Specific interaction of central nervous system myelin basic protein with lipids. Specific regions of the protein sequence protected from the proteolytic action of trypsin

London, Y.; Vossenberg, F.G.A.

doi:10.1016/0005-2736(73)90295-2

Cited by 105 publications

(5 citation statements)

References 32 publications

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“…As methylation of arginine increases the hydrophobicity of MBP, methylation may be necessary to stabilize the binding of the protein to the hydrophobic environment of myelin. Studies on isolated myelin have shown that the region around the methylarginine residue is resistant to tryptic digestion (London and Vossenberg, 1973). This region of the protein may therefore be tightly associated with the myelin membrane.…”

Section: Discussionmentioning

confidence: 99%

In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein

Small

Carnegie

1982

Journal of Neurochemistry

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The amino acid sequence around the sole methylarginine residue in chicken myelin basic protein was determined and was found to be similar to that previously reported for mammalian myelin basic protein. The ratio NG, N'G-dimethylarginine: NG-monomethylarginine:arginine was approximately 1.3:0.9:1.0. No NG, NG-dimethylarginine was detected in the protein. The in vivo incorporation of methyl groups from [methyl-3H]methionine into methylarginines in myelin was found to occur readily in 2-day-old chickens. Radioactively labelled NG,N'G-dimethylarginine and NG-monomethylarginine in myelin were derived solely from myelin basic protein. Radioactivity was also incorporated into NG,NG-dimethylargnine, although this was not derived from myelin basic protein. As NG-monomethylarginine was easily separated from the dimethylarginines, and as it was derived from myelin basic protein, it may be a good marker for myelin basic protein turnover in vivo. A time course study of the incorporation showed that radioactivity was incorporated into NG-monomethylarginine up to 6 h after injection, and decayed slowly, with an apparent half-life of about 40 days.

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Section: Discussionmentioning

confidence: 99%

In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein

Small

Carnegie

1982

Journal of Neurochemistry

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“…These investigators presume that the charged groups of the polypeptides interact with the phosphate groups which form a fixed layer of negative charge at the PC-water interface. In general, electrostatic interactions between charged phospholipid vesicles and oppositely charged proteins and polypeptides result in stable complexes where subsequent hydrophobic interactions direct the rearrangement of protein and lipid in these complexes (Hammes and Schullery, 1970;Kimelberg and Papahadjopulos, 1971;London and Vossenberg, 1973). Certainly as a carrier of PC, the exchange protein does not form a stable complex with the interface.…”

Section: Discussionmentioning

confidence: 99%

Specificity of the phosphatidylcholine exchange protein from bovine liver

Kamp¹,

Wirtz²,

Baer³

et al. 1977

Biochemistry

120

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The phosphatidylcholine exchange protein from bovine liver stimulates the specific transfer of phosphatidylcholine (PC) from rat liver microsomes to mitochondria or phospholipid vesicles (Wirtz, K.W.A., Kamp, H.H., and van Deenen, L.L.M. (1972), Biochim. Biophys. Acta 274, 606). In the present study, it has been established which components of the PC molecule are essential to the specific interaction with the protein. Radiochemically labeled analogues of PC have been synthesized with modifications in the polar and apolar moiety, and their transfer was measured between donor and acceptor vesicles. Relative to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphorylcholine (egg yolk PC), transfer is inhibited or abolished when (a) the distance between phosphorus and nitrogen is decreased or increased and (b) a methyl group on the quaternary nitrogen is removed or substituted by an ethyl or propyl group. Transfer is much less affected when (a) the ester bonds are replaced by ether or carbon-carbon bonds, (b) the PC molecule contains two saturated fatty acids, and (c) the D stereoisomer is used. It is concluded that the protein has a binding site which interacts specifically with the phosphorylcholine head group and which cannot accommodate substantial configurational changes. Interaction with the apolar moiety of PC is less specific. However, lyso-PC is not transferred, suggesting that two hydrocarbon chains are required to stabilize the exchange protein-phospholipid complex. Interaction of [14C]PC-labeled exchange protein with vesicles of different phospholipid compositon has been analyzed by measuring the release of [14C]PC into these vesicles. Vesicles of egg PC or dimethylphosphatidylethanolamine function as acceptors, in contrast to vesicles of sphingomyelin or phosphatidylethanolamine.

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“…London and Vossenberg [18] showed that myelin basic protein is protected against the proteolytic action of trypsin and similar enzymes when the protein binds cerebroside sulfate or other acidic phospholipids. Based on the equal distribution of the arginine residues throughout the basic protein molecule these lipids may be attached primarily to the arginine residues thus providing further evidence for the parallelism between TBR and acidic phospholipid binding.…”

Section: Discussionmentioning

confidence: 99%

The solution behavior of the bovine myelin basic protein in the presence of anionic ligands binding behavior with the red component of trypan blue and sodium dodecyl sulfate

Liebes

Zand

Phillips

1976

Biochimica et Biophysica Acta (BBA) - Protein Structure

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The interaction of the azo dye (2,3'-dimethyldiphenyl-7-azo-8-amino-1-napthol 3,6-disulfonic acid (TBR) and sodium dodecyl sulfate with the bovine myelin basic protein has been studied using absorbance, circular dichroism and 220 MHz PMR spectroscopy. Additional analyses of the binding reaction were carried out using light scattering, ultracentrifugal and electrophoretic techniques. A procedure for preparing pure TBR was developed. A modified structure for this synthesized TBR has been suggested. The mechanism of TBR binding to the myelin basic protein was found to be metachromatic. In addition, the interaction of TBR with the basic protein which gives rise to aggregation of the dye bound species was found to be analogous to the model proposed by Schwarz, G. and Seelig-Löffler, A. ((1975) Biochim. Biophys. Acta 379, 125-138) to explain the binding of acridine orange with poly (alpha-L-glutamic acid). PMR spectral analyses suggested that arginine residues provide the majority of primary sites of attachment on the basic protein for TBR. The effect of sodium dodecyl sulfate binding with the bovine myelin basic protein was found to induce a minimal change in the conformation of the protein. The induction of only about 20% alpha helial structure could be demonstrated and the binding was reversed by raising the solution temperature to 73 degrees C. The difference in the observed behavior of basic protein arising from TBR binding as opposed to the binding of sodium dodecyl sulfate is viewed as resulting from two different binding mechanisms. The binding behavior of TBR is primarily a consequence of charge-charge interaction while the binding effects of sodium dodecyl sulfate are a consequence of hydrophobic interaction. The sodium dodecyl sulfate binding acts as a shield which limits charge-charge interaction in the basic protein molecule thus preventing aggregate formation while TBR imposes no such restraints.

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Specific interaction of central nervous system myelin basic protein with lipids. Specific regions of the protein sequence protected from the proteolytic action of trypsin

Cited by 105 publications

References 32 publications

In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein

In Vivo Methylation of an Arginine in Chicken Myelin Basic Protein

Specificity of the phosphatidylcholine exchange protein from bovine liver

The solution behavior of the bovine myelin basic protein in the presence of anionic ligands binding behavior with the red component of trypan blue and sodium dodecyl sulfate

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