins, L-ficolin and H-ficolin, are serum lectins that form complexes with mannose-binding lectin-associated serine proteases (MASPs) and play important roles in the lectin complement pathway.
Yu, Liu, Yuichi, Endo, Shunsaku, Homma, Kazuko, Kanno, Hiroyuki, Yaginuma, Teizo, Fujita   +5 more
openaire   +2 more sources

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
openaire   +3 more sources

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
openaire   +2 more sources