Characterization of cloned cDNA representing rat myelin basic protein: Absence of expression in brain of shiverer mutant mice

Roach, Arthur; Boylan, Kevin B.; Horvath, Suzanna J.; Prusiner, Stanley B.; Hood, Leroy

doi:10.1016/0092-8674(83)90536-6

Cited by 384 publications

(217 citation statements)

References 28 publications

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“…The latter have a partial deletion in the gene encoding myelin basic protein (MBP) [22][23][24][25]. The present data establish the importance of graft-derived oligodendrocytes in the functional recovery of the injured spinal cord after NS/PC transplantation.…”

Section: Introductionmentioning

confidence: 54%

“…(C): After adding platelet-derived growth factor AA and ciliary neurotrophic factor to the culture medium, both wt-NS/PCs and shi-NS/PCs differentiated into O1 þ , CNPase þ , and PLP þ oligodendrocytes. Oligodendrocytes from shi-NS/PCs showed no MBP expression, as expected [22][23][24]. Scale bar ¼ 20 lm.…”

Section: Transplanted Shi-ns/pcs Prevented Atrophic Changes In the Inmentioning

confidence: 99%

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Significance of Remyelination by Neural Stem/Progenitor Cells Transplanted into the Injured Spinal Cord

et al. 2011

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Previous reports of functional recovery from spinal cord injury (SCI) in rodents and monkeys after the delayed transplantation of neural stem/progenitor cells (NS/PCs) have raised hopes that stem cell therapy could be used to treat SCI in humans. More research is needed, however, to understand the mechanism of functional recovery. Oligodendrocytes derived from grafted NS/PCs remyelinate spared axons in the injured spinal cord. Here, we studied the extent of this remyelination's contribution to functional recovery following contusive SCI in mice. To isolate the effect of remyelination from other possible regenerative benefits of the grafted cells, NS/PCs obtained from myelin-deficient shiverer mutant mice (shi-NS/PCs) were used in this work alongside wild-type NS/PCs (wt-NS/PCs). shi-NS/PCs behaved like wt-NS/PCs in vitro and in vivo, with the exception of their myelinating potential. shi-NS/ PC-derived oligodendrocytes did not express myelin basic protein in vitro and formed much thinner myelin sheaths in vivo compared with wt-NS/PC-derived oligodendrocytes. The transplantation of shi-NS/PCs promoted some locomotor and electrophysiological functional recovery but significantly less than that afforded by wt-NS/PCs. These findings establish the biological importance of remyelination by graft-derived cells for functional recovery after the transplantation of NS/PCs into the injured spinal cord.

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Section: Introductionmentioning

confidence: 54%

Section: Transplanted Shi-ns/pcs Prevented Atrophic Changes In the Inmentioning

confidence: 99%

Significance of Remyelination by Neural Stem/Progenitor Cells Transplanted into the Injured Spinal Cord

et al. 2011

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“…To further understand the regulation of gene expression during myelination, we determined the mRNA level for MBP, the other major myelin protein, during the course of myelination. Figure 5 shows that there is a single species of MBP mRNA of 2.1 kb in size in the rat brain detected by a MBP cDNA probe (pMBP1; gift of Roach et al) as previously described (10). This cDNA was used to follow the level of MBP mRNA in rat brains of various ages.…”

Section: Isolation and Characterization Of Plp Cdna Clonesmentioning

confidence: 99%

“…To understand the basic defect in these diseases and the regulation of MBP and PLP expression, studies have been initiated to examine these proteins at the gene level. Recently the isolation of cDNA clones for MBP have been reported (10)(11)(12). We here describe the molecular cloning of a complementary DNA (cDNA) for PLP and provide preliminary evidence that the two proteins are coordinately regulated at the mRNA level during development.…”

