Chromosomal Mapping of the Human M6 Genes

Olinsky, Shari; Loop, B.T.; DeKosky, Allison; Ripepi, Benedetta; Weng, Weili; Cummins, James; Wenger, Sharon L.; Yan, Yimin; Lagenaur, Carl F.; Narayanan, Vinodh

doi:10.1006/geno.1996.0231

Cited by 24 publications

(19 citation statements)

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“…The 35 PLP-specific amino acids absent from the DM20 isoform are shown in green. The human DM20 amino acid sequence was compared with those of the DM20 of trout 14 and chicken, 15 the M6a, M6b proteins of humans 16 and mice 17 and the squalus DMα, DM and DMγ proteins. 18 Dark blue circles indicate highly conserved amino acids (90 to 100% identity), sky blue circles indicate partially conserved amino acids (60 to 89% identity) and white circles, non-conserved amino acids ( < 60% identity).…”

Section: Discussionmentioning

confidence: 99%

“…We compared the human DM20 sequence with sequences of other homologous DM proteins, including the DM20 of trout 14 and chicken 15 the M6a, M6b proteins of humans 16 and mice 17 and the DMα, DM and DMγ proteins of Squalus. 18 Amino acids 90 to 100% identical were considered to be highly conserved, those 60-89% identical, partially conserved and those less than 60% identical, not conserved.…”

Section: Amino-acid Sequence Comparison For Dm Proteinsmentioning

confidence: 99%

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Genotype–phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations

et al. 2000

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Pelizaeus-Merzbacher disease (PMD) and spastic paraplegia type 2 (SPG2) are X-linked developmental defects of myelin formation affecting the central nervous system (CNS). They differ clinically in the onset and severity of the motor disability but both are allelic to the proteolipid protein gene (PLP), which encodes the principal protein components of CNS myelin, PLP and its spliced isoform, DM20. We investigated 52 PMD and 28 SPG families without large PLP duplications or deletions by genomic PCR amplification and sequencing of the PLP gene. We identified 29 and 4 abnormalities respectively. Patients with PLP mutations presented a large range of disease severity, with a continuum between severe forms of PMD, without motor development, to pure forms of SPG. Clinical severity was found to be correlated with the nature of the mutation, suggesting a distinct strategy for detection of PLP point mutations between severe PMD, mild PMD and SPG. Single amino-acid changes in highly conserved regions of the DM20 protein caused the most severe forms of PMD. Substitutions of less conserved amino acids, truncations, absence of the protein and PLP-specific mutations caused the milder forms of PMD and SPG. Therefore, the interactions and stability of the mutated proteins has a major effect on the severity of PLP-related diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Amino-acid Sequence Comparison For Dm Proteinsmentioning

confidence: 99%

Genotype–phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations

et al. 2000

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“…It appears to play a role in heparin-binding growth factor signaling and may be involved in neural development (52). A role in neuronal development has been suggested for Glycoprotein M6B as well (53); however, no exact biochemical function has been described for the protein. This is also the case for CD133, and our identification of these proteins as hESC-specific markers may suggest new biological roles.…”

Section: Silac Labeling and Membrane Proteome Of Human Es Cellsmentioning

confidence: 99%

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) and Quantitative Comparison of the Membrane Proteomes of Self-renewing and Differentiating Human Embryonic Stem Cells

Prokhorova

Rigbolt

Johansen

et al. 2009

Molecular & Cellular Proteomics

103

117

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Stable isotope labeling by amino acids in cell culture (SILAC) is a powerful quantitative proteomics platform for comprehensive characterization of complex biological systems. However, the potential of SILAC-based approaches has not been fully utilized in human embryonic stem cell (hESC) research mainly because of the complex nature of hESC culture conditions. Here we describe complete SILAC labeling of hESCs with fully preserved pluripotency, self-renewal capabilities, and overall proteome status that was quantitatively analyzed to a depth of 1556 proteins and 527 phosphorylation events. SILAC-labeled hESCs appear to be perfectly suitable for functional studies, and we exploited a SILAC-based proteomics strategy for discovery of hESC-specific surface markers. We determined and quantitatively compared the membrane proteomes of the self-renewing versus differentiating cells of two distinct human embryonic stem cell lines. Of the 811 identified membrane proteins, six displayed significantly higher expression levels in the undifferentiated state compared with differentiating cells. This group includes the established marker CD133/Prominin-1 as well as novel candidates for hESC surface markers: Glypican-4, Neuroligin-4, ErbB2, receptor-type tyrosine-protein phosphatase (PTPRZ), and Glycoprotein M6B. Our study also revealed 17 potential markers of hESC differentiation as their corresponding protein expression levels displayed a dramatic increase in differentiated embryonic stem cell populations. Molecular & Cellular Proteomics 8:959 -970, 2009. Human embryonic stem cells (hESCs)1 are stem cells derived from the blastocyst inner cell mass. They are pluripotent; thus they are able to differentiate into any human cell type. The self-renewal capacity and pluripotency make hESCs an ideal system to study the processes of cell development and differentiation. Moreover hESC research is highly relevant for regenerative medicine, which aims at replacing or restoring tissue damaged by disease or injury through transplantation of functional hESCs (1, 2). However, factors responsible for maintaining the undifferentiated and pluripotent nature of hESCs are still largely unknown. Before hESCs can be used for transplantation into the human body, reliable and reproducible protocols for differentiating them into specific cell types are needed. To create such protocols we need to develop a thorough understanding of the mechanisms maintaining the undifferentiated pluripotent nature of hESCs and those guiding their differentiation into specific lineages.A number of factors involved in the maintenance of pluripotency have been described over the last few years (3). It has also been demonstrated that overexpression of some of these factors in somatic cells is sufficient to turn them into pluripotent stem cells very similar to hESCs (4 -8). However, it is apparent that the processes occurring during such transformation are extremely complex. A large number of factors and pathways are involved in maintaining the pluripotent state and regulat...

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“…Similar to PTPRR, GPM6A is also a neuronal protein. GPM6A is a cell surface glycoprotein expressed on neurons in the murine CNS that plays a significant role in neural cell adhesion and some aspects of neurite growth (51). The physiological link between CIITA and these neuronal proteins demands further study.…”

Section: Functions Of Genes Repressed By Ciitamentioning

confidence: 99%

Modulation of Gene Expression by the MHC Class II Transactivator

Nagarajan

Bushey

Boss

2002

The Journal of Immunology

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The class II transactivator (CIITA) is a master regulator of MHC class II expression. CIITA also modulates the expression of MHC class I genes, suggesting that it may have a more global role in gene expression. To determine whether CIITA regulates genes other than the MHC class II and I family, DNA microarray analysis was used to compare the expression profiles of the CIITA expressing B cell line Raji and its CIITA-negative counterpart RJ2.2.5. The comparison identified a wide variety of genes whose expression was modulated by CIITA. Real time RT-PCR from Raji, RJ2.2.5, an RJ2.2.5 cell line complemented with CIITA, was performed to confirm the results and to further identify CIITA-regulated genes. CIITA-regulated genes were found to have diverse functions, which could impact Ag processing, signaling, and proliferation. Of note was the identification of a set of genes localized to chromosome 1p34-35. The global modulation of genes in a local region suggests that this region may share some regulatory control with the MHC.

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Chromosomal Mapping of the Human M6 Genes

Cited by 24 publications

References 0 publications

Genotype–phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations

Genotype–phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations

Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) and Quantitative Comparison of the Membrane Proteomes of Self-renewing and Differentiating Human Embryonic Stem Cells

Modulation of Gene Expression by the MHC Class II Transactivator

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