Minnetta V. Gardinier

ORCID: 0000-0003-1211-3662
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About
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Research Areas
  • Neurogenesis and neuroplasticity mechanisms
  • Glycosylation and Glycoproteins Research
  • RNA Research and Splicing
  • RNA Interference and Gene Delivery
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Monoclonal and Polyclonal Antibodies Research
  • Axon Guidance and Neuronal Signaling
  • Immunotherapy and Immune Responses
  • interferon and immune responses
  • T-cell and Retrovirus Studies
  • Lipid Membrane Structure and Behavior
  • Peroxisome Proliferator-Activated Receptors
  • T-cell and B-cell Immunology
  • Immune Cell Function and Interaction
  • Systemic Lupus Erythematosus Research
  • Macrophage Migration Inhibitory Factor
  • Nerve injury and regeneration
  • Mesenchymal stem cell research
  • RNA regulation and disease
  • Cancer Research and Treatments
  • Caveolin-1 and cellular processes
  • RNA modifications and cancer
  • Chromosomal and Genetic Variations
  • Genomics and Chromatin Dynamics
  • Cell Adhesion Molecules Research

University of Iowa
2001-2006

Northwestern University
1995-1999

Guy's Hospital
1994

University Hospital of Lausanne
1990-1993

UCLA Medical Center
1987-1991

Ronald Reagan UCLA Medical Center
1990-1991

University Medical Center New Orleans
1984-1987

Louisiana State University
1984-1987

Abstract A recombinant protein corresponding to the Ig-like domain of myelin oligodendrocyte glycoprotein (MOG) and synthetic 15-mer peptides whole MOG molecule with eight amino acid overlaps were screened for their ability induce experimental allergic encephalomyelitis (EAE) in Biozzi AB/H (H-2dq1) SJL (H-2S) mice. Clinical histologic evidence EAE developed after sensitization both In mice at least three epitopes within residues 1-22, 43-57, 134-148 induced clinical EAE, whereas only...

10.4049/jimmunol.153.10.4349 article EN The Journal of Immunology 1994-11-15

Abstract Myelin/oligodendrocyte glycoprotein (MOG) is a primary target autoantigen in experimental autoimmune encephalomyelitis, widely used animal model for demyelinating diseases such as multiple sclerosis. We have isolated several rat MOG cDNAs and confirmed their identity by comparision with N‐terminal peptide sequence. As expected, mRNA expression CNS‐specific peaks during active myelination. Our studies show that full length ≈︁ 1.6 kb encodes signal of 27 amino acids, followed 218...

10.1002/jnr.490330123 article EN Journal of Neuroscience Research 1992-09-01

Abstract Astrocytes may serve as effectual APCs for T cell-mediated immune responses to myelin components during multiple sclerosis and experimental autoimmune encephalomyelitis (EAE). Although astrocytes have been reported not constitutively express MHC class II molecules, expression is up-regulated active EAE by in vitro incubation with IFN-gamma. Previous studies that cytokine-activated are able activate Ag-specific previously activated cells, but naive alloreactive cells. In the current...

10.4049/jimmunol.158.2.614 article EN The Journal of Immunology 1997-01-15

This study addressed the possibility that proto-myb (also called c-myb), cellular homolog of a retroviral transforming gene, plays role in hemopoiesis, particularly during maturation T cells. By gel blot hybridization, we confirmed previous reports transcripts are found at much higher levels thymic lymphocytes and cells erythroid lineage than other tissue sources. Using dot hybridizations, demonstrated further similar expression taken from young mice with active thymuses old whose have...

10.1128/mcb.4.7.1206 article EN Molecular and Cellular Biology 1984-07-01

Abstract The gene for the mouse myelin proteolipid protein has been isolated and seven exons have sequenced. Since sequence of a rat cDNA partial human determined, it was possible to demonstrate very high degree conservation protelipid among species. While there are some nucleotide changes, coding region encodes that is totally conserved relative both prteolipid proteins. regulatory noncoding regions also highly conserved. upstream 5′‐noncoding 92% homologous comparable gene, 3′‐noncoding...

10.1002/jnr.490180302 article EN Journal of Neuroscience Research 1987-01-01

We investigated the onset of expression myelin/oligodendrocyte glycoprotein (MOG) mRNA and protein in developing mouse central nervous system. In situ hybridization on brain sections at different stages embryonic postnatal development showed that MOG transcripts were first detected birth medulla oblongata. During week after birth, cells expressing located ventral longitudinal funiculus. second week, pattern extended rostrally to mid-forebrain regions reached completion by beginning third...

10.1002/(sici)1098-1136(199609)18:1<39::aid-glia4>3.0.co;2-z article EN Glia 1996-09-01

The myelin proteolipid protein gene was characterized in jimpy mice to identify the specific mutation that produces dysmyelination, oligodendrocyte cell death, and death of animal by 30 days age. Exon 5 flanking intron segments were isolated from genomic clones sequenced. A single nucleotide difference noted between normal genes: conversion an AG/GT a GG/GT splice acceptor signal preceding exon 5, which apparently destroys signal. Thus, mouse is skipped during processing mRNA, producing...

10.1016/0014-5793(87)80331-9 article EN FEBS Letters 1987-11-02

Abstract: The myelin/oligodendrocyte glycoprotein (MOG) is found exclusively in the CNS, where it localized on surface of myelin and oligodendrocyte cytoplasmic membranes. monoclonal antibody 8‐18C5 identifies MOG. Several studies have shown that anti‐MOG antibodies can induce demyelination, thus inferring an important role stability. In this study, we demonstrate MOG consists two polypeptides, with molecular masses 26 28 kDa. This doublet becomes a single 25‐kDa band after deglycosylation...

