Results 131 to 140 of about 1,942 (166)

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).
Misao Matsushita
exaly   +3 more sources

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
exaly   +3 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 ...
Teizo Fujita, Misao Matsushita, Naotaka Hamasaki   +2 more
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

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

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
openaire   +2 more sources