scholarly journals Temperature gradients drive mechanical energy gradients in the flight muscle of Manduca sexta

2012 ◽  
Vol 215 (3) ◽  
pp. 471-479 ◽  
Author(s):  
N. T. George ◽  
S. Sponberg ◽  
T. L. Daniel
2012 ◽  
Vol 102 (3) ◽  
pp. 361a
Author(s):  
Chen-Ching Yuan ◽  
Jiangmin Liu ◽  
Thomas C. Irving
Keyword(s):  

2012 ◽  
Vol 102 (3) ◽  
pp. 148a
Author(s):  
Mohit Kumar ◽  
Peter Schemmel ◽  
Chen-Ching Yuan ◽  
Thomas C. Irving

1996 ◽  
Vol 74 (2) ◽  
pp. 155-164 ◽  
Author(s):  
Robert O. Ryan

Lipid transport processes via the circulatory system of animals are a vital function that utilizes highly specialized lipoprotein complexes. These complexes of protein and lipid impart solubility to otherwise insoluble lipids. The apoprotein components of lipoprotein complexes serve to stabilize the lipid components and modulate particle metabolism and function as ligands for receptor-mediated endocytosis of lipoproteins. We have used an insect (Manduca sexta) model system for studies of lipid transport. In this system, flight activity elicits a dramatic increase in the demand for glycerolipid fuel molecules by flight muscle tissue. These lipids are mobilized from a storage organ and transported through the hemolymph (blood) to the flight muscle by the lipoprotein, lipophorin. This system possesses the unique property that lipids are loaded onto pre-existing high density lipophorin through the action of a lipid transfer particle (LTP). LTP is a high molecular weight hemolymph component that facilitates net vectorial lipid transfer from fat body tissue to lipophorin. The increase in lipid content of the lipoprotein induces association of a low molecular weight amphipathic exchangeable apolipoprotein, apolipophorin III (apoLp-III). ApoLp-III is a 18 kDa protein that normally exists as a water-soluble monomeric hemolymph protein. The structural properties of apoLp-III have been investigated by X-ray crystallography. ApoLp-III from Locusta migratoria adopts a five helix bundle conformation wherein each of the amphipathic helices orients with its hydrophobic face directed toward the interior of the bundle. It has been hypothesized that lipid association requires a dramatic conformational change wherein the helix bundle opens about putative hinge domains located in the loops between helices. The data accumulated support the concept that apoLp-III is a member of the broad class of exchangeable apolipoproteins and structural information learned from this system is directly applicable to analogous proteins in higher organisms.Key words: lipid transport, apoprotein, lipoprotein, Manduca sexta, diacylglycerol.


2013 ◽  
Vol 2013 ◽  
pp. 1-4 ◽  
Author(s):  
Wei-Rong Zhong ◽  
Zhi-Cheng Xu ◽  
Ming-Ming Yang ◽  
Bao-Quan Ai

Transport of helium atoms in the carbon nanotubes is investigated in the presence of temperature gradients. The heat current flowing along the carbon nanotubes can induce a stable directed transport of helium; it is demonstrated that the heat current density rather than the temperature gradient performs as a fundamental physical factor to the mass transport. We provide an alternative route to control the mass transport by using heat. Our results reported here are also relevant for understanding the transition from thermal energy to mechanical energy.


2010 ◽  
Vol 98 (3) ◽  
pp. 348a-349a ◽  
Author(s):  
Nicole T. George ◽  
Jiangmin Liu ◽  
Lacy Simons ◽  
Thomas L. Daniel ◽  
Thomas C. Irving
Keyword(s):  

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