bluuebunny/crossref_metadata_2025_split huggingface dataset:
Age‐related loss of knee joint afferents in mice
Authors: Salo P. T. , Tatton W. G. 
Published: January 2005

AbstractPrevious work in our laboratory revealed markedly different rates of age‐related death of four monoaminergic neuronal populations in the C57BL/6 mouse. Although dorsal root ganglion neurons (DRGns) have been reported not to suffer similar age‐related death in rodents, we determined if there is age‐related death of the subpopulation of DRGns innervating the knee joints of C57BL/6 mice, which are known to develop degenerative arthritis with aging. The somata of dorsal root ganglion neurons innervating the mouse knee joint (KJ‐DRGns) were identified by retrograde tracing with Fluoro‐Gold (FG). Lumbar ganglia were serially sectioned and the numbers of FG‐labelled KJ‐DRGns counted at five ages encompassing the animal's life span. Changes in size of the total population of lumbar DRGns (L‐DRGns) were estimated by counting nucleated somata from every fifth toluidine blue‐stained serial section from the L3 and L4 lumbar ganglia at three different ages. Using a computer‐assisted video morphometric technique somal areas were measured from random sections to determine the distribution of sizes of neurons in the KJ‐DRGn and general lumbar DRGn populations at different ages. Counts of FG‐labelled joint afferents were 238.5 ± 80.3 (mean SD) KJ‐DRGns per knee at 2 months of age, declining to 103.2 ± 20.1 by 24 months, representing a 57% loss over the average life span of the C57 mice. The loss occurred in two phases, with a rapid rate over the first 8 months of life and a more moderate rate of loss over the remaining months. L‐DRGn numbers revealed a slower overall rate of loss in comparison to the KJ‐DRGn population with an average 33.7% loss over the life span of this mouse. Somal size measurements revealed that the larger sizes of KJ‐DRGns were lost over the first 8 months of life, with little change in the distribution of somal sizes thereafter. The distributions of sizes of the L‐DRGn population did not change significantly over the life spans of the mice. The data provides evidence that the age‐related loss of KJ‐DRGns is significantly greater than DRGns in general, and may be particularly apparent in the population of largersized presumed mechanoreceptor neurons. The loss of the KJ‐DRGns is approximately reciprocal to the incidence rate of knee joint osteoarthritis reported for the C57BL/6 mice. © 1993 Wiley‐Liss, Inc.
Expression of the metabotropic glutamate receptor mGluR1α and the ionotropic glutamate receptor GluR1 in the brain during the postnatal development of normal mouse and in the cerebellum from mutant mice
Authors: Ryo Y. , Miyawaki A. , Furuichi T. , Mikoshiba K. 
Published: January 2005

AbstractExpression of the metabotropic glutamate receptor type 1α (mGluR1α) and the non‐N‐methyl‐D‐aspartate (NMDA) ionotropic glutamate receptor type 1 (GluR1) in mouse brain was investigated using the antibodies raised against the synthetic peptides corresponding to their C‐terminal amino acid sequences. Both receptor proteins are glycosylated predominantly in an asparagine‐linked manner, and are abundant in post‐synaptic membranes. We showed that mGluR1α and GluR1 expression within the first 3 postnatal weeks undergoes dramatic changes in time and space, i.e., in the hippocampus and cerebellum. These spatio‐temporal expression patterns appear to be correlated with the postnatal ontogenesis and establishment of the glutamatergic neurotransmission system in the hippocampus and cerebellum, cell migration, dendritic and axonal growth, spine formation, and synaptogenesis. In the adult cerebellum, mGluR1α is intensely expressed in Purkinje neurons and GluR1 in Bergmann glial cells. Both receptors are expressed to a fair degree in weaver mutant cerebellum despite granule cell degeneration. However, the intrinsic expression levels of both mGluR1α and GluR1 are markedly reduced in the cerebellum of the Purkinje cell‐deficient and underdeveloped mutant mice, Purkinje‐cell‐degeneration, Lurcher, and staggerer, suggesting that GluR1 expression in Bergmann glia cells may be correlated with the sustained interaction with adjacent Purkinje neurons. © 1993 Wiley‐Liss, Inc.
Purification and characterization of NCAD90, a Soluble endogenous form of N‐cadherin, which is generated by proteolysis during retinal development and retains adhesive and neurite‐promoting function
Authors: Paradies N. E. , Grunwald G. B. 
Published: January 2005

