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

Naismith, Angela; Hoffman-Chudzik, E.; Tsui, Lap Chee; Riordan, John R.

doi:10.1093/nar/13.20.7413

Cited by 64 publications

(37 citation statements)

References 25 publications

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“…PLP is remarkably well conserved among mouse (this report), rat (1,16), cow (2), and human (C.P., L.D.H., and R.A.L., unpublished work) at the amino acid and nucleotide level. The protein encoded by the mouse PLP cDNA (Fig.…”

Section: Resultsmentioning

confidence: 69%

“…The protein encoded by the mouse PLP cDNA (Fig. 1) is identical to the rat (16) and human (C.P., L.D.H., and R.A.L., unpublished work) PLP and displays only two conservative amino acid differences from the bovine sequence (2 (18) or dideoxy chain termination (19) methods. The most 5' 300 bases of phage A PLP2, which extends from position one to the secondary polyadenylylation site at 2288, were also sequenced.…”

Section: Resultsmentioning

confidence: 92%

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Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse.

Hudson¹,

Berndt²,

Puckett³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

170

113

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ABSTRACTcDNA clones encoding proteolipid protein (PLP) were isolated from a mouse brain library and sequenced. We describe two transcripts arising from the PLP locus by alternative splicing: the major one encodes the 277-amino acid PLP protein and the minor one corresponds to the DM-20 protein, a PLP-like protein of 20,000 Mr that shares both amino and carboxyl regions with PLP. These two transcripts lack -70 bases in PLP mRNA from the dysmyelinating jimpy mutant. The deletion spans amino acids 208-232; however, this region is present in thejimpy PLP-encoding gene. We propose that the jimpy mutant suffers a point mutation or the deletion of a few bases in the PLP gene that alters the normal splicing pattern and generates partially deleted PLP transcripts. RESULTS AND DISCUSSIONConservation of PLP Sequence. PLP is remarkably well conserved among mouse (this report), rat (1, 16), cow (2), and human (C.P., L.D.H., and R.A.L., unpublished work) at the amino acid and nucleotide level. The protein encoded by the mouse PLP cDNA (Fig. 1) is identical to the rat (16) and human (C.P., L.D.H., and R.A.L., unpublished work) PLP and displays only two conservative amino acid differences from the bovine sequence (2). The striking degree of conserAbbreviations: PLP, proteolipid protein; MBP, myelin basic protein.

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Section: Resultsmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 92%

Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse.

Hudson¹,

Berndt²,

Puckett³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

170

113

View full text Add to dashboard Cite

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“…The amino acid and nucleotide sequences of cow, rat, mouse, and human PLP are closely homologous (32)(33)(34)(35)(36)(37)(38)(39)(40), and mutations within the PLP gene cause severe dysmyelination (8). Thus, PLP seems to play a significant role in central nervous system myelination, presumably by promoting the apposition of extracellular surfaces of the myelin lamellae.…”

Section: Discussionmentioning

confidence: 99%

Myelin Proteolipid Protein (PLP), but Not DM-20, Is an Inositol Hexakisphosphate-binding Protein

Yamaguchi

Ikenaka

Niinobe

et al. 1996

Journal of Biological Chemistry

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“…1). Its primary structure has been established by protein sequencing (2)(3)(4) and more recently from the cloning of PLP cDNAs from several species (5)(6)(7)(8)(9)(10). A mutation in the mouse PLP gene is the primary genetic defect of the dysmyelinating mutant mouse jimpy (8)(9)(10)(11)(12), which demonstrates the critical role of PLP in CNS myelin assembly.…”

Section: Myelination In the Mammalian Central Nervous System (Cns)mentioning

confidence: 99%

Splice site selection in the proteolipid protein (PLP) gene transcript and primary structure of the DM-20 protein of central nervous system myelin.

Nave¹,

Lai²,

Bloom³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

291

215

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Proteolipid protein (PLP) is the major myelin membrane protein of the central nervous system. We have isolated a copy of an alternatively spliced PLP gene transcript from a mouse brain cDNA library that was screened for PLP-related sequences. The encoded 241-amino acid protein differs from PLP by an internal deletion of 35-amino acid residues (116-150) from the major hydrophilic domain. This PLP variant is identical with the DM-20 protein of myelin, previously described as a brain-specific myelin component and known to be related to PLP. We determined the corresponding nucleotide sequence of the rat PLP gene and found that DM-20 mRNA results when a second 5' splice site, located 105 nucleotides within the third exon of the primary PLP transcript, is utilized in precursor mRNA (pre-mRNA) splicing. This demonstrates that alternative 5' splice site selection can determine the protein product of a cellular gene. DM-20 mRNA is expressed in rat brain with approximately 50% abundance relative to PLP mRNA and appears to be developmentally coregulated. Myelination in the mammalian central nervous system (CNS)is the specialized function of differentiated oligodendrocytes and involves the coordinated expression of myelin-specific gene products. Proteolipid protein (PLP) is the most abundant myelin protein of the CNS and is a highly hydrophobic integral membrane protein (reviewed in ref. 1). Its primary structure has been established by protein sequencing (2-4) and more recently from the cloning of PLP cDNAs from several species (5-10). A mutation in the mouse PLP gene is the primary genetic defect of the dysmyelinating mutant mouse jimpy (8-12), which demonstrates the critical role of PLP in CNS myelin assembly.Another CNS specific myelin protein of lower abundance has been termed "intermediate protein" or DM-20 (13), which reflects its apparent molecular mass. Depending on the proteolipid extraction method (14), DM-20 copurifies with PLP, but the two proteins can easily be separated by NaDodSO4 gel electrophoresis. PLP and the DM-20 protein are related by amino-and carboxyl-terminal amino acid sequence homology and immunological crossreactivity (1). The exact structure of DM-20 and its relationship to PLP had been controversial, but recent evidence has suggested that DM-20 differs from PLP by an internal deletion of residues 100-140 (plus or minus a few amino acids) (15, 16). To determine the exact relationship between PLP and DM-20 and to test the possibility that the DM-20 protein is a result of alternative PLP precursor mRNA (pre-mRNA) splicing, we screened a mouse brain cDNA library for PLP-related sequences. A full-length copy from such an alternatively spliced PLP mRNA was identified and shown to encode a variant PLP form. All evidence suggests that this variant proteolipid is the DM-20 protein of myelin. To analyze the mechanism of alternative splicing, we determined the sequence of the corresponding part of the rat PLP gene § and found that RNA processing involves alternative 5' splice site selection in th...

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

Cited by 64 publications

References 25 publications

Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse.

Aberrant splicing of proteolipid protein mRNA in the dysmyelinating jimpy mutant mouse.

Myelin Proteolipid Protein (PLP), but Not DM-20, Is an Inositol Hexakisphosphate-binding Protein

Splice site selection in the proteolipid protein (PLP) gene transcript and primary structure of the DM-20 protein of central nervous system myelin.

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