Isolation and analysis of the gene encoding peripheral myelin protein zero

Lemke, Greg; Lamar, E.; Patterson, Joshua T.

doi:10.1016/0896-6273(88)90211-5

Cited by 270 publications

(185 citation statements)

References 61 publications

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“…2A). For the myelin Po gene, the 5Ј flanking sequences Ϫ912 to ϩ45 of the rat gene, which confer specific expression in Schwann cells (6,7), were cloned in the luciferase reporter gene and transfected into F10.9 cells. IL6RIL6 induced 10 -15-fold the activity of this myelin Po promoter construct (Fig.…”

Section: Transcriptional Activation Of Myelin Po and Mbp Gene Promotementioning

confidence: 99%

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Activation of Myelin Genes during Transdifferentiation from Melanoma to Glial Cell Phenotype

Slutsky

Kamaraju

Levy

et al. 2003

Journal of Biological Chemistry

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Section: Transcriptional Activation Of Myelin Po and Mbp Gene Promotementioning

confidence: 99%

“…by forskolin) induces Po and MBP (25,27) whereas it represses Pax3 (20). Activating effects of forskolin were seen on the promoters of the genes encoding myelin proteins Po (6), MBP (28,29), and peripheral myelin protein-22 (PMP-22) (30). Hormones, such as progesterone and glucocorticosteroids, also stimulate Po and PMP-22 promoter activities (31,32).…”

mentioning

confidence: 99%

Activation of Myelin Genes during Transdifferentiation from Melanoma to Glial Cell Phenotype

Slutsky

Kamaraju

Levy

et al. 2003

Journal of Biological Chemistry

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“…These include neural cell adhesion molecule (N-CAM) ~ (Barthels et al, 1987;Cunningham et al, 1987), myelinassociated glycoprotein (MAG) (Lai et al, 1987;Salzer et al, 1987), L1 (Moos et al, 1988), Po (Lemke et al, 1988), contactin (Ranscht, 1988)-which are expressed in vertebrates-and two recently identified insect proteins, fasciclin II (Harrelson and Goodman, 1988) and amalgam (Seeger et al, 1988). With the exception of Po, they contain C2-type Ig domains, and their sequence similarity extends in some cases beyond the Ig-like region (Harrelson and Goodman, 1988).…”

mentioning

confidence: 99%

The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin.

Gennarini

Cibelli

Rougon

et al. 1989

The Journal of Cell Biology

259

166

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Abstract. Several members of the Ig superfamily are expressed on neural cells where they participate in surface interactions between cell bodies and processes. Their Ig domains are more closely related to each other than to Ig variable and constant domains and have been grouped into the C2 set. Here, we report the cloning and characterization of another member of this group, the mouse neuronal cell surface antigen F3. The F3 eDNA sequence contains an open reading frame that could encode a 1,020-amino acid protein consisting of a signal sequence, six Ig-like domains of the C2 type, a long premembrane region containing two segments that exhibit sequence similarity to fibronectin type III repeats and a moderately hydrophobic COOH-terminal sequence. The protein does not contain a typical transmembrane segment but appears to be attached to the membrane by a phosphatidylinositol anchor. Antibodies against the F3 protein recognize a prominent 135-kD protein in mouse brain. In fetal brain cultures, they stain the neuronal cell surface and, in cultures maintained in chemically defined medium, most prominently neurites and neurite bundles. The mouse f3 gene maps to band F of chromosome 15. The gene transcripts detected in the brain by F3 cDNA probes are developmentally regulated, the highest amounts being expressed between 1 and 2 wk after birth.The F3 nucleotide and deduced amino acid sequence show striking similarity to the recently published sequence of the chicken neuronal cell surface protein contactin. However, there are important differences between the two molecules. In contrast to F3, contactin has a transmembrane and a cytoplasmic domain. Whereas contactin is insoluble in nonionic detergent and is tightly associated with the cytoskeleton, about equal amounts of F3 distribute between buffer-soluble, nonionic detergent-soluble, and detergent-insoluble fractions. Among other neural cell surface proteins, F3 most resembles the neuronal cell adhesion protein L1, with 25 % amino acid identity between their extracellular domains. Based on its structural similarity with known cell adhesion proteins of nervous tissue and with L1 in particular, we propose that F3 mediates cell surface interactions during nervous system development.

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“…and an extracellular domain [17,18] . The majority of MPZ mutations are located on exon 2 or 3 which corresponds to the immunoglobulin-like extracellular domain, whereas mutations in the intracellular and transmembrane domains are less frequent [19] .…”

Section: Mpz and Di-cmtd Phenotypementioning

confidence: 99%

“…MPZ is located on chromosome 1q23.3 and is 7 kb in size [16,17] . It has six exons encoding myelin protein zero (P 0 ).…”

Section: Mpz and Di-cmtd Phenotypementioning

confidence: 99%

Intermediate Charcot-Marie-Tooth disease

Liu

Zhang

2014

Neurosci. Bull.

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Charcot-Marie-Tooth (CMT) disease is a common neurogenetic disorder and its heterogeneity is a challenge for genetic diagnostics. The genetic diagnostic procedures for a CMT patient can be explored according to the electrophysiological criteria: very slow motor nerve conduction velocity (MNCV) (<15 m/s), slow MNCV (15-25 m/s), intermediate MNCV (25-45 m/s), and normal MNCV (>45 m/s). Based on the inheritance pattern, intermediate CMT can be divided into dominant (DI-CMT) and recessive types (RI-CMT). GJB1 is currently considered to be associated with X-linked DI-CMT, and MPZ, INF2, DNM2, YARS, GNB4, NEFL, and MFN2 are associated with autosomal DI-CMT. Moreover, GDAP1, KARS, and PLEKHG5 are associated with RI-CMT. Identifi cation of these genes is not only important for patients and families but also provides new information about pathogenesis. It is hoped that this review will lead to a better understanding of intermediate CMT and provide a detailed diagnostic procedure for intermediate CMT.

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Isolation and analysis of the gene encoding peripheral myelin protein zero

Cited by 270 publications

References 61 publications

Activation of Myelin Genes during Transdifferentiation from Melanoma to Glial Cell Phenotype

Activation of Myelin Genes during Transdifferentiation from Melanoma to Glial Cell Phenotype

The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin.

Intermediate Charcot-Marie-Tooth disease

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