ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80

Koch, G.; Habermann, Barbara; Mohr, Christiane; Just, Ingo; Aktories, Klaus

doi:10.1016/0922-4106(92)90086-b

Cited by 14 publications

(4 citation statements)

References 26 publications

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“…Stimulation of the RBL-2H3 cells with anti-dinitrophenol (DNP) IgE and DNP-conjugated human serum albumin (HSA) triggers degranulation. In addition, mast cells are known to degranulate in response to synthetic compounds, such as compound 48/80 and the calcium ionophore A23187, and these compounds have been used as convenient reagents for direct studies of the mechanisms of in vitro allergy responses [23,24]. The results showed that the cytoplasm of RBL-2H3 that was not activated by the activator contained limited secretory granules.…”

Section: Neferine Reduces the Degranulation Effect Of Rbl-2h3 Stimulated By Different Activatorsmentioning

confidence: 99%

Anti-Allergic and Anti-Inflammatory Effects of Neferine on RBL-2H3 Cells

Chiu

Hung

Wang

et al. 2021

IJMS

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Mast cells play a very important role in skin allergy and inflammation, including atopic dermatitis and psoriasis. In the past, it was found that neferine has anti-inflammatory and anti-aging effects on the skin, but its effect on mast cells has not yet been studied in detail. In this study, we used mast cells (RBL-2H3 cells) and mouse models to study the anti-allergic and inflammatory effects of neferine. First, we found that neferine inhibits the degranulation of mast cells and the expression of cytokines. In addition, we observed that when mast cells were stimulated by A23187/phorbol 12-myristate-13-acetate (PMA), the elevation of intracellular calcium was inhibited by neferine. The phosphorylation of the MAPK/NF-κB pathway is also reduced by pretreatment of neferine. The results of in vivo studies show that neferine can improve the appearance of dermatitis and mast cell infiltration caused by dinitrochlorobenzene (DNCB). Moreover, the expressions of barrier proteins in the skin are also restored. Finally, it was found that neferine can reduce the scratching behavior caused by compound 48/80. Taken together, our results indicate that neferine is a very good anti-allergic and anti-inflammatory natural product. Its effect on mast cells contributes to its pharmacological mechanism.

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Section: Neferine Reduces the Degranulation Effect Of Rbl-2h3 Stimulated By Different Activatorsmentioning

confidence: 99%

Anti-Allergic and Anti-Inflammatory Effects of Neferine on RBL-2H3 Cells

Chiu

Hung

Wang

et al. 2021

IJMS

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“…ADP-ribosylation factor (ARF) ~ is highly enriched in Golgi-derived vesicles and was postulated to be involved in the budding and uncoating of these vesicles (Serafini et al, 1991). Recently a role for ARF proteins in trafficking in the biosynthetic and endocytic pathways has also been reported (Koch et al, 1992;Kahn et al, 1992;Lenhard et al, 1992). With the long-term goal of elucidating the mechanisms responsible for membrane traffic in polarized epithelia, we have been searching for rab proteins involved in apical and basolateral trafficking in polarized epithelial cells.…”

mentioning

confidence: 99%

Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane.

Huber

Pimplikar

Parton

et al. 1993

The Journal of Cell Biology

443

321

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Abstract. Small GTP-binding proteins of the rab family have been implicated as regulators of membrane traffic along the biosynthetic and endocytic pathways in eukaryotic cells. We have investigated the localization and function of rab8, closely related to the yeast YPT1/SEC4 gene products. Confocal immunofluorescence microscopy and immunoelectron microscopy on filter-grown MDCK cells demonstrated that, rab8 was localized to the Golgi region, vesicular structures, and to the basolateral plasma membrane. Two-dimensional gel electrophoresis showed that rab8p was highly enriched in immuno-isolated basolateral vesicles carrying vesicular stomatitis virus-glycoprotein (VSV-G) but was absent from vesicles transporting the hemagglutinin protein (HA) of influenza virus to the apical cell surface.Using a cytosol dependent in vitro transport assay in permeabilized MDCK cells we studied the functional role of rab8 in biosynthetic membrane traffic. Transport of VSV-G from the TGN to the basolateral plasma membrane was found to be significantly inhibited by a peptide derived from the hypervariable COOH-terminal region of rab8, while transport of the influenza HA from the TGN to the apical surface and ER to Golgi transport were unaffected.We conclude that rab8 plays a role in membrane traffic from the TGN to the basolateral plasma membrane in MDCK cells.

