Disulfide Connectivity in Cerebroside Sulfate Activator Is Not Necessary for Biological Activity or α-Helical Content but Is Necessary for Trypsin Resistance and Strong Ligand Binding

2000 ◽  
Vol 376 (2) ◽  
pp. 266-274 ◽  
Author(s):  
Kym F. Faull ◽  
Jason Higginson ◽  
Alan J. Waring ◽  
Jeffrey Johnson ◽  
Trang To ◽  
...  
Keyword(s):  
Biological Activity ◽  
Ligand Binding ◽  
Cerebroside Sulfate ◽  
Helical Content

scholarly journals Ligand Binding and Signaling of HARE/Stabilin-2

Biomolecules ◽  
2019 ◽  
Vol 9 (7) ◽  
pp. 273 ◽  
Author(s):  
Edward N. Harris ◽  
Fatima Cabral
Keyword(s):  
Biological Activity ◽  
Hyaluronic Acid ◽  
Cell Surface ◽  
Ligand Binding ◽  
Antisense Oligonucleotides ◽  
External Environment ◽  
Scavenger Receptors ◽  
Extracellular Material ◽  
Synthetic Drugs ◽  
Multiple Ligands

The Stabilin receptors are a two-member family in the type H class of scavenger receptors. These dynamic receptors bind and internalize multiple ligands from the cell surface for the purpose of clearing extracellular material including some synthetic drugs and for sensing the external environment of the cell. Stabilin-1 was the first receptor to be cloned, though the biological activity of Hyaluronic Acid Receptor for Endocytosis (HARE)/Stabilin-2 was observed about 10 years prior to the cloning of Stabilin-1. Stabilin-1 has a more diverse expression profile among the tissues than HARE/Stabilin-2. This review will focus on HARE/Stabilin-2 and its interactions with hyaluronan, heparin, and phosphorothioate antisense oligonucleotides and what is known about how this receptor participates in signaling upon ligand binding.

The effect of ligand binding and acid splitting on the optical rotatory dispersion of ferric horseradish peroxidase

1968 ◽  
Vol 46 (10) ◽  
pp. 1231-1235 ◽  
Author(s):  
William D. Ellis ◽  
H. Brian Dunford
Keyword(s):  
Horseradish Peroxidase ◽  
Ligand Binding ◽  
Protein Conformation ◽  
Spectral Region ◽  
Optical Rotatory Dispersion ◽  
Rotatory Dispersion ◽  
Optical Rotatory ◽  
Helical Content ◽  
Protein Moiety ◽  
Soret Region

The optical rotatory dispersion of horseradish peroxidase and its cyanide, fluoride, and hydroxide complexes was studied in the spectral region 215–450 mμ, and that of the azide complex at 350–450 mμ. The effect that splitting the heme from the protein of peroxidase has on the optical rotatory dispersion in the 215–450 mμ region was also studied. Results of measurements of the reduced mean residue rotation at 233 mμ, lead to the conclusion that there are no significant changes in gross protein conformation upon the binding of ligands to peroxidase, but that the splitting of the heme causes a reduction of the helical content of the protein. Pure peroxidase was estimated to have 43% α-helical content, which was reduced to 33% when the heme was split from the protein. Results of studies in the Soret region indicate that the binding of various ligands does not cause an alteration of the geometry of the heme with respect to the protein moiety.

scholarly journals The influence of N-acetylneuraminic acid on the properties of human orosomucoid

1986 ◽  
Vol 236 (1) ◽  
pp. 149-153 ◽  
Author(s):  
M L Friedman ◽  
J R Wermeling ◽  
H B Halsall
Keyword(s):  
Thermal Stability ◽  
Biological Activity ◽  
Fluorescence Spectroscopy ◽  
Ligand Binding ◽  
Protein Conformation ◽  
Acid Content ◽  
Acetylneuraminic Acid ◽  
Water Of Hydration ◽  
Hydrophobic Binding ◽  
A Charge

