Role of Glycosylation in the Lipid-Binding Activity of the Exchangeable Apolipoprotein, Apolipophorin-III

1998 ◽  
Vol 243 (2) ◽  
pp. 372-376 ◽  
Author(s):  
J.L. Soulages ◽  
J. Pennington ◽  
O. Bendavid ◽  
M.A. Wells
Keyword(s):  
Lipid Binding ◽  
Binding Activity ◽  
Apolipophorin Iii ◽  
Exchangeable Apolipoprotein

scholarly journals Essential Role of the Conformational Flexibility of Helices 1 and 5 on the Lipid Binding Activity of Apolipophorin-III

2001 ◽  
Vol 276 (36) ◽  
pp. 34162-34166 ◽  
Author(s):  
Jose L. Soulages ◽  
Estela L. Arrese ◽  
Palaniappan S. Chetty ◽  
Veronica Rodriguez
Keyword(s):  
Essential Role ◽  
Conformational Flexibility ◽  
Lipid Binding ◽  
Binding Activity ◽  
Apolipophorin Iii

scholarly journals Role of the N- and C-Terminal Helices in Apolipophorin III Stability and Lipid Binding

2012 ◽  
Vol 102 (3) ◽  
pp. 58a
Author(s):  
Pankaj Dwivedi ◽  
Johana Rodriguez ◽  
Paul M.M. Weers
Keyword(s):  
Lipid Binding ◽  
Apolipophorin Iii

Role of charged amino acid side chains in the stability and lipid binding ofManduca sexta apolipophorin III

1995 ◽  
Vol 30 (2-3) ◽  
pp. 211-223 ◽  
Author(s):  
Minal Upadhyaya ◽  
Kim Oikawa ◽  
Cyril M. Kay ◽  
Douglas G. Scraba ◽  
Roger Bradley ◽  
...  
Keyword(s):  
Amino Acid ◽  
Lipid Binding ◽  
Side Chains ◽  
Apolipophorin Iii ◽  
Amino Acid Side Chains ◽  
The Stability

Abstract 391: Apolipoprotein E3, Apolipoprotein AI, and Apolipophorin III Chimeras Provide Insight Into the Domain Organization of Apolipoproteins

2016 ◽  
Vol 36 (suppl_1) ◽  
Author(s):  
James V Horn ◽  
Mark Lek ◽  
Nnejiuwa Ibe ◽  
Rachel A Ellena ◽  
Wendy H Beck ◽  
...  
Keyword(s):  
Cholesterol Efflux ◽  
Dominant Role ◽  
Lipoprotein Metabolism ◽  
Lipid Binding ◽  
Binding Activity ◽  
Domain Model ◽  
Helix Bundle ◽  
Apolipophorin Iii ◽  
Helical Content ◽  
The Stability

Apolipoproteins (apo) A-I and E are exchangeable apolipoproteins that play a dominant role in regulating lipoprotein metabolism. They are composed of a series of amphipathic α-helices, which are organized into an N-terminal (NT) helix bundle domain and a smaller C-terminal (CT) domain. The objective of the current study is to understand the functional and structural role of the domains of these proteins by “domain swapping” using apoE3 and apoAI, both of which bear a 4-helix bundle in their NT domain, and apolipophorin III (apoLp-III), a monomeric one-domain model apolipoprotein. A series of chimeric apolipoproteins were generate: apoE3-NT/apoAI-CT, apoAI-NT/apoE-CT and apoLp-III/apoA-I-CT. The α-helical content of the chimeras was comparable to that of the parent proteins. Unfolding studies indicated that addition of CT-apoE3 to NT-apoAI conferred more stability to apoAI. While addition of CT-apoAI to NT-apoE3 had no significant effect on the stability of apoE3, addition of NT-apoAI to apoLp-III increased the stability of apoLp-III. Moreover, apoLp-III switched from a monomeric to an oligomeric protein upon addition of CT-apoAI, showing that CT-apoAI has a strong tendency to self-associate. Addition of CT-apoAI to NT-apoE or apoLp-III increased the lipid binding activity by ~ 10-fold, while addition of apoE-CT to apoA-I-NT had no measurable effect on the lipid binding activity. All three chimeras promote ABCA1-mediated cholesterol efflux from J774 macrophages, with the efflux capability being highest for apoAI-NT/apoE-CT. Whereas apoE3-NT/apoAI-CT elicits LDLr binding ability, apoAI-NT/apoE-CT did not. These results suggest that CT of apoAI is a strong promoter of lipid binding, while CT of apoE3 can improve cholesterol efflux ability of apoAI.

Lipopolysaccharide binding of an exchangeable apolipoprotein, apolipophorin III, from Galleria mellonella

2004 ◽  
Vol 385 (11) ◽  
pp. 1113-1119 ◽  
Author(s):  
Cindy C. Pratt ◽  
Paul M.M. Weers
Keyword(s):  
Galleria Mellonella ◽  
Locusta Migratoria ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Progressive Increase ◽  
Binding Interaction ◽  
Apolipophorin Iii ◽  
Exchangeable Apolipoprotein ◽  
Lps Binding

AbstractA new role of apolipophorin III (apoLp-III) as an immune activator has emerged recently. To gain insight into this novel function, the interaction of apoLp-III with lipopoly-saccharide (LPS) was investigated. ApoLp-III fromGalleria mellonellawas incubated with LPS fromEscherichia coliO55:B5, and analyzed by non-denaturing polyacrylamide gel electrophoresis (PAGE). Protein staining showed that apoLp-III mobility was significantly reduced. In addition, silver and LPS fluorescent staining demonstrated that LPS mobility was increased upon incubation with apoLp-III. This result suggests association of apoLp-III with LPS. Sodium dodecyl sulfate (SDS) PAGE analysis showed decreased apoLp-III mobility upon LPS addition, indicative of LPS apoLp-III interaction in the presence of SDS. The unique tyrosine residue that resides in apoLp-III was used to provide additional evidence for LPS binding interaction. In the absence of LPS, apoLp-III tyrosine fluorescence was relatively low. However, LPS addition resulted in a progressive increase in the fluorescence intensity, indicating tertiary rearrangement in the environment of tyrosine 142 upon LPS interaction. Other well-characterized apoLp-IIIs were also examined for LPS binding.Manduca sexta,Bombyx moriandLocusta migratoriaapoLp-III were all able to interact with LPS. The ability of apoLp-III to form complexes with LPS supports the proposed role of apoLp-III in innate immunity.

Role of Buried Polar Residues in Helix Bundle Stability and Lipid Binding of Apolipophorin III:  Destabilization by Threonine 31†

Biochemistry ◽  
2005 ◽  
Vol 44 (24) ◽  
pp. 8810-8816 ◽  
Author(s):  
Paul M. M. Weers ◽  
Wazir E. Abdullahi ◽  
Jamie M. Cabrera ◽  
Tzu-Chi Hsu
Keyword(s):  
Lipid Binding ◽  
Helix Bundle ◽  
Apolipophorin Iii ◽  
Polar Residues
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