Amino acid sequence of bumblebee MCD peptide: A new mast cell degranulating peptide from the venom of the bumblebee Megabombus pennsylvanicus

Argiolas, Antonio; Herring, Patricia A.; Pisano, John J.

doi:10.1016/0196-9781(85)90410-3

Cited by 42 publications

(44 citation statements)

References 13 publications

(5 reference statements)

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“…3). Maximal histamine release occurred at a concentration of 2.5 M, and the concentration required to elicit release of 25% of the total cellular histamine content (EC 25 ) was 330 Ϯ 8 nM. The molar potency of the synthetic analog was comparable with that of natural pLR, except that the maximal release obtained with the natural pLR was 80% compared with 67.9 Ϯ 2.4% for the synthetic peptide (data not shown).…”

Section: Fig 5 Calcium and Energy Dependence Studies Of Peptide Leumentioning

confidence: 74%

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Peptide Leucine Arginine, a Potent Immunomodulatory Peptide Isolated and Structurally Characterized from the Skin of the Northern Leopard Frog, Rana pipiens

Salmon

Cross

Irvine

et al. 2001

Journal of Biological Chemistry

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On the basis of histamine release from rat peritoneal mast cells, an octadecapeptide was isolated from the skin extract of the Northern Leopard frog (Rana pipiens). This peptide was purified to homogeneity using reversed-phase high performance liquid chromatography and found to have the following primary structure by Edman degradation and pyridylethylation: LVRGC-WTKSYPPKPCFVR, in which Cys 5 and Cys 15 are disulfide bridged. The peptide was named peptide leucinearginine (pLR), reflecting the N-and C-terminal residues. Molecular modeling predicted that pLR possessed a rigid tertiary loop structure with flexible end regions. pLR was synthesized and elicited rapid, noncytolytic histamine release that had a 2-fold greater potency when compared with one of the most active histamine-liberating peptides, namely melittin. pLR was able to permeabilize negatively charged unilamellar lipid vesicles but not neutral vesicles, a finding that was consistent with its nonhemolytic action. pLR inhibited the early development of granulocyte macrophage colonies from bone marrow stem cells but did not induce apoptosis of the end stage granulocytes, i.e. mature neutrophils. pLR therefore displays biological activity with both granulopoietic progenitor cells and mast cells and thus represents a novel bioactive peptide from frog skin.Studies on the array of biologically active substances present in amphibian skin have been reported in the scientific literature for almost 40 years (1). In particular, skin is a rich source of bioactive peptides, many of which are present in copious amounts (mg/g wet weight skin) (2). Many peptides occur at concentrations that are several orders of magnitude higher than the circulating levels in the frog, indicating that a major source of biosynthesis is in the skin (3). These peptides are putative components in the defense of the frog against predation or invading microorganisms (1).Several peptides have been isolated from the skins of ranid frog species, which have structural analogs in mammalian neuroendocrine systems. Bradykinin and related family members have been identified in several Rana species (4 -8) and others include the bombesin-like peptide, ranatensin (9), thyrotropin-releasing hormone (10, 11), caerulein (12), xenopsinrelated peptide, margaratensin (13), and the tachykinin ranamargarin (14). The hemolytic/chemotactic ranid frog peptides (7, 12) and the family of temporin peptides (15) demonstrate structural similarity to the mast cell-activating and phospholipase A2-facilitating peptide, crabrolin, from the venom of the wasp, Vespa crabro (16).Many peptides activate rat peritoneal mast cells; thus, histamine release can be utilized as a screen for putative bioactive peptides. There are several frog skin peptides that have been identified in this manner, namely, peptide XO-4 from Kassina maculata (17), granuliberin R from Rana rugosa (18), and the pipinins from Rana pipiens (19). A number of peptides have also been isolated from the venoms of hornets, wasps, and bees on the basis of histam...

