Electron Microscopic Immunocytochemical Localization of Myelin Proteolipid Protein and Myelin Basic Protein to Oligodendrocytes in Rat Brain During Myelination

Schwob, Valerie S.; Clark, Helen E.; Agrawal, Daya; Agrawal, Harish C.

doi:10.1111/j.1471-4159.1985.tb04024.x

Cited by 66 publications

(36 citation statements)

References 42 publications

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“…At 10 days staining of myelin sheaths was observed. The temporal appear ance of immunocytochemical staining in our study, perinuclear and then in myelin, agrees with the studies of Nussbaum and Roussel [35] and Schwob et al [36], At 10 days, un like previous ages examined, the protein was found everywhere that the mRNA is found. Both protein and mRNA are observed throughout the subcortical white matter but are excluded from the cingulum at this age.…”

Section: Discussionsupporting

confidence: 82%

“…In situ hybridization studies reveal a strong signal in many cells at 7 days, although only a few cells with perinuclear staining are observed by immunocytochemistry. Previous studies have demonstrated that the PLP protein is expressed in the Golgi apparatus prior to its expression in myelin [35,36], The perinuclear staining we ob served is most likely staining of the proteins in the Golgi. While the in situ studies may be more sensitive than the immunocytochemical studies [our Northern blots are more sen sitive than our Western blots (data not shown)], the perinuclear staining at this stage indicates that this is the site of greatest protein within these cells.…”

Section: Discussionmentioning

confidence: 97%

“…Thus, at that age (7 days), little or no protein has accumulated in the cell surface membrane of oligodendro cytes. Schwob et al [36] observed MBP, but not PLP, in oligodendrocyte processes that first envelop axons. It was not until com paction had begun that PLP was observed in myelin.…”

Section: Discussionmentioning

confidence: 99%

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Developmental Expression of Proteolipid Protein and DM20 mRNAs and Proteins in the Rat Brain

Levine

Wong

Macklin³

1990

Dev Neurosci

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Proteolipid protein (PLP) and DM20, two abundant proteins of myelin, are produced from alternatively spliced mRNAs from the primary PLP gene transcript. Recent studies on the mouse, bovine and human central nervous systems have found that DM20 protein is expressed prior to PLP during development. As development proceeds, however, PLP becomes the predominant protein. This implies that there must be some form of regulation controlling the ratio of these proteins during development. If this regulation occurs during transcription or splicing, the PLP/DM20 mRNA ratio should mimic the PLP/DM20 protein ratio during development. In order to study these closely related mRNAs, we developed a method that used oligonucleotide probes to specifically identify PLP or DM20 mRNA. In this study, we established that (1) as with other species studied, the DM20 protein is present at higher or equivalent levels to PLP during early rat brain development, and (2) PLP and DM20 mRNAs have essentially identical developmental profiles in the rat, although the DM20 mRNA is expressed at lower levels than PLP mRNA. Since the PLP/DM20 protein ratio in young rats does not reflect the PLP/DM20 mRNA ratio, the mechanism of regulation responsible for altering the PLP/DM20 protein ratio during development must occur after transcription and splicing. Possible posttranscriptional mechanisms controlling the ratio of these proteins during development are discussed.

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 97%

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Developmental Expression of Proteolipid Protein and DM20 mRNAs and Proteins in the Rat Brain

Levine

Wong

Macklin³

1990

Dev Neurosci

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“…Hartmann et al [1982] reported that MBP was inte grated in myelin sheaths before PLP. and Schwob et al [ 1985], using an immuno-electron microscopic approach, demonstrated that the first oligodendroglial ensheathments were MBP' and PLP . Immunohistolocalization of GalC on tis sue sections is not very easy to perform.…”

