Disease relevance of Mcdp

• RESULTS: Venom toxicity required the synergistic action of two venom components, a mast cell degranulating peptide mastoparan and phospholipase A1 [1].

High impact information on Mcdp

• One of these, the mast cell degranulating peptide (MCD), releases histamine from mast cells and on central administration produces arousal at low concentrations and convulsions at higher doses [2].
• Interestingly, the binding site for 125I-labeled mast cell degranulating peptide, another putative K+-channel ligand from bee venom, which induces long-term potentiation in hippocampus, seems to reside on the same protein complex, as both binding sites copurify through the entire purification protocol [3].
• Binding was sensitive to scyllatoxin, dequalinium, gallamine, and d-tubocurarine but not to charybdotoxin, toxin I, or mast cell degranulating peptide [4].
• The characterization of high-affinity binding sites in rat brain for the mast cell-degranulating peptide from bee venom using the purified monoiodinated peptide [5].
• Specific modification of the primary amines, arginine residues, or disulfide bridges of MCD peptide results in a complete loss of binding activity [5].

Biological context of Mcdp

• MCDP is also an epileptogenic neurotoxin, an avid blocker of the potassium channels and can cause a significant lowering of the blood pressure in rats [6].
• A bee venom, mast cell degranulating peptide (MCD), which induces long-term potentiation (LTP) of synaptic transmission in hippocampal slices, was found to possess multiple functions [7].
• In high-K+, IC50 of MCDP for component f1 was 99 nM, whereas it was 7.6 microM for f2 [8].
• Amino acid sequence of bumblebee MCD peptide: a new mast cell degranulating peptide from the venom of the bumblebee Megabombus pennsylvanicus [9].
• Mast cell degranulating peptide induces the expression of the c-fos proto-oncogene in hippocampus [10].

Anatomical context of Mcdp

• MCDP is a potent anti-inflammatory agent, but at low concentrations it is a strong mediator of mast cell degranulation and histamine release [6].
• The preparation of a pure, monoiodinated derivative of mast cell-degranulating peptide (MCD peptide), the mast cell-degranulating peptide from bee venom, has enabled us to identify binding sites in rat brain membranes that have a high affinity and specificity for this peptide [5].
• These binding sites are probably associated with the neurotoxic action of MCD peptide in the central nervous system [5].
• Intracellular recordings in sensory ganglion cells showed that mast cell degranulating peptide blocks the same slowly inactivating potassium current as dendrotoxin but with lower potency, the respective IC50 values in sensory A neurons of nodose ganglion being 2.1 nM and 37 nM [11].

Associations of Mcdp with chemical compounds

• Inhibition of beta-bungarotoxin binding to brain membranes by mast cell degranulating peptide, toxin I, and ethylene glycol bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid [12].
• Compounds investigated include corticotropin and melittin derivatives, mast-cell-degranulating peptide from bee venom, polymyxin B, bradykinin and various synthetic poly(amino acids) and short-chain peptides [13].
• Inhibition of prostaglandin biosynthesis by the mast-cell-degranulating agent compound 48/80 but not by the mast-cell-degranulating peptide (peptide-401) from bee venom [14].
• Inflammatory role of two venom components of yellow jackets (Vespula vulgaris): a mast cell degranulating peptide mastoparan and phospholipase A1 [1].
• However, a wide range of other polycationic agents, such as compound 48/80, the mast-cell-degranulating peptide from bee venom and polylysine also activated this cell type [15].

Other interactions of Mcdp

• It is further suggested that apamin, mast cell degranulating peptide and tertiapin form a single molecular class [16].

Analytical, diagnostic and therapeutic context of Mcdp

• Autoradiography has shown that a high enough dendrotoxin I concentration (30 nM) prevented binding of 125I MCD peptide to all brain structures where specific receptors had been identified [17].
• Bath application of the mast cell degranulating peptide (MCD) - a peptide isolated from bee venom- also produces in hippocampal slices LTP which is indistinguishable from that produced by a train of electrical stimulation (no change in postsynaptic cell properties, APV sensitive) [18].
• The precursors of mast cell degranulating peptide (MCDP) genes were amplified by RT-PCR from the total RNA of venom gland of two honeybee species, Apis mellifera ligustica, Apis cerana cerana, and three wasp species, Vespa magnifica, Vespa velutina nigrothorax and Polistes hebraeus, respectively [19].

References