Laboratory of Molecular Neuroscience   printer friendly

Lipoprotein- and membrane research

Using carbon-13 labelled phospho-and sphingolipids in NMR-spectroscopic studies on reconstituted high density lipoproteins (HDL) provided insight into apolipoprotein-lipid interaction studies as well as lipid-membrane protein interactions. A generally accepted model for high density lipoprotein has be elaborated. The biosynthesis and processing of apolipoprotein preproapo AI and AII has been elucidated in in vitro systems.

The Low Density Lipoprotein (LDL) apheresis has been developed as an efficient treatment method of homozygous and severe heterozygous familiar hypercholesterolemic patients. This method is being applied in several clinical centres around the world. LDL-apheresis paved the way for further immunoabsorption apheresis applications in medicine.

References
  1. Wahle, S. and Stoffel, W. 1998 Cotranslational Integration of Myelin Proteolipid Protein (PLP) into the Membrane of Endoplasmic Reticulum:Analysis of Topology by Glycosylation Scanning and Protease Domain Protection Assay GLIA 24, 226-235
  2. D. Boison, H. Büssow, D. D'Urso, H.-W. Müller and W. Stoffel Adhesive properties of proteolipid protein are responsible for the compaction of CNS myelin sheaths J. Neurosc., 15(8), 5502-5513 (1995)
  3. R. Gutierrez, D. Boison, U. Heinemann, W. Stoffel Decompaction of CNS myelin leads to a reduction of the conduction velocity of action potentials in optic nerve. Neurosc. Letters 195, 93-96 (1995)
  4. D. Boison, W. Stoffel Disruption of the compacted myelin sheath of axons of the central nervous system in proteolipid protein-deficient mice Proc. Natl. Acad. Sci. USA 91, 11709-11713 (1994)
  5. T. Weimbs, W. Stoffel Topology of CNS myelin proteolipid protein. Evidence for the non-enzymatic glycosylation of extracytoplasmic domains in normal and diabetic animals Biochem., 33, 10408-10415 (1994)
  6. R. Janz, W. Stoffel Characterization of a brain-specific SP1-like activity interacting with an unusual binding site within the myelin proteolipid protein promoter Biol. Chem. Hoppe-Seyler, 374, 507-517 (1993)
  7. T. Weimbs, W. Stoffel Proteolipid protein (PLP) of CNS myelin: positions of free, disulfide bonded, and fatty acid thioester-linked cysteine residues. Implications for the membrane topology of PLP Biochem., 31, 12289-12296 (1992)
  8. F. Schließ, W. Stoffel Evolution of the myelin integral membrane proteins of the central nervous system. Biol. Chem. Hoppe-Seyler, 372, 865-874 (1991)
  9. W. Stoffel The myelin membrane of the central nervous system. Essential macromolecular structure and function Angew. Chem. Int. Ed., 29, 958-976 (1990)
  10. T. Weimbs, T. Dick, W. Stoffel, E. Boltshauser A point mutation at the X-chromosomal proteolipid protein locus in Pelizaeus-Merzbacher disease leads to disruption of myelinogenesis Biol. Chem. Hoppe-Seyler, 371, 1175-1183 (1990)
  11. R. Streicher, W. Stoffel The organization of the human myelin basic protein gene Biol. Chem. Hoppe-Seyler, 370, 503-510 (1989) D. Boison, W. Stoffel
  12. D. Boison, W. Stoffel Myelin-deficient rat: a point mutation in exon III (AÆC, Thr75ÆPro) of the myelin proteolipid protein causes dysmyelination and oligodendrocyte death EMBO J., 8, 3295-3302 (1989)
  13. W. Stoffel, T. Subkowski, S. Jander Topology of proteolipid protein in the myelin membrane of central nervous system Biol. Chem. Hoppe-Seyler, 370, 165-176 (1989)
  14. D. Boison, W. Stoffel Myelin-deficient rat: a point mutation in exon III (AgC, Thr75Pro) of the myelin proteolipid protein causes dysmyelination and oligodendrocyte death EMBO J., 8, 3295-3302 (1989)
  15. M. Schaich, R.-M. Budzinski, W. Stoffel Cloned proteolipid protein and myelin basic protein cDNA Biol. Chem. Hoppe-Seyler, 367, 825-834 (1986)
  16. H.-J. Diehl, M. Schaich, R.-M. Budzinski, W. Stoffel Individual exons encode the integral membrane domains of human myelin proteolipid protein Proc. Natl. Acad. Sci. USA, 83, 9807-9811 (1986)
  17. W. Stoffel, H. Giersiefen, H. Hillen, W. Schröder, B. Tunggal Amino-acid sequence of human and bovine brain myelin proteolipid protein (lipophilin) is completely conserved Biol. Chem. Hoppe-Seyler, 366, 627-635 (1985)
  18. W. Stoffel, H. Hillen The primary structure of bovine brain myelin lipophilin (proteolipid apoprotein) Hoppe-Seyler's Zeitschr. Physiol. Chemie, 364, 1455-1466 (1983)
  19. W. Stoffel, W. Schröder, H. Hillen, R. Deutzmann Lipophilin (proteolipid apoprotein) of brain white matter. Purification and amino acid sequence studies of the four tryptophan fragments Hoppe-Seyler's Zeitschr. Physiol. Chemie, 363, 1397-1407 (1982)
  20. W. Stoffel, W. Schröder, H. Hillen, R. Deutzmann Analysis of the primary structure of the strongly hydrophobic brain myelin proteolipid apoprotein (lipophilin). Isolation and amino acid sequence determination of proteolytic fragments Hoppe-Seyler's Zeitschr. Physiol. Chemie, 363, 1117-1131 (1982)


July 12, 2011
Center for Biochemistry, Joseph-Stelzmann-Straße 52, D50931 Cologne
Suggestions and wishes: Budi Tunggal
Voice: +49 221 4786930, Fax: +49 221 4786979
dummy