Dibutyryl cAMP- or Interleukin-6-induced astrocytic differentiation enhances mannose binding lectin (MBL)-associated serine protease (MASP)-1/3 expression in C6 glioma cells

2018 ◽  
Vol 653 ◽  
pp. 39-49 ◽  
Author(s):  
Valentina Pagliara ◽  
Maddalena Parafati ◽  
Annagrazia Adornetto ◽  
Misti C. White ◽  
Mariorosario Masullo ◽  
...  
Keyword(s):  
Serine Protease ◽  
Interleukin 6 ◽  
Glioma Cells ◽  
C6 Glioma ◽  
Mannose Binding Lectin ◽  
C6 Glioma Cells ◽  
Dibutyryl Camp ◽  
Mannose Binding ◽  
Astrocytic Differentiation ◽  
Binding Lectin

scholarly journals beta-Naphthoflavone disturbs astrocytic differentiation of C6 glioma cells by inhibiting autocrine interleukin-6

2004 ◽  
Vol 90 (3) ◽  
pp. 750-757 ◽  
Author(s):  
Hiromi Takanaga ◽  
Tomoko Yoshitake ◽  
Emi Yatabe ◽  
Shuntaro Hara ◽  
Manabu Kunimoto
Keyword(s):  
Interleukin 6 ◽  
Glioma Cells ◽  
C6 Glioma ◽  
C6 Glioma Cells ◽  
Astrocytic Differentiation

scholarly journals cAMP-induced Astrocytic Differentiation of C6 Glioma Cells Is Mediated by Autocrine Interleukin-6

2004 ◽  
Vol 279 (15) ◽  
pp. 15441-15447 ◽  
Author(s):  
Hiromi Takanaga ◽  
Tomoko Yoshitake ◽  
Shuntaro Hara ◽  
Chieri Yamasaki ◽  
Manabu Kunimoto
Keyword(s):  
Interleukin 6 ◽  
Glioma Cells ◽  
C6 Glioma ◽  
C6 Glioma Cells ◽  
Astrocytic Differentiation

Investigation of the mechanism of interaction between Mannose-binding lectin-associated serine protease-2 and complement C4

2015 ◽  
Vol 67 (2) ◽  
pp. 287-293 ◽  
Author(s):  
Nicole Drentin ◽  
Paul Conroy ◽  
Menachem J. Gunzburg ◽  
Robert N. Pike ◽  
Lakshmi C. Wijeyewickrema
Keyword(s):  
Serine Protease ◽  
Mannose Binding Lectin ◽  
Complement C4 ◽  
Mannose Binding ◽  
Mechanism Of Interaction ◽  
Binding Lectin

scholarly journals L-Ficolin/Mannose-Binding Lectin-Associated Serine Protease Complexes Bind to Group B Streptococci Primarily through N-Acetylneuraminic Acid of Capsular Polysaccharide and Activate the Complement Pathway

2007 ◽  
Vol 76 (1) ◽  
pp. 179-188 ◽  
Author(s):  
Youko Aoyagi ◽  
Elisabeth E. Adderson ◽  
Craig E. Rubens ◽  
John F. Bohnsack ◽  
Jin G. Min ◽  
...  
Keyword(s):  
Serine Protease ◽  
Specific Antibody ◽  
Capsular Polysaccharide ◽  
Mannose Binding Lectin ◽  
Lectin Pathway ◽  
Group B Streptococci ◽  
Acetylneuraminic Acid ◽  
Mannose Binding ◽  
Group B ◽  
Binding Lectin

ABSTRACT Group B streptococci (GBS) are the most common cause of neonatal sepsis and meningitis. Most infants who are colonized with GBS at birth do not develop invasive disease, although many of these uninfected infants lack protective levels of capsular polysaccharide (CPS)-specific antibody. The lectin pathway of complement is a potential mechanism for initiating opsonization of GBS with CPS-specific antibody-deficient serum. In this study, we determined whether mannose-binding lectin (MBL)/MBL-associated serine protease (MASP) complexes and L-ficolin/MASP complexes bind to different strains of GBS to activate the lectin pathway, and we identified the molecules recognized by lectins on the GBS surface. We found that MBL did not bind to any GBS examined, whereas L-ficolin bound to GBS cells of many serotypes. L-ficolin binding to GBS cells correlated with the CPS content in serotypes Ib, III (restriction digestion pattern types III-2 and III-3), and V but not with the group B-specific polysaccharide (GBPS) content or with the lipoteichoic acid (LTA) content. L-ficolin bound to purified CPS and GBPS in a concentration-dependent manner but not to purified LTA. All strains to which L-ficolin/MASP complexes bound consumed C4. When N-acetylneuraminic acid (NeuNAc) was selectively removed from GBS cells by treatment with neuraminidase, the reduction in L-ficolin binding was correlated with the amount of NeuNAc removed. Additionally, L-ficolin was able to bind to wild-type strains but was able to bind only weakly to unencapsulated mutants and a mutant strain in which the CPS lacks NeuNAc. We concluded that L-ficolin/MASP complexes bind to GBS primarily through an interaction with NeuNAc of CPS.

Two mannose-binding lectin homologues and an MBL-associated serine protease are expressed in the gut epithelia of the urochordate species Ciona intestinalis

2010 ◽  
Vol 34 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Mikkel-Ole Skjoedt ◽  
Yaseelan Palarasah ◽  
Karina Rasmussen ◽  
Lars Vitved ◽  
Jan Salomonsen ◽  
...  
Keyword(s):  
Serine Protease ◽  
Ciona Intestinalis ◽  
Mannose Binding Lectin ◽  
Mannose Binding ◽  
Binding Lectin
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