10.1111/j.1471-4159.1992.tb10040.x article EN Journal of Neurochemistry 1992-05-01

A clone specific for the rat myelin proteolipid protein (PLP) was isolated from a cDNA library made in pUC18 17-day-old brain stem mRNA. This corresponded to carboxyl-terminal third of PLP-coding region. The used identify PLP-specific mRNAs mouse and establish time course PLP mRNA expression during development. Three were seen, approximately 1,500, 2,400, 3,200 bases length, which largest most abundant. During development, maximal period 14 25 days age, this similar that basic expression....

10.1128/mcb.6.11.3755-3762.1986 article EN Molecular and Cellular Biology 1986-11-01

A clone specific for the rat myelin proteolipid protein (PLP) was isolated from a cDNA library made in pUC18 17-day-old brain stem mRNA. This corresponded to carboxyl-terminal third of PLP-coding region. The used identify PLP-specific mRNAs mouse and establish time course PLP mRNA expression during development. Three were seen, approximately 1,500, 2,400, 3,200 bases length, which largest most abundant. During development, maximal period 14 25 days age, this similar that basic expression....

10.1128/mcb.6.11.3755 article EN Molecular and Cellular Biology 1986-11-01

Abstract: Myelin/oligodendrocyte glycoprotein (MOG) is a CNS‐specific integral membrane protein that an atypical member of the immunoglobulin (Ig) superfamily with two potential transmembrane domains based upon hydropathy analysis. With only one other exception, all Ig family members possess single or no spanning region. In order to analyze MOG topology, we prepared stably transfected cells express mouse and used three domain‐specific antisera ascertain localization these hydrophilic...

10.1046/j.1471-4159.1996.67052219.x article EN Journal of Neurochemistry 1996-11-01

Abstract: The mouse myelin proteolipid protein (PLP) gene has been studied in normal and jimpy msd mice. Potential upstream regulatory regions of the have cloned mapped, but when these were mice by Southern blots, no alterations observed, relative to gene. To assess whether low ratio PLP DM20 proteins this mutant reflected an altered PLP/DM20 mRNAs, S1 nuclease analyses undertaken, which demonstrated that at all ages both mice, mRNA was elevated above mRNA. When exon 3 (the site alternative...

10.1111/j.1471-4159.1991.tb02576.x article EN Journal of Neurochemistry 1991-01-01

This study addressed the possibility that proto-myb (also called c-myb), cellular homolog of a retroviral transforming gene, plays role in hemopoiesis, particularly during maturation T cells. By gel blot hybridization, we confirmed previous reports transcripts are found at much higher levels thymic lymphocytes and cells erythroid lineage than other tissue sources. Using dot hybridizations, demonstrated further similar expression taken from young mice with active thymuses old whose have...

10.1128/mcb.4.7.1206-1212.1984 article EN Molecular and Cellular Biology 1984-07-01

Myelin/oligodendrocyte glycoprotein (MOG) is an integral membrane protein expressed on the oligodendrocyte cell surface and outermost of myelin sheaths. Due to this localization, MOG a primary target antigen involved in immune-mediated demyelination. We previously reported that unique member immunoglobulin (Ig) superfamily it possesses two large hydrophobic domains. highly conserved between deduced peptide sequences rodent human (≈89% identity). have completed investigation alternative...

10.1002/(sici)1097-4547(19961015)46:2<271::aid-jnr16>3.0.co;2-5 article EN Journal of Neuroscience Research 1996-10-15

Oligodendrocytes possess two distinct membrane compartments – uncompacted plasma (cell body, processes) and compact myelin. Specific targeting mechanisms must exist to establish maintain these domains. Polarized epithelial cells have the best characterized system for components apical basolateral compartments. Since oligodendrocytes arise from neuroepithelial cells, we investigated whether they might utilize paradigms similar polarized cells. Myelin/oligodendrocyte glycoprotein (MOG) is a...

10.1046/j.1471-4159.2001.00343.x article EN Journal of Neurochemistry 2001-06-01

Abstract Oligodendrocytes elaborate an extensive membrane network that ensheathes CNS axons in multilamellar wrappings. A compaction process excludes much of the cytoplasm mature myelin membranes, giving rise to distinct lipid/protein compositions two compartments (compact and membranes cell body processes). Insofar as oligodendrocytes arise from neuroepithelial progenitors, it seems likely some elements are shared for protein targeting by these types. We hypothesized certain proteins...

10.1002/jnr.10035 article EN Journal of Neuroscience Research 2001-11-30

Abstract The human myelin/oligodendrocyte glycoprotein (MOG) gene is encoded by 10 exons that exhibit a complex pattern of alternative splicing. This report demonstrates several MOG‐specific splice variants are indeed expressed in oligodendrocytes (OLs) and myelin during perinatal development retained through adulthood. While all forms possess the common extracellular Ig‐like domain, these MOG structures differ significantly their respective cytoplasmic domains. Peptide‐specific antibodies...

10.1111/j.1471-4159.2006.04296.x article EN Journal of Neurochemistry 2006-11-14

We investigated the onset of expression myelin/oligodendrocyte glycoprotein (MOG) mRNA and protein in developing mouse central nervous system. In situ hybridization on brain sections at different stages embryonic postnatal development showed that MOG transcripts were first detected birth medulla oblongata. During week after birth, cells expressing located ventral longitudinal funiculus. second week, pattern extended rostrally to mid-forebrain regions reached completion by beginning third...

10.1002/(sici)1098-1136(199609)18:1<39::aid-glia4>3.3.co;2-t article EN Glia 1996-09-01

10.1111/j.1749-6632.1990.tb42392.x article EN Annals of the New York Academy of Sciences 1990-11-01
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