Structure and Expression of the Mouse Myelin Proteolipid Protein Gene<sup>a</sup>

Macklin, Wendy B.; Gardinier, Minnetta V.; Obeso, Zaida O.

doi:10.1111/j.1749-6632.1990.tb42392.x

Cited by 45 publications

(61 citation statements)

References 45 publications

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“…A reduction in PLP/DM20 messages was observed as the animal aged ( Figure 2D), which is in accordance with previous reports (Macklin et al 1987;Ikenaka et al 1992).…”

Section: In Situ Hybridizationsupporting

confidence: 82%

“…MOG RT-PCR was performed using the sense and antisense primers corresponding to the sequences 60-80 and 767-789, respectively, from the mouse MOG cDNA sequence (Ballenthin and Gardinier 1996). For the PLP-specific isoform, the sense primer corresponds to nucleotides 524-543 and the antisense primer to 612-635 nucleotides from exon 3 of the nucleotide sequence of the mouse proteolipid protein gene (Macklin et al 1987).…”

Section: Resultsmentioning

confidence: 99%

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Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Jalabi

Cerghet

Skoff

et al. 2003

J Histochem Cytochem.

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S U M M A R Y Oligodendrocytes, the myelin-forming cells in the central nervous system, were visualized with excellent resolution at the light microscopic level using in situ hybridization (ISH). Digoxigenin (Dig)-tagged probes were synthesized and efficiently labeled by PCR. Specific probes to myelin genes were made by RT from brain total RNAs, followed by PCR with designed specific primers in the presence of Dig-11-dUTP. Probes specific to proteolipid protein (PLP), PLP and its isoform DM20 (PLP/DM20), and myelin oligodendrocyte glycoprotein (MOG) were synthesized and labeled. ISH was then applied on vibratomed tissue sections from mouse brains. Despite a low expression of MOG-specific and PLP-specific mRNAs in adult and newborn mouse brains, an oligodendrocyte population was detected. The specificity of Dig-labeled probes was confirmed with the double labeling of carbonic anhydrase II (CA II) and glial fibrillary acidic protein (GFAP) immunocytochemistry and ISH. This versatile and easy method for synthesis and labeling of specific probes to oligodendrocytes can be also applied to detect many other mRNAs in the nervous system and in other tissues.

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“…A reduction in PLP/DM20 messages was observed as the animal aged ( Figure 2D), which is in accordance with previous reports (Macklin et al 1987;Ikenaka et al 1992).…”

Section: In Situ Hybridizationsupporting

confidence: 82%

Section: Resultsmentioning

confidence: 99%

Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Jalabi

Cerghet

Skoff

et al. 2003

J Histochem Cytochem.

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“…The two antisense constructs targeted the region of the initiation codon: the 23-mer antisense ODN (5Ј-AGC CCA TGT CTT TGG CAC TCT GA -3Ј) spanned nucleotides (nts) Ϫ163ϩ7 and the 27-mer (5Ј-GCA CAA CAC TCT AAC AAG CCC ATG TCT -3Ј) spanned nts Ϫ43ϩ23 (Macklin et al, 1987). A search of GenBank and EMBL databases showed identical bases for only the targeted PLP sequence.…”

Section: Methodsmentioning

confidence: 99%

Proteolipid Protein Regulates the Survival and Differentiation of Oligodendrocytes

Yang

Skoff

1997

J. Neurosci.

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Proteolipid protein (PLP) has been postulated to play a critical role in the early differentiation of oligodendrocytes (OLs) in addition to its known role as a structural component of myelin.To identify this early function, we blocked the synthesis of PLP in glial cultures with antisense oligodeoxynucleotides that targeted the PLP initiation codon. Primary glial cultures were incubated with phosphorothioate-protected oligodeoxynucleotides (S-ODNs) for up to 11 d. PLP in OLs was reduced Ͼ90%. OLs treated with antisense S-ODNs appeared strikingly healthy as judged by (1) immunocytochemical staining for myelin glycolipids and myelin basic protein, (2) their prolonged survival compared with untreated cultures, and (3) their ability to reestablish membrane sheets after removal of the S-ODNs.Our studies show that PLP is required for elaboration and stability of the myelin membrane sheets made by most OLs, but it is not necessary for the network of processes established by OLs. More importantly, the number of OLs in the antisensetreated cultures was nearly sevenfold greater after a 10 -11 d incubation with S-ODNs than in control cultures. The number of proliferating OL progenitors was not increased in the antisensetreated cultures, indicating that the increase in the number of OLs was attributable to prolonged OL survival. The tissue culture studies reveal that the absence of PLP/DM20 has the positive effect of promoting OL survival but the negative effect of preventing their full differentiation. This finding clarifies many of the paradoxical findings seen in the PLP mutants, the PLP overexpressers, and the PLP Ϫ animals.

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“…Proteolipid protein (PLP) and a second myelin protein, DM20, account for approxi mately 50% of the total myelin protein [1][2][3][4]. DM20 protein is identical to PLP except for the absence of an internal peptide of 35 amino acids, residues 116-150 [5][6][7][8], PLP and DM20 proteins are produced from alter natively spliced mRNAs that are generated from the primary PLP gene transcript [7][8][9], The effect(s) of the presence or absence of the PLP-specific peptide on the conforma tion of the protein has not been established, although some interesting leads do exist. The PLP-specific peptide accounts for the ma jority of one of three hydrophilic regions in an otherwise hydrophobic molecule [10], and it has been proposed to extend out of the lipid bilayer and interact with molecules in the apposing bilayer [10][11][12], Interactions of this kind could be, in part, responsible for the compaction of the lipid bilayer that oc curs in the mature myelin membrane.…”

Section: Introductionmentioning

confidence: 99%

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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Structure and Expression of the Mouse Myelin Proteolipid Protein Gene^a

Cited by 45 publications

References 45 publications

Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Proteolipid Protein Regulates the Survival and Differentiation of Oligodendrocytes

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

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Structure and Expression of the Mouse Myelin Proteolipid Protein Genea

Cited by 45 publications

References 45 publications

Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Detection of Oligodendrocytes in Tissue Sections Using PCR Synthesis of Digoxigenin-labeled Probes

Proteolipid Protein Regulates the Survival and Differentiation of Oligodendrocytes

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

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Product

Resources

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Structure and Expression of the Mouse Myelin Proteolipid Protein Gene^a