AbstractThe cadherins are calcium‐dependent cell adhesion molecules which regulate cell–cell interactions during morphogenesis. During development, cadherin expression is subject to dynamic patterns of regulation. We have previously demonstrated that expression of N‐cadherin, the predominant cadherin of neural tissues, is sharply down‐regulated during development of the retina and brain during later stages of histogenesis (Lagunowich and Grunwald, Dev Biol 135:158–171, 1989; Lagunowich et al., J Neurosci Res32;202–208, 1992), and that this down‐regulation is due to multiple factors, including decreased mRNA levels and turnover apparently mediated by endogenous metalloproteolytic activity (Roark et al., Development 114:973–984, 1992). In the present study, we describe metabolic studies which provide direct biochemical evidence for turnover of 130‐kDa N‐cadherin in embryonic retina tissues, yielding a soluble 90‐kDa N‐terminal fragment. We demonstrate that this form of N‐cadherin, which we refer to as NCAD90, accumulates in vivo during development. We further demonstrate that purified NCAD90, obtained from embryonic vitreous humor, retains biological function and promotes cell adhesion and neurite growth in a dose‐dependent fashion among chick embryo neural retina cells when present in a substrate‐bound form. The morphology of retinal cells and neurites grown on a substrate of NCAD90 differs strikingly from that seen on a laminin substrate, in a manner similar to that described for intact 130‐kDa N‐cadherin. We conclude that proteolysis of N‐cadherin at the cell surface during embryonic retinal histogenesis is an endogenous mechanism for regulating N‐cadherin expression which generates a novel and functional from of the protein. The results further indicate that an intact cytoplasmic domain is not essential for all cadherin functions. © 1993 Wiley‐Liss, Inc.
Microtubule‐associated protein 2 appears in axons of cultured dorsal root ganglia and spinal cord neurons after rotavirus infection
Authors: Weclewicz K. , Svensson L. , Billger M. , Holmberg K. , Wallin M. , Kristensson K. 
Published: January 2005

AbstractThe immunohistochemical distribution of microtubule‐associated protein 2 (MAP2), being normally restricted to nerve cell bodies and dendrites, became altered in rat dorsal root ganglia and spinal cord neurons in cultures infected with rhesus rotavirus. MAP2 appeared in axons of both sources of neurons as displayed with monoclonal antibodies to MAP2a+b and MAP2a+b+c at 48 hr post‐infection (p.i.). Other cytoskeletal elements, i.e., tau, MAP1, MAP5, neurofilament, actin, and tubulin, did not reveal any alterations in the rotavirus‐infected neurons. One of the rotavirus cytosolic proteins, the inner capsid protein vp6, was expressed in axons at 48 hr p.i. simultaneously with the appearance of MAP2, while two other viral proteins, vp4 and NS28, remained in the nerve cell bodies. By quantitative enzyme‐linked immunosorbent assay (ELISA) a binding of single‐shelled rotaviruses, which express vp6 on their surfaces, to purified MAP2 was found. There was no binding of these viral particles to tau or tubulin proteins. This study indicates that a selective interaction between certain viral and neuronal cytoskeletal proteins can occur and that a non‐cytolytic viral infection can cause alterations in the polarized sorting of neuronal proteins. © 1993 Wiley‐Liss, Inc.
Atypical localization of the oligodendrocytic isoform (PI) of glutathione‐S‐transferase in astrocytes during cuprizone intoxication
Authors: Cammer W. , Zhang H. 
Published: January 2005

