Lipid and basic protein interaction in myelin

Banik, Naren L.; Davison, Alan

doi:10.1042/bj1430039

Cited by 58 publications

(20 citation statements)

References 50 publications

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“…Methionine residues were successfully regenerated by treatment with thioglycollic acid. The specific interaction of the myelin basic protein with acidic lipids reported by Palmer & Dawson (1969) and Banik & Davison (1974) has been confirmed in the present study. The observation that neither peptide fragment showed any interaction with complex lipids such as cerebroside, sphingomyelin and phosphatidylcholine is not surprising, since this is also the case for the intact basic protein ; the present work).…”

Section: Resultssupporting

confidence: 89%

“…For a two-phase system to study lipid interaction with protein (Palmer & Dawson, 1969;Banik & Davison, 1974) samples of lipid (up to 400ug) were evaporated under N2 in stoppered test tubes. Chloroform/methanol (2:1, v/v; 1.Oml) was added to each tube, followed by 0.25 ml of lOmM-Tris/HCI buffer, pH7.0, which contained about 100,ug of protein.…”

Section: Methodsmentioning

confidence: 99%

“…The myelin basic protein interacts specifically with acidic-lipids (Banik & Davison, 1974;Palmer & Dawson, 1969). Further detailed studies indicate that the N-terminal region of the basic protein (residues 20-113) interacts in a different manner compared with the rest of the protein molecule (Gould & London, 1972;Demel et al, 1973;.…”

mentioning

confidence: 98%

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Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein

Jones¹,

Rumsby²

1977

Biochemical Journal

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The myelin basic protein from bovine brain tissue was purified and the two peptides obtained by cleavage of the polypeptide chain at the single tryptophan residue were isolated. The interaction of these peptides and the intact basic protein with complex lipids was investigated by following the solubilization of lipid-protein complexes into chloroform in a biphasic solvent system. The C-terminal peptide fragment (residues 117-170) and the intact basic protein both formed chloroform-soluble complexes with acidic lipids, but not with neutral complex lipids. The N-terminal fragment (residues 1-115) did not form chloroform-soluble complexes with either acidic or neutral complex lipids. The molar ratio of lipid to protein that caused a 50 % loss of protein from the upper phase to the lower chloroform phase was the same for the intact basic protein as for the smaller C-terminal peptide fragment. Phosphatidylserine and phosphatidylinositol were approximately twice as efficient as sulphatide at causing protein redistribution to the chloroform phase. The results are interpreted as indicating that the sites for ionic interactions between lipid and charged groups on the basic protein of myelin are located in the C-terminal region of the protein molecule.

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Section: Resultssupporting

confidence: 89%

Section: Methodsmentioning

confidence: 99%

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Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein

Jones¹,

Rumsby²

1977

Biochemical Journal

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“…Steck et al (1976) reported that this binding could be reduced by acylating a number of the lysyl residues on the protein, presumably by reducing its net positive charge. Evidence that portions of the basic protein could extend into a lipid bilayer also has been presented (Boggs & Moscarello, 1978). These and other studies Demel et al, 1973;Smith, 1977a) support the notion that MBP can interact with both the hydrophobic and hydrophilic portions of lipid bilayers.…”

mentioning

confidence: 53%

Interactions of free and immobilized myelin basic protein with anionic detergents

Burns¹,

Campagnoni²,

Chaiken³

et al. 1981

Biochemistry

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The interaction of free and immobilized myelin basic protein (MBP) with sodium deoxycholate (DOC) and sodium dodecyl sulfate (NaDodSO,) was studied under a variety of conditions. Free MBP formed insoluble complexes with both detergents. Analysis of the insoluble complexes revealed that the molar ratio of detergent/MBP in the precipitate increased in a systematic fashion with increasing detergent concentration until the complex became soluble. At pH 4.8, equilibrium dialysis studies indicated that N 15 mol of NaDodS04 could bind to the protein without precipitation occurring. Regardless of the surfactant, however, minimum protein solubility occurred when the net charge on the protein-detergent complex was between +18 and -9. Complete equilibrium binding isotherms of both detergents to the protein were obtained by using MBP immobilized on agarose. The %e myelin basic protein (MBP)' is a low molecular weight, highly charged, peripheral membrane protein which constitutes

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“…Basic protein in situ in purified myelin is easily hydrolysed by acetylated trypsin (Wood et al, 1974;Banik & Davison, 1974), and purified basic protein is hydrolysed by purified brain acid proteinase (Einstein et al, 1968), Pronase, and elastase (M. E. Smith, unpublished work). When associated with myelin lipid, basic protein may be partially protected from the activity of proteolytic enzymes (London & Vossenberg, 1973).…”

Section: Discussionmentioning

confidence: 99%

Enzymic hydrolysis of myelin basic protein and other proteins in central nervous system and lymphoid tissues from normal and demyelinating rats

Buletza¹,

Smith²

1976

Biochemical Journal

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Proteolytic activity of central-nervous-system tissue of the normal rat was examined over the pH range 2-9 with casein, haemoglobin and myelin basic proteii as substrates. With casein as a substrate, brain and spinal cord homnogenates showed very similar activity profiles with increasing pH, with the min peaks of proteolytic activity at pH3-4 and 5-6.When haemoglobin was used, one broad main peak ofactivity fromn pH 3 to 5 was demonstrated. There was no optimum pH, however, for proteolytic activity with myelin basic protein as a substrate, and considerable hydrolysis were observed from pH3.5 up to pH8. Proteolytic activity at the various pH values was compared by using homogentaws of spinal cords from rats with acute expenniental allergic encephalomyelitis and those from rats injected with Freund's adjuvant alone. The profiles ofactivity were similar with peaks at pH 3.5 and 5.5 with casein as a substrate, but the specific activity was significantly higher at most pH values in the spinal-cord homogenates from rats with experimental allergic encephalomyelitis. Sinilarly the spinal.'rd homogenates from these latter rats contained much more proteolyticactivitytoward myelin basic protein throughout the pH range than was present in the control spal cords. Homogenates from lymph nodes of rats with experimental allergic encephalomyelitis and from those of the controls contained two to three times as much proteolytic activity as that of the central-nervous-system tissue and had a different proteolytic actvity profile from that of the central nervous system, with higher activity at the neutral than at acid pH. The results are discussed with regard to

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Lipid and basic protein interaction in myelin

Cited by 58 publications

References 50 publications

Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein

Localization of sites for ionic interaction with lipid in the C-terminal third of the bovine myelin basic protein

Interactions of free and immobilized myelin basic protein with anionic detergents

Enzymic hydrolysis of myelin basic protein and other proteins in central nervous system and lymphoid tissues from normal and demyelinating rats

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