Evidence for receptors for hyaluronan in discrete nerve cell populations of the brain

Fuxé, Kjell; Agnati, Luigi F.; Tinner, B.; Forsberg, Nina; McCourt, Peter; Gustafson, Stefan

doi:10.1016/0006-8993(96)00720-2

Cited by 10 publications

(4 citation statements)

References 17 publications

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“…Previously, Igα v mRNA and protein have been found to be expressed in the rat SN and expression is up‐regulated by the administration of glial‐derived neurotrophic factor (Chao et al ., ), suggesting a role in neuronal survival pathways. Although CD44 receptors were previously reported to be present on dopaminergic neurones in SN (Fuxe et al ., ), a study in mice did not detect the mRNA using in situ hybridisation (Glezer et al ., ).…”

Section: Discussionmentioning

confidence: 99%

“…The mRNA for Igβ 1 has been found in rat SN but there was no expression for Igβ 3 or for Igα v (Pinkstaff et al ., ) although the protein for Igα v was found on nigral dopaminergic neurones (Chao et al ., ). CD44 receptors are expressed by dopaminergic neurones in SN (Fuxe et al ., ) but changes in their distribution in PD models have not been investigated, nor has the interaction of OPN with CD44 or Ig receptors in SN. As a consequence, it is not known whether Igβ 3 and Igβ 1 are expressed in the SN nor is it known whether Igα v , Igβ 3 , Igβ 1 and CD44 receptors are expressed on neurones and/or glial cells.…”

Section: Introductionmentioning

confidence: 99%

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Expression of integrin and CD44 receptors recognising osteopontin in the normal and LPS‐lesioned rat substantia nigra

Ailane

Long

Jenner

et al. 2013

Eur J of Neuroscience

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The multifunctional protein osteopontin (OPN) is expressed in the substantia nigra (SN) and protects nigral dopaminergic neurones against toxic insult in animal models of Parkinson's disease, although the mechanisms involved are uncertain. In the periphery, OPN regulates inflammatory processes by interacting with integrin and CD44 receptors but the presence and distribution of these sites in SN is unknown. We investigated the expression of integrin receptor subunits and CD44 receptors in the normal SN and after induction of inflammation by lipopolysaccharide (LPS), and their interaction with OPN. In normal rat SN, integrin αv , β3 and β1 , and CD44, receptors were expressed on neurones including TH-positive cells but not on glia. LPS administration induced a loss of TH-positive neurones in SN and increased expression of glial cells as shown by GFAP, OX-6 and ED-1 immunoreactivity. In LPS-lesioned SN, there was up-regulation of the expression of integrin β3 and CD44 receptors. Co-localisation studies showed that this related to their increased expression on OX-6-, ED-1- and GFAP-positive cells. Furthermore, OPN interacted with integrin and CD44 receptors in the normal rat SN as demonstrated by co-immunoprecipitation and pull-down techniques. These data show that integrin and CD44 receptors are present on neurones in normal rat SN and that they are up-regulated on glial cells following LPS-mediated inflammation in SN, suggesting that they are functionally important in the inflammatory process. The interaction of OPN with these receptors suggests a role in the neuroprotective effect of this protein in the LPS model of Parkinson's disease.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Expression of integrin and CD44 receptors recognising osteopontin in the normal and LPS‐lesioned rat substantia nigra

Ailane

Long

Jenner

et al. 2013

Eur J of Neuroscience

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“…Of particular interest to us are molecules known to be associated with neuronal plasticity, and several of them have been found at particularly high levels in the SOC of adult mammals, such as the rat. Among these are the growth factors BDNF (Hafidi, 1999), FGF-2 (Grothe and Janet, 1995), and NGF (Nishio et al, 1994), the mRNA of GAP-43, a protein associated with axonal growth (Illing et al, 1999), and receptors for hyaluronic acid, which may activate protein kinase activity or influence the architecture of the cytoskeleton (Fuxe et al, 1996). Moreover, neurons of the SOC appear to be unique in the handling of certain integrin subunits.…”

Section: Olivocochlear Neuronsmentioning

confidence: 99%

Plasticity of the superior olivary complex

Illing

Kraus

Michler

2000

Microsc. Res. Tech.

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“…Numerous secreted and cell‐associated hyaladherins have been found in brain and spinal cord, including CD44, aggrecan, versican, neurocan, BEHAB/brevican, glial HA‐binding protein, and hyaluronectin (Kuppner et al, 1992; Rauch et al, 1992; Bignami et al, 1993a,b; Delpech et al, 1993; Fuxe et al, 1996; Yamada et al, 1997), although the functions of these and of HA in the CNS are poorly understood. As in peripheral tissue, in which studies of hyaladherins have provided an understanding of their functional importance in relation to interactions with HA, investigations of these proteins in the CNS are expected to shed light on the actions of HA in this HA‐rich tissue.…”

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confidence: 99%

Identification of sequence, protein isoforms, and distribution of the hyaluronan‐binding protein RHAMM in adult and developing rat brain

Lynn

Cattini

et al. 2001

J of Comparative Neurology

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The protein RHAMM (for "receptor for hyaluronan-mediated motility"; CD168) is a member of the hyaladherin family of hyaluronan-binding proteins. RHAMM has a role in cell signaling, migration, and adhesion via interactions with hyaluronan, microtubules, actin, calmodulin, and components of the extracellular regulated kinase (erk) signaling pathway. Based on previous findings of potentially similar roles in neural cells in culture, we investigated the molecular characteristics, protein expression profile, and distribution of RHAMM in rat brain. Reverse transcriptase-polymerase chain reaction (RT-PCR) using RNA isolated from adult rat brain yielded a single RHAMM sequence of 2.1 kilobases encoding a protein of 82.4 kDa. RHAMM is subject to alternate splicing in other systems, but no RT-PCR evidence was found for splice variants in brain, although our analysis does not rule out this possibility. The amino acid sequence displayed homology with human and murine RHAMM (74% and 80%, respectively) but contained only one copy of a 21-amino-acid sequence that is repeated five times in the murine homologue. By using anti-RHAMM antibodies, several RHAMM isoforms were identified in brain. Immunohistochemically, RHAMM was found in the vast majority of neurons and in many oligodendrocytes throughout brain, with heterogeneous levels among cell populations, and was confined to the somata and initial processes of these cells. RHAMM was detected in neurons of cerebral cortex and most subcortical and brainstem structures at postnatal day 1 and exhibited an adult distribution pattern by postnatal day 5. High levels were detected in oligodendrocytes by postnatal day 10. The widespread expression of RHAMM in adult and developing brain implies a role for this protein and its ligand hyaluronan in key events of cell signaling and cytoskeletal regulation in the CNS.

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Evidence for receptors for hyaluronan in discrete nerve cell populations of the brain

Cited by 10 publications

References 17 publications

Expression of integrin and CD44 receptors recognising osteopontin in the normal and LPS‐lesioned rat substantia nigra

Expression of integrin and CD44 receptors recognising osteopontin in the normal and LPS‐lesioned rat substantia nigra

Plasticity of the superior olivary complex

Identification of sequence, protein isoforms, and distribution of the hyaluronan‐binding protein RHAMM in adult and developing rat brain

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