MCD-EPR studies of deoxy[FeII,FeII]hemerythrin: probes of endogenous bridging ligands and exogenous ligand binding

1984 ◽  
Vol 106 (26) ◽  
pp. 8323-8325 ◽  
Author(s):  
Richard C. Reem ◽  
Edward I. Solomon
2013 ◽  
Vol 52 (22) ◽  
pp. 13014-13020 ◽  
Author(s):  
Yasunori Okamoto ◽  
Akira Onoda ◽  
Hiroshi Sugimoto ◽  
Yu Takano ◽  
Shun Hirota ◽  
...  

1991 ◽  
Vol 113 (7) ◽  
pp. 2799-2800 ◽  
Author(s):  
Richard C. Conover ◽  
Jae Bum Park ◽  
Michael W. W. Adams ◽  
Michael K. Johnson

2017 ◽  
Author(s):  
Anton Novak ◽  
Clifford Lingwood

AbstractCholesterol and glycosphingolipids (GSL) are the major species that accumulate in plasma membrane lipid rafts. These complexes imbue the membrane with increased order, which in turn, plays a central role in the transmembrane signaling foci lipid rafts provide. In addition, both GSL and cholesterol binding can mediate (separate) signal pathways. We have shown that cholesterol and GSLs however, form a complex in which the GSL sugar is reoriented from a membrane perpendicular to parallel format, becoming largely unavailable for exogenous ligand binding. Similarly, the steroid hydroxyl is masked, restricting access of cholesterol ligands. This was observed in model and cell membranes and in human tumour frozen tissue sections. We now show the order of exogenous ligand binding plays a significant role to determine the extent of GSL or cholesterol receptor activity. Ligand binding to cholesterol enhances subsequent GSL recognition and vice versa, suggesting that ligand binding to “free” receptor (membrane perpendicular GSL carbohydrate, nonmasked cholesterol) can result in partial dissociation of the GSL/cholesterol complex to allow additional GSL ligand and cholesterol ligand binding. Since many GSLs can complex with membrane cholesterol, the binding of a single cholesterol ligand may unmask cholesterol-complexed GSL for increased binding of both a single or multiple GSL-specific ligands. We show that multiple cholesterol-masked GSLs can be coincident in tissues. This provides a mechanism for GSL-dependent signal amplification and diversification, representing a biological ‘transistor’, regulating amplitude and potentially, diversity of GSL signaling. The process represents a new mechanism of ‘cross-talk’ between GSL and cholesterol signaling. This is of clinical importance since we have found cholesterol/GSL masking applies to monoclonal anti GSL antibodies in development and in current use as antineoplastic therapeutics.


1992 ◽  
Vol 114 (22) ◽  
pp. 8711-8713 ◽  
Author(s):  
Kristoffer K. Andersson ◽  
Timothy E. Elgren ◽  
Lawrence Que ◽  
John D. Lipscomb

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S187
Author(s):  
Tadayuki Uno ◽  
Kaori Kukino ◽  
Hatsuo Maeda ◽  
Yoshikazu Tomisugi ◽  
Yoshinobu Ishikawa ◽  
...  

2004 ◽  
Vol 44 (supplement) ◽  
pp. S126
Author(s):  
T. Uno ◽  
H. Tsutsumi ◽  
D. Ryu ◽  
K. Kiyota ◽  
Y. Tomisugi ◽  
...  

2006 ◽  
Vol 35 (1) ◽  
pp. 126-127 ◽  
Author(s):  
Takako Ohyama ◽  
Yoshitake Kato ◽  
Hajime Mita ◽  
Yasuhiko Yamamoto

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