Brain slices obtained from young rats were incubated with different radioactive precursors, in the presence and absence of L-cycloserine (an inhibitor of the synthesis of sphingosine) in order to explore the possibility that transport of proteolipids-and specifically of the major myelin proteolipid
Vesicular transport of myelin proteolipid and cerebroside sulfates to the myelin membrane
β Scribed by M. C. Brown; M. Besio Moreno; E. R. Bongarzone; P. D. Cohen; E. F. Soto; Dr. J. M. Pasquini
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 719 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0360-4012
No coin nor oath required. For personal study only.
β¦ Synopsis
The possibility that cerebroside sulfates and myelin proteolipid (PLP) could be simultaneously located in transport vesicles destined to be assembled in myelin was investigated in the brain of 20 day old rats. The brain was homogenized and fractionated according to Burkart et al. (J B i d Chem 257:3151-3156, 1982) to obtain a microsomal fraction that was further subfractionated in a linear sucrose density gradient following the procedure of Siegrist et al. (J Neurochern 33:497-504, 1979) to obtain a vesicular fraction which has been shown to transport cerebroside sulfates (Burkart et al., as above)
. This fraction was associated with acid bydrolase activity and bad a lipid composition different from that of myelin and microsomal fractions. Studied by slab gel electropboresis, dot blot, and Western blot analysis, using a highly specific anti-PLP antibody, it was found to contain myelin PLP. In view of previous findings of several laboratories including our own, the presence of myelin proteolipid in a vesicular fraction which is related to the transport of cerebroside sulfates gives further support to the hypothesis that the delivery of both constituents to the myelin membrane could be associated.
π SIMILAR VOLUMES
## Abstract The proteolipid (PLP) gene encodes at least four proteins, including the classic PLP and DM20, which are important components of the myelin sheath, and the recently identified somaβrestricted (sr) isoforms, srPLP and srDM20. The classic PLP and DM20 gene products have been implicated in
The four transmembrane domain topology of the proteolipid protein (PLP) in the myelin membrane of the central nervous system (CNS) has been further substantiated by biochemical studies. We have analyzed the cotranslational polytopic integration of nascent PLP during protein synthesis into the membra
The possibility that transport of proteolipid protein (PLP) from its site of synthesis to the plasma membrane is dependent on cotransport with (sulfo)galacto-cerebrosides was investigated in primary cultured oligodendrocytes and Chinese hamster ovary (CHO) cells expressing PLP. Sulfation was inhibit
## Abstract Uso1 is a yeast essential protein that functions to tether vesicles in the ERβtoβGolgi transport. Its recruitment to the ERβderived vesicles has been demonstrated in in vitro membrane transport systems using semiβintact cells. Here we report that the binding of Uso1 to specific membrane