Interaction of melittin with the (Na+ + K+)ATPase: Evidence for a melittin-induced conformational change

Cuppoletti, John; Abbott, Alan J.

doi:10.1016/0003-9861(90)90639-g

Cited by 38 publications

(17 citation statements)

References 20 publications

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“…Besides its powerful antimicrobial and lytic activity, MLT exhibits a variety of other biological effects. MLT hinder transport pumps, such as (H + + K + ) ATPase (Cuppoletti et al, 1989) and (Na + + K + ) ATPase (Cuppoletti and Abbott, 1990) and accelerate the permeability of cell membranes to ions. It induces inhibition and aggregation of membrane proteins (Clague and Cherry, 1988;Mahaney and Thomas, 1991), and also MLT stimulates activity of phospholipase A2 (Kuchinka and Seelig, 1989).…”

Section: Discussionmentioning

confidence: 99%

Inhibitory effects of bee venom and its components against viruses in vitro and in vivo

et al. 2016

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Bee venom (BV) from honey bee (Apis Melifera L.) contains at least 18 pharmacologically active components including melittin (MLT), phospholipase A (PLA), and apamin etc. BV is safe for human treatments dose dependently and proven to possess different healing properties including antibacterial and antiparasitidal properties. Nevertheless, antiviral properties of BV have not well investigated. Hence, we identified the potential antiviral properties of BV and its component against a broad panel of viruses. Co-incubation of non-cytotoxic amounts of BV and MLT, the main component of BV, significantly inhibited the replication of enveloped viruses such as Influenza A virus (PR8), Vesicular Stomatitis Virus (VSV), Respiratory Syncytial Virus (RSV), and Herpes Simplex Virus (HSV). Additionally, BV and MLT also inhibited the replication of non-enveloped viruses such as Enterovirus-71 (EV-71) and Coxsackie Virus (H3). Such antiviral properties were mainly explained by virucidal mechanism. Moreover, MLT protected mice which were challenged with lethal doses of pathogenic influenza A H1N1 viruses. Therefore, these results provides the evidence that BV and MLT could be a potential source as a promising antiviral agent, especially to develop as a broad spectrum antiviral agent.

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Section: Discussionmentioning

confidence: 99%

Inhibitory effects of bee venom and its components against viruses in vitro and in vivo

et al. 2016

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“…Melittin induces pore formation in erythrocytes (reviewed in Raghuraman and Chattopadhyay, 2007) and inhibits NaKATPase activity (Cuppoletti and Abbott, 1990), activities that could be factors in decreased transport. Additional experiments, such as electrophysiological recordings, could be done to determine whether melittin affects Na + or Cl − gradients across cellular membranes.…”

Section: Discussionmentioning

confidence: 99%

Melittin stimulates fatty acid release through non-phospholipase-mediated mechanisms and interacts with the dopamine transporter and other membrane-spanning proteins

Keith¹,

Eshleman

Janowsky

2011

European Journal of Pharmacology

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Phospholipase A2 releases the fatty acid arachidonic acid from membrane phospholipids. We used the purported phospholipase A 2 stimulator, melittin, to examine the effects of endogenous arachidonic acid signaling on dopamine transporter function and trafficking. In HEK-293 cells stably transfected with the dopamine transporter, melittin reduced uptake of [ 3 H]dopamine. Additionally, measurements of fatty acid content demonstrated a melittin-induced release of membrane-incorporated arachidonic acid, but inhibitors of phospholipase C, phospholipase D, and phospholipase A 2 did not prevent the release. Subsequent experiments measuring [ 125 I]RTI-55 binding to the dopamine transporter demonstrated a direct interaction of melittin, or a melittinactivated endogenous compound, with the transporter to inhibit antagonist binding. This effect was not specific to the dopamine transporter, as [ 3 H]spiperone binding to the recombinant dopamine D 2 receptor was also inhibited by melittin treatment. Finally, melittin stimulated an increase in internalization of the dopamine transporter, and this effect was blocked by pretreatment with cocaine. Thus, melittin acts through multiple mechanisms to regulate cellular activity, including release of membrane-incorporated fatty acids and interaction with the dopamine transporter.

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“…This region contains neurons which project to sympathetic preganglionic neurons of the intermediolateral cell column (36,37). The effects of ouabain may be due to the inhibition of Na ϩ , K ϩ -ATPase in the RVLM, because nonspecific inhibition of Na ϩ , K ϩ -ATPase by melittin, an amphipathic helical polypeptide (38), caused similar effects. Although microinjection of 100 ng of ouabain elicited depressor and sympathoinhibitory responses preceded by initial pressor and sympathoexcitatory responses in two out of seven rats, these responses were probably attributable to profound disturbances in the ionic homeostasis (39) or the neuronal toxicity of ouabain (40).…”

Section: Discussionmentioning

confidence: 99%

Role of ouabain-like compound in the rostral ventrolateral medulla in rats.

Teruya¹,

Yamazato²,

Muratani³

et al. 1997

J. Clin. Invest.

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To determine whether ouabain-like compound (OLC) exerts modulatory influences on the activity of vasomotor neurons in the rostral ventrolateral medulla (RVLM), we examined the effects of microinjecting ouabain, digoxin-specific antibody Fab fragments, and mAb against ouabain on the rat RVLM. Microinjection of ouabain into the unilateral RVLM of anesthetized normotensive rats elicited dose-dependent increases in mean arterial pressure (MAP) and renal sympathetic nerve activity (

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Interaction of melittin with the (Na+ + K+)ATPase: Evidence for a melittin-induced conformational change

Cited by 38 publications

References 20 publications

Inhibitory effects of bee venom and its components against viruses in vitro and in vivo

Inhibitory effects of bee venom and its components against viruses in vitro and in vivo

Melittin stimulates fatty acid release through non-phospholipase-mediated mechanisms and interacts with the dopamine transporter and other membrane-spanning proteins

Role of ouabain-like compound in the rostral ventrolateral medulla in rats.

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