Expression of plasmolipin in the developing rat brain

Sapirstein, Victor S.; Nolan, Charles E.; Stadler, István; Fischer, Itzhak

doi:10.1002/jnr.490310114

Cited by 11 publications

(6 citation statements)

References 22 publications

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“…1996), which clearly confined plasmolipin transcripts to oligodendrocytes and myelinating Schwann cells of the CNS and PNS, respectively. Further, the post‐natal developmental expression profiles of plasmolipin protein in rat brain (Sapirstein et al . 1992b) and sciatic nerve (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…As myelin is a very specialized laminar membraneous organelle with common characteristics of apical epithelial membranes and as an asymmetric plasmolipin distribution appeared to occur in nephron tubuli (Sapirstein et al . 1992b), we carefully investigated the cellular localization of plasmolipin in the epithelial tissues kidney and stomach.…”

Section: Epithelial Expression Of Plasmolipinmentioning

confidence: 99%

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Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Bosse

Hasse

Pippirs

et al. 2003

Journal of Neurochemistry

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The proteolipid plasmolipin is member of the expanding group of tetraspan (4TM) myelin proteins. Initially, plasmolipin was isolated from kidney plasma membranes, but subsequent northern blot analysis revealed highest expression in the nervous system. To gain more insight into the functional roles of plasmolipin, we have generated a plasmolipin-specific polyclonal antibody. Immunohistochemical staining confirms our previous observation of glial plasmolipin expression and proves plasmolipin localization in the compact myelin of rat peripheral nerve and myelinated tracts of the CNS. Western blot analysis indicates a strong temporal correlation of plasmolipin expression and (re-) myelination in the PNS and CNS. However, following axotomy plasmolipin expression is also recovered in non-regenerating distal nerve stumps. In addition, we detected plasmolipin expression in distinct neuronal subpopulations of the CNS. The observed asymmetric distribution of plasmolipin in compact myelin, as well as in epithelial cells of kidney and stomach, indicates a polarized cellular localization. Therefore, we purified myelin from the CNS and PNS and demonstrated an enrichement of phosphorylated plasmolipin protein in detergent-insoluble lipid raft fractions, suggesting selective targeting of plasmolipin to the myelin membranes. The present data indicate that the proteolipid plasmolipin is a structural component of apical membranes of polarized cells and provides the basis for further functional analysis.

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Section: Discussionmentioning

confidence: 99%

Section: Epithelial Expression Of Plasmolipinmentioning

confidence: 99%

Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Bosse

Hasse

Pippirs

et al. 2003

Journal of Neurochemistry

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“…These proteins are plasmolipin and MAL (myelin and lymphocyte protein/VIP17/MVP17). Plasmolipin was previously identified in both compact myelin (Cochary et al, 1990) and renal tubular epithelial cells (Sapirstein et al, 1992). In renal epithelial cells, expression of plasmolipin is localized to apical surfaces.…”

Section: Discussionmentioning

confidence: 97%

Mutually exclusive apicobasolateral sorting of two oligodendroglial membrane proteins, proteolipid protein and myelin/oligodendrocyte glycoprotein, in Madin‐Darby canine kidney cells

Kroepfl

Gardinier

2001

J of Neuroscience Research

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Oligodendrocytes elaborate an extensive membrane network that ensheathes CNS axons in multilamellar wrappings. A compaction process excludes much of the cytoplasm in mature myelin membranes, giving rise to distinct lipid/protein compositions in two membrane compartments (compact myelin and membranes of the cell body and processes). Insofar as oligodendrocytes arise from neuroepithelial progenitors, it seems likely that some elements are shared for protein targeting by these two cell types. We hypothesized that certain membrane proteins targeting different oligodendroglial membrane compartments would preferentially sort to opposite domains when transfected into Madin-Darby canine kidney (MDCK) epithelial cells. Myelin/oligodendrocyte glycoprotein (MOG) is found in uncompacted membrane (cell body, processes), and it sorts exclusively to MDCK basolateral membrane. Proteolipid protein (PLP) is found in compact myelin, and it sorts exclusively to MDCK apical membrane. Myelin-associated glycoprotein (MAG) is primarily in the periaxonal inner loop of myelin; however, it fails to target preferentially within MDCK cells. This inability of MAG to sort within MDCK cells suggests a lack of required oligodendroglial-specific targeting components. In contrast, the sorting machinery in both oligodendrocytes and MDCK cells recognizes targeting signals for MOG and PLP, and we propose that these oligodendroglial membrane proteins delineate cognate basolateral and apical domains, respectively.

