Myelin proteolipid protein

DPDPB has been used to study the endocytosis of cadherin from intracellular junctions (Troyanovsky et al., 2006), the subunit arrangement in the flagellar rotor assembly (Lowder et al., 2005), and the disease-associated mutations in myelin proteolipid protein in the endoplasmic reticulum (ER) (Swanton et al., 2005). DPDPB can be used to conjugate reduced antibody molecules to p-D-galactosidase using essentially the same protocol as that described by O Sullivan et al. (1979). 

Swanton, E., Holland, A., High, S., and Woodman, P. (2005) Disease-associated mutations cause premature oligomerization of myelin proteolipid protein in the endoplasmic reticulum. PNAS 102, 4342-4347. 

Greer, J. M. and Lees, M. B. Myelin proteolipid protein-the first 50 years. Int. J. Biochem. Cell. Biol. 34, 211-215,2002. 

Gudz, T. I., Schneider, T. E., Haas, T. A. et al. Myelin proteolipid protein forms a complex with integrins and may participate in integrin receptor signaling in oligodendrocytes. /. Neurosci. 22,7398-7407, 2002. 

Another, but less well defined, class of molecules, some of whose members mediate adhesion interaction, is the four-transmembrane domain family, which shares similar hydropathy plots and may have similar dispositions with respect to the phospholipid bilayer, for example the myelin proteolipid proteins, the connexins of gap junctions, the ryanodine receptor and others. 

Major myelin proteolipid proteins, PLP and DM-20. In 1951 Folch and Lees discovered that a substantial amount of proteins from brain white matter could be... 

Dal Canto MC, Calenoff M A, Miller SD, Vanderlugt CL (2000) Lymphocytes from mice chronically infected with Theiler s murine encephalomyelitis virus produce demyelination of organotypic cultures after stimulation with the major encephalitogenic epitope of myelin proteolipid protein. Epitope spreading in TMEV infection has functional activity. J Neuroimmunol 104 79-84. 

Kuchroo, V. K., Martin, C. A., Greer, J. M., Ju, S. T., Sobel, R. A., and Dorf, M. E. (1993) Cytokines and adhesion molecules contribute to the ability of myelin proteolipid protein-specific T cell clones to mediate experimental allergic encephalomyelitis. J. Immunol. 151, 4371-4382. 

The conformation of bovine myelin basic protein (MBP) in AOT/isooctane/water reversed micellar systems was studied by Waks et al. 67). This MBP is an extrinsic water soluble protein which attains an extended conformation in aqueous solution 68 but is more density packed at the membrane surface. The solubilization of MBP in the AOT reversed micelles depends on the water/AOT-ratio w0 68). The maximum of solubilization was observed at a w0-value as low as 5.56. The same value was obtained for another major protein component of myelin, the Folch-Pi proteolipid 69). According to fluorescence emission spectra of MBP, accessibility of the single tryptophane residue seems to be decreased in AOT reversed micelles. From CD-spectra one can conclude that there is a higher conformational rigidity in reversed micelles and a more ordered aqueous environment. 

Jimpy mouse, rumpshaker mouse, myelin-deficient (md) rat, shaking dog X-linked Proteolipid protein (PLP) Variable degrees of oligodendrocyte death and CNS myelin deficiency, decreased spacing at intraperiod line of compact CNS myelin see text 1,9,10,43,44... 

Hudson, L. D. Proteolipid protein gene. In R. A. Lazzarini (ed.), Myelin biology and disorders. San Diego, CA Elsevier Academic Press, 2004,401-420. 

Stecca, B., Southwood, C. M., Gragerov, A. et al. The evolution of lipophilin genes from invertebrates to tetrapods DM-20 cannot replace proteolipid protein in CNS myelin. /. Neurosci. 20,4002-4010, 2000. 

In the CNS of mammals, two proteins are needed to accomplish the dual role of adhesion at both myelin bilayer surfaces that P0 effects in the PNS. The four-trans-membrane-domain proteolipid protein (PLP) is likely to be responsible for adhesion of the extracellular surfaces, while the very basic cytoplasmic myelin basic protein... 

Kalwy, S. A. and Smith, R. Mechanisms of myelin basic protein and proteolipid protein targeting in oligodendrocytes. Mol. Membr. Biol. 11 67-78,1994. 

The most hydrophobic integral membrane proteins can be extracted into organic solvents such as mixtures of chloroform and methanol. One such proteolipid protein, the 23.5-kDa lipophilin, accounts for over half the protein of myelin.57 182 The purified protein from rat brain contains 66% of nonpolar amino acids and six molecules of covalently bound palmitic acid and other fatty acids per peptide chain in thioester linkage to cysteine side chains. This protein evidently has four transmembrane helical segments with the six fatty acid chains incorporated into the membrane bilayer. It also has cytoplasmic and extracellular loops, one of which binds inositol hexakisphosphate (Ins P-6). (Fig. 11-9).183 The myelin proteolipid is an essential component of the myelin sheath and defects in this protein are associated with some demyelinating diseases57 which are discussed in Chapter 30. 

The intramuscular injection of naked pDNA has also been evaluated for therapy of EAE, a mouse model of multiple sclerosis. The disease is induced in mice by s.c. injection of myelin basic protein (MBP) or proteolipid protein (PLP). In a recent study, mice were injected i.m. with pDNA encoding either IL-4/IgG or TGF / 48 hours prior to each MBP injection (on days zero and seven) (Piccirillo and Prud -homme, 1999). The disease severity was 70% lower in the IL-4/IgG or TGF / -treated mice and the mean clinical scores were significantly reduced in both groups. In addition, the IL-4 and TGF -treated mice had significantly reduced CNS inflammation, reduced T cell proliferative responses to MBP and low levels of the Th 1 cytokines IL-12 and IFN7. Thus, the pDNA therapy appeared to shift the mice to a Th2 response, which was therapeutic and reduced the severity of the disease. 

Knapp PE (1996) Proteolipid protein Is it more than just a structural component of myelin Dev Neurosci 18 297—308. 

PLP refers to proteolipid protein that is present in myelin. 

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