Little is known of the relationships that may exist among the three principal functionalities of glycoproteins. Orosomucoids of closely defined N-acetylneuraminic acid content were examined for evidence of influence of N-acetylneuraminic acid content on the physical properties of the glycoprotein. Fluorescence spectroscopy gave no indication of conformational change in the protein core upon desialylation. Small changes in the chromatographic partition coefficient, sigma, and thermal stability, Td, are interpreted to reflect loss of water of hydration and increased glycan stem-protein interaction without a major repositioning of the chains. Ligand-binding measurements indicate no alteration in the hydrophobic binding domain and a possible interaction between chlorpromazine and N-acetylneuraminic acid. All changes seen are progressive and occur through a region where changes in biological activity are not found. It is suggested that the dependence of biological activity on N-acetylneuraminic acid content in orosomucoid reflects, not coupled changes in protein conformation, but a charge-density-related interaction such that, below a contribution of four or five N-acetylneuraminic acid residues, activity is modified.

Biological activity and ligand binding mode to the progesterone receptor of A-homo analogues of progesterone

2011 ◽  
Vol 19 (5) ◽  
pp. 1683-1691 ◽  
Author(s):  
Lautaro D. Alvarez ◽  
María V. Dansey ◽  
Marcelo A. Martí ◽  
Paola Y. Bertucci ◽  
Pablo H. Di Chenna ◽  
...  
Keyword(s):  
Biological Activity ◽  
Progesterone Receptor ◽  
Ligand Binding ◽  
Binding Mode

Identification of Residues of the IFNAR1 Chain of the Type I Human Interferon Receptor Critical for Ligand Binding and Biological Activity†

Biochemistry ◽  
2004 ◽  
Vol 43 (39) ◽  
pp. 12498-12512 ◽  
Author(s):  
Chantal Cajean-Feroldi ◽  
Florence Nosal ◽  
Pierre C. Nardeux ◽  
Xavier Gallet ◽  
Jacqueline Guymarho ◽  
...  
Keyword(s):  
Biological Activity ◽  
Ligand Binding ◽  
Human Interferon ◽  
Type I ◽  
Interferon Receptor

scholarly journals Role of N-linked glycosylation in biosynthesis, trafficking, and function of the human glucagon-like peptide 1 receptor

2010 ◽  
Vol 299 (1) ◽  
pp. E62-E68 ◽  
Author(s):  
Quan Chen ◽  
Laurence J. Miller ◽  
Maoqing Dong
Keyword(s):  
Biological Activity ◽  
Cell Surface ◽  
Ligand Binding ◽  
Receptor Expression ◽  
Site Directed Mutagenesis ◽  
Amino Terminal ◽  
Glycosylation Sites ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1 ◽  
And Function

The family B G protein-coupled glucagon-like peptide 1 (GLP-1) receptor is an important drug target for treatment of type 2 diabetes. Like other family members, the GLP-1 receptor is a glycosylated membrane protein that contains three potential sites for N-linked glycosylation within the functionally important extracellular amino-terminal domain. However, the roles for each potential site of glycosylation in receptor biosynthesis, trafficking, and function are not known. In this work, we demonstrated that tunicamycin inhibition of glycosylation of the GLP-1 receptor expressed in CHO cells interfered with biosynthesis and intracellular trafficking, thereby eliminating natural ligand binding. To further investigate the roles of each of the glycosylation sites, site-directed mutagenesis was performed to eliminate these sites individually and in aggregate. Our results showed that mutation of each of the glycosylation sites individually did not interfere with receptor expression on the cell surface, ligand binding, and biological activity. However, simultaneous mutation of two or three glycosylation sites resulted in almost complete loss of GLP-1 binding and severely impaired biological activity. Immunostaining studies demonstrated receptor biosynthesis but aberrant trafficking, with most of the receptor trapped in the endoplasmic reticulum and golgi compartments and little of the receptor expressed on the cell surface. Interestingly, surface expression, ligand binding, and biological activity of these mutants improved significantly when biosynthesis was slowed using low temperature (30°C). These data suggest that N-linked glycosylation of the GLP-1 receptor is important for its normal folding and trafficking to the cell surface.

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