AbstractImmunocytochemical staining for the Pi and Mu isoforms of glutathione‐S‐transferase was used to investigate changes in the glial cells in the mouse forebrain. During early development in mouse forebrains the localizations of carbonic anhydrase, Pi and Mu were similar to the respective cellular localizations that had been observed in neonatal rat brain. That is, Pi was found in oligodendrocyte precursors, Mu in astrocytes, and carbonic anhydrase in both oligodendrocyte precursors and astrocytes. In forebrains of 6‐week‐old mice the neurotoxicant, cuprizone, induced oligodendrocyte degeneration, gliosis, and partial demyelinatin. Degeneration of oligodendrocytes, and astrocytosis, began during the initial week of cuprizone feeding, and by the end of the eighth week some demyelination was observed. After mice were fed cuprizone for 4 to 7 weeks, Pi appeared in some of the reactive astrocytes, and Pi‐positive astrocytes were present for at least 7 additional weeks. Normally, Pi appeared only in oligodendrocyts. Very few Pi‐positive oligodendrocyes remained after the second week. During the eighth week healthy‐looking carbonic anhydrase‐positive oligodendrocytes reappeared and began to accumulate, and a few small patches of Pi‐positive oligodendrocytes were also observed. In summary, some novel findings about glial cells were the observation of an enzyme (Pi) that is lost earlier from oligodendrocytes than is carbonic anhydrase, the apparently unique shift in Pi expression from oligodendrocytes to astrocytes and the greater temporal dissociation between loss of oligodendrocytes and demyelination in the older mice. © 1993 Wiley‐Liss, Inc.
Characterization of the neuroimmune protein F5: Localization to the dendrites and perikarya of mature neurons and the basal aspect of choroid plexus epithelial cells
Authors: Arai M. , Cohen J. A. 
Published: January 2005

AbstractF5 was identified originally as an interleukin‐2‐regulated gene in L2 cells, a murine helper T‐lymphocyte clone. In adult mouse, F5 mRNA was expressed at a modest level in lymphoid tissues, at a high level in mature neurons in the nervous system, but not in other tissues. Although the F5 sequence is highly conserved over evolution, the function of the F5 protein is unknown. In the present studies, the putative F5 protein coding region was translated in vitro using a reticulocyte lysate system and in Escherichia coli, yielding a protein with the predicted molecular weight of 42 kDa. Polyclonal rabbit anti‐F5 antibody specifically recognized recombinant F5 protein. Western blot studies demonstrated a strongly‐reactive 42‐kDa band and a faint 39‐kDa band in extracts of adult mouse brain regions, the levels of which paralleled F5 mRNA expression. Immunoperoxidase studies of adult mouse brain demonstrated F5 immunoreactivity in neuronal perikarya and dendrites but not axons. Neurons expressing the highest levels of F5 protein corresponded to those with the highest levels of F5 mRNA. Choroid plexus epithelial cells also exhibited strong reactivity localized to their basal aspect. These observations suggest that the F5 protein, expression of which appears to be regulated predominantly at the RNA level, may be involved in the maintenance of the functional or anatomic polarity of neurons and choroid plexux epithelial cells. © 1993 Wiley‐Liss, Inc.
cDNA cloning and expression of stress‐inducible rat hsp70 normal and injured rat brain
Authors: Longo F. M. , Wang S. , Narasimhan P. , Zhang J. S. , Chen J. , Massa S. M. , Sharp F. R. 
Published: January 2005

AbstractA reverse transcriptase‐polymerase chain reaction(RT‐PCR) product obtained from ischemic rat brain RNA was used to screen a rat ischemic forebrain cDNA library for a cDNA clone containing the entire open reading frame for the inducible hsp70. The coding sequence for the rat hsp70 cDNA demonstrated significant similarities with the human hsp70 of Hunt and Morimoto (Proc Natl Acad Sci82:6455–6459, 1985) and the mouse hsp70 of Hunt and calderwood (Gene87:199–204, 1990). The rat inducible hsp70 and constitutive hsc73 sequences are distinct. There was a low level of hsp70 mRNA expression in normal rat brain as is found in other tissues. hsp70 mRNA was markedly induced in rat brain 8 hours following global ischomia and kainic acid‐induced sizures. Northern blots showed a ∼2.9kb hsp70 mRNA band from control, kainic acid, and ischemic brains. RTPCR confirmed the presence of hsp70 mRNA in normal rat brain. Since there are at least five human and six mouse inducible hsp70 genes known, many other rat hsp70 genes probably exist that could function in different cells or organelles or be induced under different circumstances. © 1993 Wiley‐Liss, Inc.
Induction of primary T cell responses by human glial cells
Authors: Williams K. , Ulvestad E. , Cragg L. , Blain M. , Antel J. P. 
Published: January 2005

