scholarly journals Natural Monoclonal Antibody to Oxidized Low-Density Lipoprotein and Aggregatibacter actinomycetemcomitans

2017 ◽  
pp. 155-167 ◽  
Author(s):  
Chunguang Wang ◽  
Sohvi Hörkkö
Keyword(s):  
Monoclonal Antibody ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Aggregatibacter Actinomycetemcomitans ◽  
Low Density ◽  
Oxidized Low Density Lipoprotein

scholarly journals The terminal six amino-acids of the carboxy cytoplasmic tail of CD36 contain a functional domain implicated in the binding and capture of oxidized low-density lipoprotein

2002 ◽  
Vol 364 (2) ◽  
pp. 507-515 ◽  
Author(s):  
Eric MALAUD ◽  
Delphine HOURTON ◽  
Louise Marie GIROUX ◽  
Ewa NINIO ◽  
Robin BUCKLAND ◽  
...  
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibody ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Cytoplasmic Tail ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Low Density ◽  
Wild Type ◽  
Oxidized Low Density Lipoprotein

CD36, a major adhesion molecule expressed by monocytes/macrophages, plays a key role in the binding and internalization of oxidized low-density lipoprotein (OxLDL). This adhesion molecule, a member of an important scavenger receptor family, contains a very short C-terminal cytoplasmic tail that is known to induce intracellular signalling events. However, the domains on the cytoplasmic tail involved in such signal transduction are unknown. In this study, we have investigated the functional components of the cytoplasmic tail by site-directed mutagenesis coupled with functional OxLDL and monoclonal antibody (mAb) binding studies. Seven truncated or punctual CD36 constructs, localized in the cytoplasmic tail, were produced by site-directed mutagenesis. Each construct was stably expressed in HEK293 cells. We used a quantitative and a qualitative method, labelling OxLDL with either iodine or rhodamine, to determine the functional importance of the cytoplasmic domains in OxLDL internalization. Results indicate that: (1) a deletion of the last amino-acid (construct K472STOP) significantly reduces, compared with wild-type, the binding, internalization and degradation of OxLDL; (2) truncation of the last six amino-acids (construct R467STOP) significantly reduces OxLDL binding; (3) the above two constructs (K472STOP and R467STOP) showed a reduced rate of OxLDL internalization compared with wild-type; (4) the binding and rate of internalization of an anti-CD36 monoclonal antibody (10/5) was not affected by the above mentioned mutants (K472STOP and R467STOP), compared with wild-type. This study shows, for the first time, a specific site on the CD36 cytoplasmic tail that is critical for the binding, endocytosis and targeting of OxLDL.

Oxidized Low-Density Lipoprotein Induces Apoptosis of Human Endothelial Cells by Activation of CPP32-Like Proteases

Circulation ◽  
1997 ◽  
Vol 95 (7) ◽  
pp. 1760-1763 ◽  
Author(s):  
Stefanie Dimmeler ◽  
Judith Haendeler ◽  
Jan Galle ◽  
Andreas M. Zeiher
Keyword(s):  
Endothelial Cells ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Oxidized Low Density Lipoprotein ◽  
Human Endothelial Cells
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