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Section: Fig 5 Calcium and Energy Dependence Studies Of Peptide Leumentioning

confidence: 74%

“…This peptide shows no known sequence similarity with other peptides, which have also been isolated on the basis of mast cell activation or with other histamine-releasing peptides, such as melittin and magainin-2-amide (Table I). The EC 25 of pLR (330 Ϯ 8 nM; Fig. 3) is 2-fold greater than that of melittin (600 Ϯ 2 nM; FIG.…”

Section: Discussionmentioning

confidence: 99%

Peptide Leucine Arginine, a Potent Immunomodulatory Peptide Isolated and Structurally Characterized from the Skin of the Northern Leopard Frog, Rana pipiens

Salmon

Cross

Irvine

et al. 2001

Journal of Biological Chemistry

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“…In addition to the effects just described, melittin shows an insecticidal activity toward D. melanogaster, acts antimicrobially to Gram-positive and Gram-negative bacteria and to fungi in the micromolar range, and is nearly as active as cytolytic peptides from spider venoms [64,82,106,107]. Bombolitins, cytolytic peptides isolated from the venom of the bumblebee Megabombus pennsylvanicus [108], are five structurally related heptadecapeptides possessing one to three cationic residues and an amidated C-terminus (table 2, 3). They constitute about 25 % of the dry weight venom.…”

Section: Bees and Bumblebeesmentioning

confidence: 97%

Antimicrobial and cytolytic peptides of venomous arthropods

Kuhn‐Nentwig

2003

Cellular and Molecular Life Sciences (CMLS)

186

131

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As a response to invading microorganisms, the innate immune system of arthropods has evolved a complex arrangement of constitutive and inducible antimicrobial peptides that immediately destroy a large variety of pathogens. At the same time, venomous arthropods have developed an additional offensive system in their venom glands to subdue their prey items. In this complex venom system, several enzymes, low-molecular-mass compounds, neurotoxins, antimicrobial and cytolytic peptides interact together, resulting in extremely rapid immobilization and/or killing of prey or aggressors. This review provides an overview of antimicrobial peptides identified in the hemolymph of venomous arthropods, and especially of cytolytic peptides in their venom. For these peptides a dual role is proposed: acting as antimicrobials as well as increasing the potency of the venom by influencing excitable cells.

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“…Such peptides constitute a major fraction of the venoms of bees, bumblebees, wasps, and ants [12,[21][22][23][24][25][26].…”

Section: Introductionmentioning

confidence: 99%

Latarcins: versatile spider venom peptides

Dubovskii

Vassilevski

Kozlov

et al. 2015

Cell. Mol. Life Sci.

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Arthropod venoms feature the presence of cytolytic peptides believed to act synergetically with neurotoxins to paralyze prey or deter aggressors. Many of them are linear, i.e., lack disulfide bonds. When isolated from the venom, or obtained by other means, these peptides exhibit common properties. They are cationic; being mostly disordered in aqueous solution, assume amphiphilic α-helical structure in contact with lipid membranes; and exhibit general cytotoxicity, including antifungal, antimicrobial, hemolytic, and anticancer activities. To suit the pharmacological needs, the activity spectrum of these peptides should be modified by rational engineering. As an example, we provide a detailed review on latarcins (Ltc), linear cytolytic peptides from Lachesana tarabaevi spider venom. Diverse experimental and computational techniques were used to investigate the spatial structure of Ltc in membrane-mimicking environments and their effects on model lipid bilayers. The antibacterial activity of Ltc was studied against a panel of Gram-negative and Gram-positive bacteria. In addition, the action of Ltc on erythrocytes and cancer cells was investigated in detail with confocal laser scanning microscopy. In the present review, we give a critical account of the progress in the research of Ltc. We explore the relationship between Ltc structure and their biological activity and derive molecular characteristics, which can be used for optimization of other linear peptides. Current applications of Ltc and prospective use of similar membrane-active peptides are outlined.

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Amino acid sequence of bumblebee MCD peptide: A new mast cell degranulating peptide from the venom of the bumblebee Megabombus pennsylvanicus

Cited by 42 publications

References 13 publications

Peptide Leucine Arginine, a Potent Immunomodulatory Peptide Isolated and Structurally Characterized from the Skin of the Northern Leopard Frog, Rana pipiens

Peptide Leucine Arginine, a Potent Immunomodulatory Peptide Isolated and Structurally Characterized from the Skin of the Northern Leopard Frog, Rana pipiens

Antimicrobial and cytolytic peptides of venomous arthropods

Latarcins: versatile spider venom peptides

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