Myelin basic protein stimulates the proliferation of astrocytes: possible explanation for multiple sclerosis plaque formation

Bologa, Liane; Deugnier, Marie‐Ange; Joubert, Raymonde; Bisconte, J. C.

doi:10.1016/0006-8993(85)91117-5

Cited by 32 publications

(15 citation statements)

References 25 publications

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“…Binding of MBP to astrocytes was previously shown (Owh et al, 1997), as well as its role in the induction of astrocyte proliferation (Bologa et al, 1985;South et al, 2000). Furthermore, a recent study (Schluesener and Seid, 2000) reports an increased expression of HO-1 in monocytes, microglia, and astrocytes surrounding the inflammatory lesions of rat experimental autoimmune encephalomyelitis, a commonly used animal model of multiple sclerosis.…”

Section: ϩmentioning

confidence: 80%

“…Furthermore, recent reports indicate the central role of oxidative stress in axon and myelin damage observed during multiple sclerosis (Smith et al, 1999;Bartnik et al, 2000) and the occurrence of HO-1 in astrocytes surrounding inflammatory lesions of rat experimental autoimmune encephalomyelitis (Schluesener and Seid, 2000). Myelin basic protein (MBP) and several MBP-related peptide fragments produced by macrophage proteolytic processing of myelin stimulate astrocyte proliferation (Bologa et al, 1985;South et al, 2000), suggesting a direct effect of these factors on glial cells. This work determined whether MBP induced HO-1 in human astroglial cells.…”

Section: ϩmentioning

confidence: 99%

“…We observed a single band of 32 kD, which results to be increased by 60% compared to controls, following treatment with 5 or 10 M MBP. Since the maximum effect was achieved by 5 M MBP and a similar range of concentrations proved to be effective in the induction of astrocyte proliferation (Bologa et al, 1985), besides to be used to induce experimental allergic encephalomyelitis in animal models (Sobel et al, 1984;De Santis and Roth, 1996), the dose of 5 M was chosen for subsequent experiments. Similar results were obtained using the glioblastoma cell line T70 (not shown).…”

Section: ϩmentioning

confidence: 99%

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Myelin basic protein induces heme oxygenase‐1 in human astroglial cells

Businaro

Fabrizi

Caronti

et al. 2001

Glia

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Heme oxygenase-1 (HO-1), also known as heat-shock protein 32 (HSP-32), is induced in many cells by a large variety of stimuli. Its induction in nervous system cells following toxic and oxidative stress was suggested to play a protective role. Its presence was recently detected by immunohistochemical studies at the level of inflammatory lesions of rat experimental autoimmune encephalomyelitis. In the present study, we demonstrate that myelin basic protein (MBP) induces HO-1 in human astroglial cells, as shown by Western blots and RT-PCR. Proteolytic fragments derived from the whole MBP show a different behavior in the HO-1 induction: MBP152-167 was able to produce a light but still significant increase in HO-1 mRNA and protein levels, whereas MBP68-84 was not. The increase in HO-1 production seems to be mediated by a Ca(2+)-dependent mechanism, since MBP addition to astrocytoma cultures induced a strong and immediate increment of [Ca(2+)](i) increase; MBP152-167 elicited a delayed and less pronounced [Ca(2+)](i) increase; no [Ca(2+)](i) changes were induced following cell treatment with MBP68-84. NO pathway involvement in the induction of HO-1 by MBP was ruled out since the expression of the inducible isoform of nitric oxide synthase was not upregulated in treated cells, neither nitrite levels were modified, as demonstrated by Greiss reaction. The possible significance of HO-1 induction following MBP stimulation is discussed.

