Abstract
In a recent analysis we classified amphipathic helix domains into a minimum of seven distinct classes. Four amphipathic helix classes are found in lipid-associating proteins: apolipoproteins, certain polypeptide hormones, polypeptide venoms and antibiotics, and certain complex transmem brane proteins. Three amphipathic helix classes are involved in both intra and intermolecular protein-protein interactions: calmodulin-regulated protein kinases, coiled-coil containing proteins that include the so-called leucine zipper, and globular helical proteins.
Three central hypothesis have been developed in our studies of the apolipoprotein class of amphipathic helixes: 1) The “Snorkel” hypothesis proposes that when the amphipathic helix is associated with phospholipid, amphipathic basic residues extend toward the polar face of the helix to insert their charged residues into the aqueous milieu: thus the entirety of the uncharged van der Waals’surface of the amphipathic helix is buried within the lipid. 2) We have formulated a hypothesis that Glutamyl residues located at positions 78 and 111 in apolipoprotein A-I on the nonpolar face of two amphipathic helical domains are critical to LCAT activation. 3) The hinged-domain hypothesis was proposed to explain the structural basis for the quantization of HDL subspecies, protein-protein interactions in HDL, and the HDL disc to sphere transformation.
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
J. P. Segrest, R. L. Jackson, J. D. Morrisett, and A. M. Gotto, Jr., FEBS Lett., 38:247 (1973).
J. P. Segrest, H. De Loof, J. G. Dohlman, C. G. Brouillette, and G. M. Anantharamaiah, Proteins, In press (1990).
C -C. Luo, W -H. Li, M. N. Moore, and L. Chan, J. Mol. Biol., 187:325 (1986)
G. M. Anantharamaiah, J. L. Jones, C. G. Brouillette, C. F. Schmidt, B. H. Chung, T. A. Hughes, A. S. Bhown, and J.P. Segrest, J.Biol. Chem., 260:10248 (1985).
G. M. Anantharamaiah, Synthetic peptide analogs of apolipoproteins, In: Methods of Enzymology, J. P. Segrest and J. J. Albers, eds., Academic Press, New York, 128:627 (1986).
R. M. Epand, A. Gawish, M. Iqbal, K. B. Gupta, C. H. Chen, J. P. Segrest, and G. M. Anantharamaiah, J. Biol. Chem., 262:9389 (1987).
Y. V. Venkatachalapathi, K. B. Gupta, H. De Loof, J. P. Segrest, and G. M. Anantharamaiah, In: Peptides, ESCOM Press (J. Rivier Ed.) 672 (1990)
C. J. Fielding, V. G. Shore, P. E. Fielding, Biophys. Biochem. Res. Cpmmun, 46:1493 (1972).
J. J. Albers, J. T. Lin, G. P. Roberts, Artery, 5:61 (1979)
G. M. Anantharamaiah, Y. V. Venkatachalapathi, C. G. Brouillette, and J. P. Segrest, Arteriosclerosis, 10:95 (1990).
C. G. Brouillette, J. L. Jones, T. C. Ng, H. Kercert, B. H. Chung, and J. P. Segrest, Biochemistry, 23:359 (1984)
A. Jonas, K. E. Kezdy, and J. H. Wald, J. Biol. Chem, 264:4818 (1989).
W. C. Cheung, J. P. Segrest, J. J. Albers, J. T. Cone, C. G. Brouillette, B. H. Chung, M. Kashyap,, A. Glasscock, and G. M. Anantharamaiah, J. Lipid Res., 28:913 (1987).
B. H. Chung, J. P. Segrest M. J. Ray, J. D. Brunzell, J. E. Hokanson, R. M. Krauss, K. Beaudrie, and J. T. Cone, Single vertical spin density gradient ultracentrifugation, In: Methods of Enzymology, J. P. Segrest and J. J. Albers, eds, Academic Press, New York, 128:181 (1986).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
Anantharamaiah, G.M. et al. (1990). Role of Amphipathic Helixes in HDL Structure/Function. In: Malmendier, C.L., Alaupovic, P., Brewer, H.B. (eds) Hypercholesterolemia, Hypocholesterolemia, Hypertriglyceridemia, in Vivo Kinetics. Advances in Experimental Medicine and Biology, vol 285. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5904-3_17
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5904-3_17
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5906-7
Online ISBN: 978-1-4684-5904-3
eBook Packages: Springer Book Archive