AbstractGlial cells of the central nervous system (CNS) are postulated to function as immune accessory cells which may regulate immune reactivity occurring within the CNS, activating or alternatively inhibiting T cell responses. We have utilized surgically resected cerebral tissue derived from young adult humans to prepare dissociated cultures of glial cells (mixed astrocyte‐microglia‐oligodendrocyte cultures) and demonstrate that such cells are capable of acting as stimulators of primary T cell responses, using proliferation of T cells to allogeneic determinants on the glial cells as the test system. Studies of resected adult cerebral tissue indicated major histocompatibility complex (MHC) class II antigen expression on microglia in situ. Using a mixed lymphocyte reaction (MLR), we observed that enriched microglial cultures alone were capable of stimulating primary responses of freshly isolated T cells or the CD4+ T cell subset, a response which could be inhibited with an anti‐MHC class II blocking antibody. In agreement with previous studies using rodent‐derived astrocytes, we found that human astrocytes (fetal), could not initiate a primary T cell response even after up‐regulation of MHC class II antigen expression with interferon gamma (IFNγ) and tumor necrosis factor alpha (TNFα). Our results indicate that a primary T cell response, as well as a secondary response to a recall antigen, can occur within the CNS; our data implicate microglia as the central cell involved in the former. © 1993 Wiley‐Liss, Inc.
Cellular reaction to an acute demyelinating/remyelinating lesion of the rat brain stem: Localisation of GD3 ganglioside immunoreactivity
Authors: Reynolds R. , Wilkin G. P. 
Published: January 2005

AbstractWe describe a simple and reproducible acute demyelinating lesion of the rat brain stem induced by injection of ethidium bromide into the cisterna magna of young adult rats. Using immunofluorescence with a panel of antibodies to cell‐specific antigens we have studied the changes in cell populations that occur at various stages during lesion progression and repair. In particular we localized the expression of ganglioside GD3 immunoreactivity, a marker for oligodendroglial progenitors in developing brain. Both astroglia (GFAP+) and oligodendroglia (CNP+) were destroyed during the early response to the ethidium bromide although axons were spared. Splitting of myelin lamellae occurred as early as 4 days post‐injection (DPI), with extensive demyelination of the inferior cerebellar peduncle following by 6 DPI. Large numbers of ED1+ and OX‐42+ macrophages were present in the lesion site at this stage. Astrogliosis occurred around the perimeter of the lesions. Two populations of GD3+ cells appeared within and around the lesion sites during the demyelination. One population was identified by the phenotype GD3+ ED1+ and thus probably belonged to the macrophage/microglial lineage. In these cells both antigens appeared cytoplasmic. The second population of GD3+ cells exhibited cell membrane GD3 immunoreactivity but did not express the ED1 antigen. These cells are suggested to be oligodendroglial progenitors generated in response to the demyelination. No such cells were seen in control tissue. GD3+ cells were present within the lesion sites from 6 DPI until 10–12.Following the clearance of myelin debris from the lesions, remyelination was a relatively rapid event with thin MBP+ myelin sheaths first seen at 11–12 DPI. Remyelination, which was extensive by 25 DPI, was predominantly oligodendroglial in origin (MBP+Po− myelin) with only small pockets of peripheral myelin (MBP+Po+ myelin) observed. The present study, in addition to identifying putative glial progenitors within a demyelinated lesion, also demonstrates the difficulties in unambiguously identifying such cells in the normal and damaged adult CNS. © 1993 Wiley‐Liss, Inc.
Myelination in cerebellar slice cultures: Development of a system amenable to biochemical analysis
Authors: Notterpek L. M. , Bullock P. N. , Malek‐Hedayat S. , Fisher R. , Rome L. H. 
Published: January 2005

AbstractMyelin deposition and maintenance are critical to proper function of the mammalian nervous system. Previous investigations of myelination in the central nervous system (CNS) were hampered by the lack of an in vitro system that can faithfully reproduce in vivo events yet is amenable to biochemical investigation. We have developed a procedure, based on organotypic cultures, which permits efficient preparation of large numbers of cerebellar slice cultures that can be easily manipulated. Cultures have been examined to document myelination biochemically (by incorporation of [35S] sulfate into sulfolipids), immunohistochemically (by labeling the myelin components myelin basic protein and galactocerebroside), and morphologically (by both light and electron microscopy). We tested the effects of biologically active peptides and antibodies on myelination in the thin slices. The results indicate that the cultures provide an in vitro system that can be used to examine specific cellular events that occur during CNS myelination. © 1993 Wiley‐Liss, Inc.
Members of several gene families influence survival of rat motoneurons in vitro and in vivo
Authors: Hughes R. A. , Sendtner M. , Thoenen H. 
Published: January 2005