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Section: ϩmentioning

confidence: 80%

Section: ϩmentioning

confidence: 99%

Section: ϩmentioning

confidence: 99%

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Myelin basic protein induces heme oxygenase‐1 in human astroglial cells

Businaro

Fabrizi

Caronti

et al. 2001

Glia

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“…Yachnis and Mescher [3] found that myelin contained proteinaceous cellular growth factors. Furthermore, Westmark and Wasteson [4] and Bologa et al [5] found that normal glia and astrocytes were stimulated by these growth factors. Therefore, rapid cellular proliferation, which has been deemed adverse, may be initiated by released growth factors.…”

Section: Discussionmentioning

confidence: 99%

“…It has also been shown that cell proliferation factors are released during nerve degeneration [3]. Such factors stimulate both oligodendrocyte and astrocyte proliferation [4,5,6]. Astroglial proliferation may contribute to plaque formation in MS, resulting in increasing clinical disability.…”

Section: Introductionmentioning

confidence: 99%

Cell Proliferation Inhibition in Remitting Multiple Sclerosis CSF

Westall¹,

Seil

2006

Eur Neurol

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Sixty percent of the CSF samples from 21 multiple sclerosis (MS) patients in remission inhibited cellular proliferation of a variety of neuronal and glial cell lines. No inhibition was observed with CSF from relapsing or progressive MS patients (0/19). Two of 82 samples from stationary MS patients were positive. No inhibition was found in MS sera. The CSF samples had no effect on myelination of mouse organotypic cerebellar cultures. Like MS cellular proliferation and subsequent lesion formation, the ‘deactivation’ of the lesion also is an active defined process, rather than just the cessation of the immunological events. Furthermore, approximately 20% of samples from Huntington’s, Alzheimer’s and Parkinson’s disease patients were also positive. However, no inhibition was seen in CSF from amyotrophic lateral sclerosis patients or controls.

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Myelin basic protein (MBP) and MBP peptides are mitogens for cultured astrocytes

South

Deibler²,

Tzeng

et al. 2000

Glia

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After CNS demyelination, astrogliosis interferes with axonal regeneration and remyelination. We now provide evidence that myelin basic protein (MBP) can contribute to this observed astrocyte proliferation. We found that astrocytes grown in either serum‐containing or serum‐free medium proliferate in response to MBP. The mitogenic regions of MBP in both media were MBP1–44, MBP88–151 and MBP152–167. The mitogenic effect of these individual peptides was potentiated by simultaneous treatment with microglia conditioned media (CM). MBP‐induced proliferation was inhibited by suramin at concentrations known to block the fibroblast growth factor receptor (FGFR), whereas neither MBP1–44, MBP88–151 nor MBP152–167 were affected. Cholera toxin B, that binds to ganglioside GM1, inhibited the mitogenicity of MBP1–44 and had no significant effect on the mitogenicity of MBP, MBP88–151 or MBP152–167. Treatment of astrocytes with MBP and MBP152–167 caused a modest and transitory elevation of intracellular calcium, whereas treatment with MBP1–44 resulted in a substantial and sustained increase in intracellular calcium. These results suggest that for cultured astrocytes 1) FGFR and extracellular calcium play a major role in MBP mitogenicity; 2) MBP1–44, MBP88–151 and MBP152–167 are the mitogenic regions of MBP; 3) MBP1–44 and MBP152–167 interact with ganglioside GM1 and FGFR, respectively; 4) Component(s) present in microglial CM potentiate the mitogenicity of MBP1–44, MBP88–151 and MBP152–167. These data support the hypothesis that MBP related peptides in conjunction with microglial secreted factors may stimulate astrogliosis after demyelination in vivo. GLIA 29:81–90, 2000. © 2000 Wiley‐Liss, Inc.

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Myelin basic protein stimulates the proliferation of astrocytes: possible explanation for multiple sclerosis plaque formation

Cited by 32 publications

References 25 publications

Myelin basic protein induces heme oxygenase‐1 in human astroglial cells

Myelin basic protein induces heme oxygenase‐1 in human astroglial cells

Cell Proliferation Inhibition in Remitting Multiple Sclerosis CSF

Myelin basic protein (MBP) and MBP peptides are mitogens for cultured astrocytes

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