Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

Caamaño, Claudio A.; Zand, Ramin

doi:10.1016/0014-5793(89)80894-4

Cited by 9 publications

(4 citation statements)

References 25 publications

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“…These data agree with the results of Tzeng et al (1995) that used an ELISA assay to show that MBP 1-44 was able to bind ganglioside GM 1 . Cholera toxin B, however, did not have a significant effect on the mitogenicity of MBP 88-151 , that would indicate that this peptide does not interact with ganglioside GM 1 , contrary to the results of Caamano and Zand (1989) and Tzeng et al (1995). Therefore, the FGFR seems to be the receptor utilized by intact MBP and MBP 152-167 to induce astrocyte proliferation.…”

Section: Discussionsupporting

confidence: 86%

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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Section: Discussionsupporting

confidence: 86%

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

South

Deibler²,

Tzeng

et al. 2000

Glia

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“…Therefore, MBP,-,, may interact with ganglioside GM1 to exert its mitogenic activity, However, MBPx8-151 was not mitogenic for SCs although it was shown to associate with ganglioside GM1 (Tzeng et al, submitted). As shown in Figure 8, comparison of the amino acid sequence of MBP and cholera toxin has revealed a homology between residues 8-19 of MBP and residues 53-64 of CTA which is an activator of G protein (Caamano and Zand, 1989). MBP can bind GTP and MBP can also be ADP-ribosylated, suggesting that MBP has properties similar to that of a G protein (Chan et al, 1988).…”

Section: As Shown Inmentioning

confidence: 97%

“…Amino acid sequence of rabbit MBP indicating the regions of homology to the cholera toxin B and cholera toxin A subunits. The regions of MBP which interact with the ganglioside GM, receptor (1-44) and the FGF receptor (152-167) are indicated; the numbers in parentheses in the indicated cholera toxin binding sites indicate the cholera toxin sequence which is homologous to the sequence of MBP which is underlined(Caamano and Zand, 1989).…”

mentioning

confidence: 99%

Two mitogenic regions of myelin basic protein interact with different receptors to induce Schwann cell proliferation in a cAMP dependent process

Tzeng

Deibler²,

Neuberger

et al. 1995

J of Neuroscience Research

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Previous studies have shown that myelin basic protein (MBP) is mitogenic for Schwann cells (SCs) in the presence of elevated intracellular cAMP. Two mitogenic regions of MBP have been identified: one mitogenic region within the first 44 residues of the aminoterminus (1-44) and the other mitogenic region within the terminal 15 residues of the carboxyl end of the molecule (152-167). Unlike the mitogenic effect of a myelin enriched fraction (MEF), the mitogenic effect of MBP was not reduced by the addition of the lysosomal inhibitor, ammonium chloride. These data indicate that MBP causes SC proliferation by direct interaction of MBP with a surface receptor. Using Scatchard analysis of the binding of MBP to SCs, we report that treatment with forskolin does not cause the upregulation of receptors for MBP. Moreover, MBP blocks the cross-linking of 125I-bFGF with two fibroblast growth factor (FGF) receptors having apparent molecular weights of 140 kDa and 120 kDa, respectively. Since neither TGF-beta nor PDGF-BB displaced cell surface bound 125I-MBP, we conclude that MBP binds to the FGF receptor rather than other growth factor receptors. Furthermore, only MBP interacted with ganglioside GM1, whereas MBP did not interact with this ganglioside. These results are consistent with the view that ganglioside GM1 mediates the mitogenic effects of MBP, while the FGF receptor mediates the mitogenic effect of MBP. Intracellular cAMP of SCs was transiently increased after the addition of macrophage conditioned medium, suggesting that macrophages may produce factors in vivo which can transiently elevate intracellular cAMP levels, allowing a wave of SC proliferation in response to MBP-related mitogens.

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“…One implication of this observation is that these portions of the molecule may have important functions in the MBPdirected myelin formation. [99][100][101] which has been highlighted as an important structural feature (88) similar to that contained in immunoglobin G (IgG) (106), and sequences homologous to cholera toxin A and B subunits [residues 102-118 and 67-77 in human MBP] which may possibly be involved in GM1 ganglioside and GTP binding as well as ADP ribosylation of MBP (107).…”

Section: Sequence --Microheterogeneitymentioning

confidence: 99%

Central nervous system myelin: structure, function, and pathology

Deber

Reynolds

1991

Clinical Biochemistry

109

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Multiple sclerosis (MS) and a number of related distinctive diseases are characterized by the active degradation of central nervous system (CNS) myelin, an axonal sheath comprised essentially of proteins and lipids. These demyelinating diseases appear to arise from complex interactions of genetic, immunological, infective, and biochemical mechanisms. While circumstances of MS etiology remain hypothetical, one persistent theme involves recognition by the immune system of myelin-specific antigens derived from myelin basic protein (MBP), the most abundant extrinsic myelin membrane protein, and/or another equally susceptible myelin protein or lipid component. Knowledge of the biochemical and physical-chemical properties of myelin proteins and lipids, particularly their composition, organization, structure, and accessibility with respect to the compacted myelin multilayers, thus becomes central to the understanding of how and why these antigens become selected during the development of MS. This review focuses on current understanding of the molecular basis underlying demyelinating disease as it may relate to the impact of the various protein and lipid components on myelin morphology; the precise molecular architecture of this membrane as dictated by protein-lipid and lipid-lipid interactions; and the relationship, if any, between the protein/lipid components and the destruction of myelin in pathological situations.

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Homologous sequences in cholera toxin A and B subunits to peptide domains in myelin basic protein

Cited by 9 publications

References 25 publications

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

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

Two mitogenic regions of myelin basic protein interact with different receptors to induce Schwann cell proliferation in a cAMP dependent process

Central nervous system myelin: structure, function, and pathology

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