AbstractThe survival and functional maintenance of spinal motoneurons, both during the period of developmental cell death and in adulthood, have been shown to be dependent on trophic factors. In vitro experiments have previously been used to identify several survival factors for motoneurons, including CNTF, LIF, and members of the neurotrophin, FGF, and IGF gene families. Some of these factors have also been shown to be active in vivo, either on chick motoneurons during embryonic development or on lesioned facial and spinal motoneurons of the newborn rat. Here we demonstrate that lesioned newborn rat facial motoneurons can be rescued by NT‐4/5, IGF‐I and LIF. Furthermore, in contrast to chick motoneurons, the survival of isolated embryonic rat motoneurons can be maintained by the neurotrophins BDNF, NT‐3, and NT‐4/5. IGF‐I and FGF‐5 were also active in this system, each supporting more than 50% of the originally plated neurons. The responsiveness of motoneurons to multiple factors in vitro and in vivo suggests that motoneuron survival and function are regulated by the coordinated actions of members of different gene families. © 1993 Wiley‐Liss, Inc.
Trophic effects of basic fibroblast growth factor (bFGF) on differentiated oligodendroglia: A mechanism for regeneration of the oligodendroglial lineage
Authors: Grinspan J. B. , Stern J. L. , Franceschini B. , Pleasure D. 
Published: January 2005

AbstractWe have investigated the effect of basic fibroblast growth factor (bFGF) on the proliferation and phenotype of differentiated oligodendroglia. Using primary cell cultures enriched in oligodendrocytes but containing few O2A‐oligodendrocyte progenitor cells, we demonstrate that bFGF treatment greatly increases the proportion of 02A cells while decreasing the proportion of galactocerebroside +(GalC+), myelin basic protein +(MBP+) oligodendrocytes, and the steady state levels of MPB mRNA. Complement mediated cell lysis experiments using the A2B5 antibody to deplete existing O2A cells or the R‐Mab antibody to deplete existing oligodendroglia show that bFGF elicits a rapid increse in the number of O2A cells in cultures previously depleted of O2A cells, but does not cause an early incrase in O2A cells in cultures from which oligodendroglia had been removed, indication that the oligodendrocytes are the source of the newly recruited O2A cells. This bFGF‐mediated transition from oligodendrocyte to O2A cells occurs with a time course similar to the bFGF‐induced incrase of the proliferation rate of the GalC+ oligo‐dendrocvtes. Studies with purified, passaged cells of the oligodendroglial lineage show that bFGF augmenta oligodendroglial dedifferntiation and proliferation in chronologically adult oligodendrocytes and in the virtual absence of other cell types. We have thusdemonstrated that mature oligodendrocytes are induced by bFGF to dedifferentiate and proliferate, suggesting a mechanism for regeneration of the oligodendroglial lineage following demyelinating disease. © 1993 Wiley‐Liss, Inc.
Humoral immune recognition of proteolipid protein (PLP)‐specific encephalitogenic epitopes in the SJL/J mouse
Authors: Potter N. T. , Stephens T. S. 
Published: January 2005

AbstractSJL/J mice were immunized with human PLP as well as encephalitogenic PLP peptides 139–151 and 178–191 and the resulting antibody responses examined for immunochemical specificity employing a panel of 17 synthetic PLP peptide ligands. All animals had demonstrable circulating titers of antibodies early in the humoral immune response to their respective encephalitogens, however, there was no clear qualitative correlation between antibody responses and the induction of EAE. In the majority of PLP immunized animals, determinant‐specific antibody populations, including those against encephalitogenic centers, were not detectable in the presence of an anti‐PLP antibody response. Antiencephalitogenic peptide antibodies were present in both 139–151 and 178–191 immunized animals regardless of clinical/histologic status. Neither group produced cross‐reactive anti PLP antibodies as detected by ELISA. In animals immunized with peptide 139–151, only anti‐139–151 antibody specificities were noted. In contrast, all animals immunized with peptide 178–191 had an antibody population cross‐reactive with three other PLP peptides: 97–110, 209–217, and 215–228. As humoral immune responses can be demonstrated against PLP‐specific encephalitogenic epitopes, the significance of these B cell responses should be considered in the context of their potential role in the development, modulation, and/or potentiation of EAE. © 1994 Wiley‐Liss, Inc.