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“…However, we observed that Nod factors could activate phospholipase C in vitro independently of heterotrimeric G-proteins (Kelly and Irving 2001), although this does not exclude heterotrimeric G-protein involvement in vivo. Koch et al 1991Koch et al , 1992. All the heterotrimeric G-protein agonists tested induced root hair deformation and, interestingly, this could be inhibited by the phospholipase C antagonists, neomycin and U-73122 (Table 1).…”

Section: Discussionmentioning

confidence: 95%

“…Koch et al 1991Koch et al , 1992. We investigated the effects of these modulators on root hair deformation for two reasons.…”

Section: Resultsmentioning

confidence: 99%

Nod factors activate both heterotrimeric and monomeric G-proteins in Vigna unguiculata (L.) Walp

Kelly

Irving

2003

Planta

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Nod factors are lipo-chito-oligosaccharides secreted by rhizobia that initiate many responses in the root hairs of the legume hosts, culminating in deformed hairs. The heterotrimeric G-protein agonists mastoparan, Mas7, melittin, compound 48/80 and cholera toxin provoke root hair deformation, whereas the heterotrimeric G-protein antagonist pertussis toxin inhibits mastoparan and Nod factor NodNGR[S]-(from Rhizobium sp. NGR234) induced root hair deformation. Another heterotrimeric G-protein antagonist, isotetrandrine, only inhibited root hair deformation provoked by mastoparan and melittin. These results support the notion that G-proteins are implicated in Nod factor signalling. To study the role of G-proteins at a biochemical level, we examined the GTP-binding profiles of root microsomal membrane fractions isolated from the nodulation competent zone of Vigna unguiculata (L.) Walp. GTP competitively bound to the microsomal membrane fractions labelled with [ 35 S]GTPcS, yielding a two-site displacement curve with displacement constants (K i ) of 0.58 lM and 0.16 mM. Competition with either ATP or GDP revealed a one-site displacement curve with K i of 4.4 and 29 lM, respectively, whereas ADP and UTP were ineffective competitors. The GTP-binding profiles of microsomal membrane fractions isolated from roots pretreated with either NodNGR[S] or the four-sugar, N-N'-N''-N'''-tetracetylchitotetraose (TACT) backbone of Nod factors were significantly altered compared with control microsomal fractions. To identify candidate proteins, membrane proteins were separated by SDS-PAGE and electrotransferred to nitrocellulose. GTP overlay experiments revealed that membrane fractions isolated from roots pretreated with NodNGR[S] or TACT contained two proteins (28 kDa and 25 kDa) with a higher affinity for GTPcS than control membrane fractions. Western analysis demonstrated that membranes from the pretreated roots contained more of another protein ($55 kDa) recognised by Ga common antisera. These results provide pharmacological and biochemical evidence supporting the contention that G-proteins are involved in Nod factor signalling and, importantly, implicate monomeric G-proteins in this process.

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ADP-ribosylation of rho proteins is inhibited by melittin, mast cell degranulating peptide and compound 48/80

Cited by 14 publications

References 26 publications

Anti-Allergic and Anti-Inflammatory Effects of Neferine on RBL-2H3 Cells

Anti-Allergic and Anti-Inflammatory Effects of Neferine on RBL-2H3 Cells

Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane.

Nod factors activate both heterotrimeric and monomeric G-proteins in Vigna unguiculata (L.) Walp

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