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  • 1
    Electronic Resource
    Electronic Resource
    A Hydroxyproline-Containing Protein from Shark Brain That Is Related to Myelin Basic Protein (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 55 (1990), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Myelin basic protein (MBP) from shark (Chondricthyes) consists of a simpler mixture of charge isomers than human MBP. About two-thirds of the total amount applied to a CM-52 cellulose cation-exchange column was recovered in the unbound fraction of the column; the remaining one-third bound to column and was eluted as a single OD280 peak. This bound material did not show the usual pattern of charge microheterogeneity found with human or bovine MBP. The unbound fraction was composed of a high molecular weight protein (55–60 kDa), which constituted most of this protein fraction and a low molecular weight protein (∼ 18 kDa). The amino acid composition of our unbound fraction was similar to that reported earlier. The Glx (glutamic acid + glutamine) was increased about threefold whereas the Arg content was only about 25% of that of the 18.5 kDa variant of bovine or human origin. The presence of hydroxyproline (1.2 residues/100) in this protein was noteworthy, identification of which was achieved by amino acid analysis in two different systems and by mass spectrometry. In the precolumn derivatization method, hydroxyproline eluted at 2.7 min; in the postcolumn derivatization method it eluted at 12.2 min. Identification of hydroxyproline was completed by fast atom bombardment-mass spectral analysis. The effect of hydroxyproline on the secondary structure of this protein is being studied. Verification that this high molecular weight protein contained MBP sequences within its primary structure was confirmed by immunological methods. Good reactivity, comparable to that found with human MBP was observed in the enzyme-linked immunosorbent assay with an antibody (S-53) raised in rats against the synthetic peptide GSLPQKAQRPQDEN. The fraction that bound to the CM-52 cellulose column and was eluted with a salt gradient corresponded in net charge to component 5 of the bovine or human MBPs as deduced by alkaline gels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1990.tb04958.x
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of a highly purified myelin protein (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 4756-4763 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00801a024
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  • 3
    Electronic Resource
    Electronic Resource
    Conformational flexibility of a myelin protein (1973)
    s.l. : American Chemical Society
    Biochemistry 12 (1973), S. 3402-3406 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00742a006
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  • 4
    Electronic Resource
    Electronic Resource
    Lipid phase separation induced by a hydrophobic protein in phosphatidylserine-phosphatidylcholine vesicles (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 2325-2329 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00630a003
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  • 5
    Electronic Resource
    Electronic Resource
    Conformational studies on carbon-13-enriched human and bovine myelin basic protein, in solution and incorporated into liposomes (1978)
    s.l. : American Chemical Society
    Biochemistry 17 (1978), S. 898-903 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00598a024
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  • 6
    Electronic Resource
    Electronic Resource
    Interaction of glycosylated human myelin basic protein with lipid bilayers (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 4209-4216 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00436a013
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  • 7
    Electronic Resource
    Electronic Resource
    Peptidylarginine deiminase: a candidate factor in demyelinating disease (2002)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 81 (2002), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In earlier studies we demonstrated that an increase in the relative amounts of citrullinated myelin basic protein (MBP) was found in multiple sclerosis (Moscarello et al. 1994). To determine the temporal relationship between the citrullinated MBP and peptidylarginine deiminase (PAD), the enzyme responsible for deiminating arginyl residues in proteins, we studied enzyme activity, enzyme protein, PAD mRNA in a spontaneously demyelinating transgenic mouse model and we correlated the amount of PAD with citrullinated MBP. Both PAD protein as measured in an immunoslot blot method and PAD RNA were elevated. In fractionation studies we showed that the increase in PAD enzyme was due to an increase in the PAD found in membrane fractions and not the soluble PAD (PADII). From our data we concluded that up-regulation of myelin-associated PAD was responsible for the increase in citrullinated MBP in our transgenic mice prior to onset of clinical or pathological signs of demyelination. We postulate that a similar mechanism may be responsible for the increase in citrullinated MBP in multiple sclerosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2002.00834.x
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  • 8
    Electronic Resource
    Electronic Resource
    Prostaglandins in inflammatory bone pathology: Mechanism and therapeutic benefit of etodolac (1989)
    Springer
    Inflammation research 26 (1989), S. 310-318 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To investigate the role of PGE2 in the development of bone and joint pathology in rat adjuvant arthritis, hindlimb paws were evaluated by calcified tissue histologic techniques focusing on histochemical visualization of cartilage and bone lesions. Case studies of hindlimbs from normal, adjuvant arthritic, and etodolac-treated arthritic rats demonstrated the association of disease severity with inflammation, chondromalacia, replacement of adipose bone marrow with a fibroid marrow, osteoclastic bone resorption, synovial cysts, and pannus formation within the joints. Extensive periosteal intramembranous bone formation was temporally associated with joint destruction and medullary tissue pathology.In vivo data were correlated within vitro effects of inflammatory mediators (IL-1, PGE2) on bone resorption. Etodolac blocked bone explant PGE2 accumulation at concentrations of 10−7 M and higher, and inhibited bone resorption at concentrations of 10−5 M and higher. The data indicate thatin vitro andin vivo models of bone metabolism are well correlated regarding prostaglandin synthesis; that the inflammatory mediator PGE2 is largely responsible for the involvement of skeletal tissue in the adjuvant arthritis model; and that the effects of etodolac are specifically mediated by its ability to inhibit PGE2 accumulationin vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01967295
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  • 9
    Electronic Resource
    Electronic Resource
    Inhibition of prostaglandin biosynthesis by etodolac. I. Selective activities in arthritis (1987)
    Springer
    Inflammation research 21 (1987), S. 160-166 
    Details
    ISSN: 1420-908X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Etodolac is the first anti-inflammatory drug belonging to the tetrahydropyranoindole class. In contrast to several other common anti-inflammatory drugs, etodolac exhibited an unusually high potency as an inhibitor of established adjuvant arthritis relative to its activity against carrageenan paw edema in the rat. This phenomenon led us to investigate whether the ability of NSAIDs to inhibit prostaglandin biosynthesis differed between cultures of macrophages, which are present in inflammatory exudates, and cultures of synoviocytes and chondrocytes, which contribute to inflammation of the articulating joint. Although other anti-inflammatory drugs were found to be equally active in all three cell types, etodolac was found to be much more effective on the cells of the joint than on the macrophage. This differential activity may be responsible for the striking efficacy of etodolac as an anti-arthritic drug.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01974936
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  • 10
    Electronic Resource
    Electronic Resource
    Transmembrane orientation of lipophilin in phosphatidylcholine vesicles (1980)
    Springer
    Neurochemical research 5 (1980), S. 745-755 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Lipophilin, a hydrophobic myelin protein, was incorporated into phosphatidylcholine vesicles by dialysis from 2-chloroethanol which has been shown to produce single-layered lipid-protein vesicles. These vesicles were labeled with a nonpenetrating surface-labeling reagent, 4,4′-diisothiocyano-2,2′-ditritiostilbene disulfonic acid, ([3H]DIDS), in order to determine if the protein completely spans the bilayer. After labeling the vesicles, lipophilin was isolated. At least 88% of the protein was labeled with [3H]DIDS. Dextran (mol wt 250,000–275,000) was converted to the dialdehyde form and reacted with lipophilin-PC vesicles. In this case greater than 90% of the protein was complexed to the dextran. The high degree of labeling obtained with both compounds was consistent with a model in which lipophilin was considered to span the bilayer completely.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964712
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