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“…Clathrin coated vesicles (CVs) or axolemmal enriched fractions as either a source of enzyme and;or native APPs were isolated from rat brain as previously described (26)(27)(28). CV pellets containing ca.…”

Section: Methodsmentioning

confidence: 99%

Brain cathepsin B but not metalloendopeptidases degrade rAPP⁷⁵¹ with production of amyloidogenic fragments

Marks

Berg

Sapirstein

et al. 1995

International Journal of Peptide and Protein Research

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Lysosomal cathepsin B but not L degraded rAPP751 to yield C‐terminal 19–25 kDa fragments containingβA4, reinforcing the view that acidic proteases participate in endosonial‐lysosomal processing to yield amyloidogenic fragments in situ. This mechanism is consistent with fragmentation of endogenous APPs within clathrin‐coated vesicles (CVs) by vesicular hydrolases, with the appearance of C‐terminal amyloidogenic fragments following incubation at pH 6.5. A neutral endopeptidase resembling NEP 24.11 (PS‐NEP) purified from detergent extracts of human brain degraded rAPP751; however, breakdown was not blocked robustly by metal chelators or phosphoramidon, suggesting the presence of an alternative processing enzyme. Effects of other inhibitors showed that breakdonn was mediated b) serine‐protease‐like component(s). A phosphoramidon‐insensitive metalloendopeptidase (PI‐NEP) partially purified from rat brain P2 using detergents, and resembling NEP 24.15, showed no activity towards I‐rAPP751. Peptides containing putative β‐ or γ‐secretase sites were synthesized for purposes of examining their metabolism by the brain enzymes. Those containing β‐secretase sites were hydrolysed at one or more sites by the four enzymes, but only PI‐ and PS‐NEP acted at the Met‐Asp site of Ac‐VaI‐Lys‐Met‐Asp‐Ala‐Glu‐Phe‐Arg.NH2. In the case of substrates Containing the γ‐site, these two categories of enzymes were the only ones degrading N‐Ac‐Ilc‐Ala NH2. These data imply that the brain metalloendopeptidases, while inactive towards intact precursors, may be involved in turnover of intermediates containing β‐ or 7‐sites.

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Expression of plasmolipin in the developing rat brain

Cited by 11 publications

References 22 publications

Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Mutually exclusive apicobasolateral sorting of two oligodendroglial membrane proteins, proteolipid protein and myelin/oligodendrocyte glycoprotein, in Madin‐Darby canine kidney cells

Brain cathepsin B but not metalloendopeptidases degrade rAPP⁷⁵¹ with production of amyloidogenic fragments

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Expression of plasmolipin in the developing rat brain

Cited by 11 publications

References 22 publications

Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Proteolipid plasmolipin: localization in polarized cells, regulated expression and lipid raft association in CNS and PNS myelin

Mutually exclusive apicobasolateral sorting of two oligodendroglial membrane proteins, proteolipid protein and myelin/oligodendrocyte glycoprotein, in Madin‐Darby canine kidney cells

Brain cathepsin B but not metalloendopeptidases degrade rAPP751 with production of amyloidogenic fragments

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Brain cathepsin B but not metalloendopeptidases degrade rAPP⁷⁵¹ with production of amyloidogenic fragments