Section: Discussionmentioning

confidence: 99%

Oligodendroglial Expression and Deposition of Four Major Myelin Constituents in the Myelin Sheath during Development

et al. 1986

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We have studied the sequence of expression in the oligodendrocyte of four myelin constituents: galactosylceramide (GalC), myelin basic protein (MBP), proteolipid protein (PLP) and Wolfgram protein (W₁). These investigations were performed on freshly dissociated cell preparations from mouse olfactory bulb and cerebellum before and during early myelinogenesis. Our data showed that the first myelin antigen to be detected in the oligodendrocyte was GalC, followed 24 h later by W₁ and after a 5-day time lag (relative to GalC) by MBP. Expression of PLP occurred shortly after that of MBP. This sequence of events was identical in the cerebellum and in the olfactory bulb, but it commenced earlier in the cerebellum (E18) than in the olfactory bulb (P2). Deposition of these components in the nascent myelin sheaths was studied on tissue sections. These histological preparations showed that the temporal order of deposition of the myelin constituents did not correlate with their order of expression in the oligodendrocyte. As judged both by the intensity of the labeling and the number of positive fibers, W₁ and MBP were the first antigens to be deposited, followed by PLP and finally by GalC. Furthermore, this deposition process was initiated immediately after completion of expression of these antigens in the oligodendrocyte.

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“…MBP and PLP stabilize apposed myelin membrane surfaces in compact myelin, and their transport routes are segregated. Thus, following its biosynthesis at the rough endoplasmic reticulum and processing through the Golgi apparatus (9,10), the transmembrane protein PLP is transported via vesicles to the myelin membrane (11,12). In marked contrast, MBP, a peripheral membrane protein facing the cytoplasm, is synthesized at and associates with the myelin membrane on site, involving myelin membrane-directed transport of its mRNA rather than the native protein (13,14).…”

mentioning

confidence: 99%

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

Baron

Ozgen

Klunder

et al. 2015

Molecular and Cellular Biology

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bMyelin membranes are sheet-like extensions of oligodendrocytes that can be considered membrane domains distinct from the cell's plasma membrane. Consistent with the polarized nature of oligodendrocytes, we demonstrate that transcytotic transport of the major myelin-resident protein proteolipid protein (PLP) is a key element in the mechanism of myelin assembly. Upon biosynthesis, PLP traffics to myelin membranes via syntaxin 3-mediated docking at the apical-surface-like cell body plasma membrane, which is followed by subsequent internalization and transport to the basolateral-surface-like myelin sheet. Pulse-chase experiments, in conjunction with surface biotinylation and organelle fractionation, reveal that following biosynthesis, PLP is transported to the cell body surface in Triton X-100 (TX-100)-resistant microdomains. At the plasma membrane, PLP transiently resides within these microdomains and its lateral dissipation is followed by segregation into 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate (CHAPS)-resistant domains, internalization, and subsequent transport toward the myelin membrane. Sulfatide triggers PLP's reallocation from TX-100-into CHAPS-resistant membrane domains, while inhibition of sulfatide biosynthesis inhibits transcytotic PLP transport. Taking these findings together, we propose a model in which PLP transport to the myelin membrane proceeds via a transcytotic mechanism mediated by sulfatide and characterized by a conformational alteration and dynamic, i.e., transient, partitioning of PLP into distinct membrane microdomains involved in biosynthetic and transcytotic transport.

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Electron Microscopic Immunocytochemical Localization of Myelin Proteolipid Protein and Myelin Basic Protein to Oligodendrocytes in Rat Brain During Myelination

Cited by 66 publications

References 42 publications

Developmental Expression of Proteolipid Protein and DM20 mRNAs and Proteins in the Rat Brain

Developmental Expression of Proteolipid Protein and DM20 mRNAs and Proteins in the Rat Brain

Oligodendroglial Expression and Deposition of Four Major Myelin Constituents in the Myelin Sheath during Development

The Major Myelin-Resident Protein PLP Is Transported to Myelin Membranes via a Transcytotic Mechanism: Involvement of Sulfatide

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