Alteration of the erythrocyte membrane via enzymatic degradation of ankyrin (band 2.1): subcellular surgery characterized by EPR spectroscopy

Hensley, Kenneth; Postlewaite, Jennifer; Dobbs, Pamela; Butterfield, Allan

doi:10.1016/0005-2736(93)90290-g

Cited by 19 publications

(6 citation statements)

References 37 publications

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“…Reaction sites that allow minimal rotation are termed "S sites" (strongly immobilized) , while those protein reaction sites that only mildly hinder rotation of the nitroxide radical are known as "W sites" (weakly immobilized). The ratio of the EPR spectral amplitude of the low-field weakly immobilized component to that of the strongly immobilized component (W/S ratio) has been shown by our laboratory and others (15-18,21, 23, 24, [26][27][28][29][30][31] as being a highly sensitive monitor of the conformation and association of membrane cytoskeletal proteins as well as accurately depicting the segmental motion of the protein reaction sites. For example, spermine, known to increase cytoskeletal protein-protein interactions, decreases the W/S ratio (28) while hemin, known to decrease the cytoskeletal membrane-protein interactions, increases the W/S ratio of MAL-6 bound to erythrocyte membranes (29).…”

Section: Resultsmentioning

confidence: 69%

“…Furthermore, spectrin in the dimeric state, with subsequently decreased cytoskeletal protein-protein interactions, has an increased W/S ratio that is returned to control values when spectrin is returned to the tetrameric state in the membrane (30). Similarly, proteolytic digestion of ankyrin, the connecting protein between spectrin in the cytoskeleton and a fraction of the transmembrane band 3 molecules, decreased proteinprotein interactions and increased the W/S ratio of MAL-6 (31). Others (24) report that our MAL-6 spin-labeling method (21) yields highly reproducible spectra that serve as excellent indicators of the state of membrane proteins.…”

Section: Resultsmentioning

confidence: 99%

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Effects of .beta.-(N-methylamino)-L-alanine on cytoskeletal proteins of erythrocyte membranes

Butterfield

Nc²,

Sj³

1993

Chem. Res. Toxicol.

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The interaction of the amino acid beta-(N-methylamino)-L-alanine, a neurotoxin found in the seed of the false sago palm, with erythrocyte membranes has been monitored by electron paramagnetic resonance techniques of spin labeling. This neurotoxin did not alter the motion or order of bilayer lipids, but a highly-significant and dose-dependent alteration in the physical state of cytoskeletal proteins was observed. These results are discussed in reference to potential mechanisms involved in the neurotoxicity produced by beta-(N-methylamino)-L-alanine and in reference to the unusual neurological disorders among the Chamorro population of Guam and other Marianas Islands.

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Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

Effects of .beta.-(N-methylamino)-L-alanine on cytoskeletal proteins of erythrocyte membranes

Butterfield

Nc²,

Sj³

1993

Chem. Res. Toxicol.

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“…Starting from the observation that spermine prevented the lateral diffusion of transmembrane proteins in erythrocyte ghosts (80), subsequent electron paramagnetic resonance studies demonstrated a pronounced decrease in the segmental motion of spin-labeled cytoskeletal proteins (mainly spectrin and the cytoplasmic pole of the anion transporter band 3) indicating a strengthening of cytoskeletal protein-protein interactions by spermine (81)(82)(83). As spectrin is rich in electronegative charges, it was hypothesized that spermine might link spectrin to the also negatively charged band 3 protein by bridging.…”

Section: Spectrin and The Cytoskeletonmentioning

confidence: 99%

Interactions of natural polyamines with mammalian proteins

Schuster

Bernhardt

2011

BioMolecular Concepts

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The ubiquitously expressed natural polyamines putrescine, spermidine, and spermine are small, flexible cationic compounds that exert pleiotropic actions on various regulatory systems and, accordingly, are essentially involved in diverse life functions. These roles of polyamines result from their capability to interact with negatively charged regions of all major classes of biomolecules, which might act in response by changing their structures and functions. The present review deals with polyamine-protein interactions, thereby focusing on mammalian proteins. We discuss the various modes in which polyamines can interact with proteins, describe major types of affected functions illustrated by representative examples of involved proteins, and support information with respective structural evidence from elucidated three-dimensional structures. A specific focus is put on polyamine interactions at protein surfaces that can modulate the aggregation of proteins to organized structural networks as well as to toxic aggregates and, moreover, can play a role in important transient protein-protein interactions.

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“…Therefore, if it is possible to obtain reliable information on the cytoskeletal interaction from force curve measurement, it would be a welcome new technology. Traditionally, interaction of membrane proteins with cytoskeletal proteins has been studied by, e.g., detergent extraction of unassociated proteins together with membrane lipids leaving those with association with cytoskeleton on the delipidated remains of the cell [66], or from the measurement of the rotational diffusion coefficient of labeled proteins [67]. It is, therefore, quite useful if AFM force curves can be used to distinguish membrane proteins with or without cytoskeletal associations as postulated by Afrin and Ikai.…”

Section: Iv4 Force Curves Showing Interaction With Cytoskeletal Strmentioning

confidence: 99%

Editorial [ Hot Topic: Nanomechanics (Guest Editors: Atsushi Ikai, Alastair Smith and Masaru Tsukada)]

Ikai¹,

Smith²,

Tsukada³

2007

Current Nanoscience

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This paper reviews a recent progress of molecular level studies on the rigidity of surface immobilized as well as membrane bound proteins embedded in the lipid bilayer. Some details and emphasis are given to the work done in our laboratory in the last few years. Immobilization of protein molecules on a solid surface through covalent crosslinkers on one side and to the probe of the atomic force microscope on the other enabled us to pull or push a single protein molecule to specified directions. On pulling, the internal structure of the protein molecule is mechanically opened up and, on pushing, it is compressively deformed until it is flattened out. Such experiments reveal the mechanical rigidity of the folded structure of a protein molecule in two different ways. In the field of ligand-protein interaction, some merits and problems of newly introduced compression free method are discussed. When a protein molecule is embedded in a lipid membrane, information on its anchoring force to the membrane can be obtained by pulling it out from the membrane. Experiments have been done either on a lipid bilayer formed on a solid surface, or on the surface of live cells. The extraction process of membrane proteins is often accompanied by extrusion of a thin lipid tether trailing behind the target protein of the tensile force. A short review of the tether forming process from the red cell membrane surface will be given.

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Alteration of the erythrocyte membrane via enzymatic degradation of ankyrin (band 2.1): subcellular surgery characterized by EPR spectroscopy

Cited by 19 publications

References 37 publications

Effects of .beta.-(N-methylamino)-L-alanine on cytoskeletal proteins of erythrocyte membranes

Effects of .beta.-(N-methylamino)-L-alanine on cytoskeletal proteins of erythrocyte membranes

Interactions of natural polyamines with mammalian proteins

Editorial [ Hot Topic: Nanomechanics (Guest Editors: Atsushi Ikai, Alastair Smith and Masaru Tsukada)]

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