Results 141 to 150 of about 5,097 (156)

A novel human dendritic cell-derived C1r-like serine protease analog inhibits complement-mediated cytotoxicity

Biochemical and Biophysical Research Communications, 2004
Trypsin-like serine proteases are involved in diverse biological processes such as complement activation, tissue remodeling, cellular migration, tumor invasion, and metastasis. Here we report a novel human C1r-like serine protease analog, CLSPa, derived from dendritic cells (DC). The 487-residue CLSPa protein contains a CUB domain and a serine protease
Naisong, Lin, Shuxun, Liu, Nan, Li, Pingping, Wu, Huazhang, An, Yizhi, Yu, Tao, Wan, Xuetao, Cao   +7 more
openaire   +2 more sources

Assignment of the complement serine protease genes C1r and C1s to chromosome 12 region 12p13

Human Genetics, 1988
C1r and C1s are distinct, but structurally and functionally similar, serine protease zymogens responsible for the enzymatic activity of the first component of complement (C1). Recent comparisons indicate a significant degree of sequence similarity between C1r and C1s and support the hypothesis that they are related by gene duplication.
V C, Nguyen, M, Tosi, M S, Gross, O, Cohen-Haguenauer, C, Jegou-Foubert, M F, de Tand, T, Meo, J, Frézal   +7 more
openaire   +2 more sources

Genetic polymorphism of human C1R subcomponent of the first complement component in the Japanese population

Forensic Science International, 1988
Genetic polymorphism of the C1R subcomponent of human complement component C1 has been investigated in neuraminidase treated EDTA plasma samples of 440 healthy Japanese individuals living in Tokyo by means of thin-layer polyacrylamide gel isoelectric focusing (PAGIEF) at pH 3.5-9.5 in the presence of 8.0 M urea followed by an electroblotting with ...
S, Nakamura, O, Ohue, K, Akiyama, K, Abe
openaire   +2 more sources

Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin

Journal of Molecular Biology, 1989
The exon-intron structure of the human complement C1s gene displays a striking similarity with that of the gene encoding haptoglobin, a peculiar transport protein distantly related to the serine proteases. While the protease regions of the serine zymogens are typically encoded by multiple exons, the protease domains of C1s and of its genetically linked
M, Tosi, C, Duponchel, T, Meo, E, Couture-Tosi   +3 more
openaire   +2 more sources

Non-coordinated biosynthesis of early complement components in a deficiency of complement proteins C1r and C1s.

Scandinavian journal of immunology, 1994
We report on a 60-year-old woman with systemic lupus erythematosus and a total (95%) C1r and a partial (36%) C1s deficiency. The patient complained about cutaneous lesions on forearms and legs without other systemic involvement. Elevated anti-nuclear, anti-native DNA and anti-SSA antibodies were present.
A, Chevailler, C, Drouet, D, Ponard, C, Alibeu, S, Suraniti, F, Carrère, G, Renier, D, Hurez, M G, Colomb   +8 more
openaire   +1 more source

A polymorphism detected in sheep using a complement subcomponent C1r (C1R) probe

Journal of Animal Science, 1995
S H, Phua, N J, Wood
openaire   +2 more sources

Human complement C1r and C1s proteins and genes: studies with molecular probes.

Behring Institute Mitteilungen, 1989
The isolation of complementary DNA clones for both enzymic subcomponents of C1 has made it possible to derive their complete amino acid sequences and to verify and extend previous protein data. We review here recent advances in studies of the C1r and C1s proteins and of the corresponding genes, using molecular probes.
M, Tosi, A, Journet, C, Duponchel, E, Couture-Tosi, T, Meo   +4 more
openaire   +1 more source

A common amino acid polymorphism in complement component C1R

Human Molecular Genetics, 1994
M M, Nöthen, G, Dewald
openaire   +2 more sources

Autocatalytic activation of C1r subcomponent of the first component of human complement.

Journal of biochemistry, 1985
Autoactivation of the proenzyme form of a subunit of the first component (C1r) was performed in the presence and absence of diisopropyl fluorophosphate (DFP). The time-course of autoactivation of zymogen C1r followed a sigmoidal curve and was accelerated by addition of the enzyme C1r and by increasing the concentration of C1r, suggesting that ...
Y, Kasahara, H, Odai, K, Takahashi, S, Nagasawa, J, Koyama   +4 more
openaire   +1 more source

The substrate specificity of the complement initiating protease, C1r

Molecular Immunology, 2010
Lakshmi C. Wijeyewickrema, Thuy Tran, Phillip E. Thompson, Anthony Matthews, Dion Kaiserman, Phillip Bird, Robert Pike   +6 more
openaire   +1 more source