Section: Introductionmentioning

confidence: 99%

Study of the expression of myelin proteolipid protein (lipophilin) using a cloned complementary DNA

et al. 1985

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We have prepared a XgtlO cDNA library with the mRNA isolated from fetal calf brains which were actively myelinating. Using two oligonucleotides made according to the known amino acid sequence of myelin proteolipid protein (PLP or lipophilin), we have isolated several cDNA clones for this major intrinsic membrane protein of myelin. One of these clones, designated as pLPl, is found to contain 444 bp of coding sequence for the C-terminal half of PLP and 486 bp of 3' untranslated sequence. Using pLPl as a hybridization probe, we have studied the regulation of PLP at the mRNA level during rat brain development. Our results show that the relative amounts of mRNA for PLP and that for the major extrinsic protein of the myelin membrane, myelin basic protein, increase coordinately during the course of myelination in the brain.

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“…Although the myelin proteins appear at different times during oligodendrocyte development, the mRNAs encoding these proteins accumulate with similar temporal profiles both in the developing brain and in oligodendrocytes in culture (Z eller et al, 1985;Collarini et al, 1992;Grinspan et al, 1993;Scherer et al, 1994). Regulation of this process, including the accumulation of myelin-specific mRNAs and proteins, as well as compact myelin, can be accounted for by the transcriptional activation of the set of myelin-specific protein genes during the final stage of oligodendrocyte differentiation (Z eller et al, 1984;Milner, 1985;Z eller et al, 1985;Roach et al, 1983;. Thus a coordinated activation of myelin-specific gene expression precedes the onset of myelination by oligodendrocytes in the C NS and is critical for normal myelin formation.…”

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confidence: 99%

Evidence That the Homeodomain Protein Gtx Is Involved in the Regulation of Oligodendrocyte Myelination

et al. 1997

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We have investigated the patterns of postnatal brain expression and DNA binding of Gtx, a homeodomain transcription factor. Gtx mRNA accumulates in parallel with the RNAs encoding the major structural proteins of myelin, myelin basic protein (MBP), and proteolipid protein (PLP) during postnatal brain development; Gtx mRNA decreases in parallel with MBP and PLP mRNAs in the brains of myelin-deficient rats, which have a point mutation in the PLP gene. Gtx mRNA is expressed in differentiated, postmitotic oligodendrocytes but is not found in oligodendrocyte precursors or astrocytes. These data thus demonstrate that Gtx is expressed uniquely in differentiated oligodendrocytes in postnatal rodent brain and that its expression is regulated in parallel with the major myelin protein mRNAs, encoding MBP and PLP, under a variety of physiologically relevant circumstances.Using a Gtx fusion protein produced in bacteria, we have confirmed that Gtx is a sequence-specific DNA-binding protein, which binds DNA sequences containing a core AT-rich homeodomain binding site. Immunoprecipitation of labeled DNA fragments encoding either the MBP or PLP promoter regions with this fusion protein has identified several Gtx-binding fragments, and we have confirmed these data using an electrophoretic mobility shift assay. In this way we have identified four Gtx binding sites within the first 750 bp of the MBP promoter and four Gtx binding sites within the first 1.3 kb of the PLP promoter. In addition, inspection of the PLP promoter sequence demonstrates the presence of six additional Gtx binding sites. These data, taken together, strongly suggest that Gtx is important for the function of differentiated oligodendrocytes and may be involved in the regulation of myelin-specific gene expression.

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Characterization of cloned cDNA representing rat myelin basic protein: Absence of expression in brain of shiverer mutant mice

Cited by 384 publications

References 28 publications

Significance of Remyelination by Neural Stem/Progenitor Cells Transplanted into the Injured Spinal Cord

Significance of Remyelination by Neural Stem/Progenitor Cells Transplanted into the Injured Spinal Cord

Study of the expression of myelin proteolipid protein (lipophilin) using a cloned complementary DNA

Evidence That the Homeodomain Protein Gtx Is Involved in the Regulation of Oligodendrocyte Myelination

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