A new mast cell degranulating peptide homologous to mastoparan in the venom of Japanese hornet (Vespa xanthoptera).

Hirai, Yuko; Kuwada, Manabu; Yasuhara, Tadashi; Yoshida, Hisanobu; Nakajima, Terumi

doi:10.1248/cpb.27.1945

Cited by 83 publications

(37 citation statements)

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“…Mastoparans have been found in the venom of various solitary and social wasps [29]. The known mastoparans, which are more similar to the dominulins, are the so-called Mastoparan X from the venom of the vespine Vespa xanthoptera [30] (14 amino acids, having the same sequence of the first four residues from the N terminal of the dominulins), the peptide B from the venom of the Polistine wasp Protonectarina sylveirae [19] (14 amino acids, having the same sequence of the first four residues from the N terminal of the dominulins) and that from the venom of Parapolybia indica [31] (14 amino acids, having the same sequence of the first five residues from the N-terminal of the dominulins). However, the only mastoparans described so far from the venom of a Polistes (P. jadwigae from Japan), have only a sequence of four amino acids similar to that of Dominulin A (second to sixth from the N-terminal) and two more residues (in Positions 11 and 13) similar to those present in the sequence of Dominulin B [32] (see Table 3).…”

Section: Discussionmentioning

confidence: 99%

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Turillazzi

Mastrobuoni

Dani

et al. 2006

J. Am. Soc. Mass Spectrom.

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Two new antibacterial peptides, denominated as Dominulin A and B, have been found on the cuticle and in the venom of females of the social paper wasp Polistes dominulus. The amino acidic sequence of the two peptides, determined by mass spectrometry, is INWKKIAE VGGKIL SSL for Dominulin A (MW ϭ 1854 Da) and INWKKIAEIGKQVL SAL (MW ϭ 1909 Da) for Dominulin B. Their presence on the cuticle was confirmed using MALDI-TOF by means of micro-extractions and direct analyses on body parts. The presence in the venom and the primary structure of the dominulins suggest their classification in the mastoparans, a class of peptides found in the venom of other Aculeate hymenoptera. Their antimicrobial action against Gramϩ and GramϪ bacteria fits in the range of the best natural antimicrobial peptides. Dominulins can represent an important defense of the colony of Polistes dominulus against microbial pathogens. (J Am Soc Mass Spectrom 2006, 17, 376 -383)

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Section: Discussionmentioning

confidence: 99%

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Turillazzi

Mastrobuoni

Dani

et al. 2006

J. Am. Soc. Mass Spectrom.

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“…MP is a 14-amino acid amphipathic peptide obtained from wasp venom (sequence: INLKALAALAKKIL-NH 2 ), which induces mitochondrial permeability transition (PT) (Please see section 2. 4. regarding PT) [195][196][197]. After induction of PT, the permeability of the mitochondrial inner membrane increases and any components with a molecular weight 1500 Da leak from the mitochondrial matrix.…”

Section: 2 Mitochondrial Delivery Of Mastoparan Using a Transferrmentioning

confidence: 99%

Mitochondrial drug delivery systems for macromolecule and their therapeutic application to mitochondrial diseases

Yamada

Harashima

2008

Advanced Drug Delivery Reviews

229

148

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Key words: Mitochondria, mitochondrial drug delivery, mitochondrial macromolecule delivery, MITO-Porter, membrane fusion, multifunctional envelope-type nano device (MEND), mitochondrial protein therapy, mitochondrial gene therapy, mitochondrial protein import machinery, mitochondrial DNA. Yamada, Y., et al. AbstractMitochondrial dysfunction has been implicated in a variety of human disorders-the so-called mitochondrial diseases. Therefore, the organelle is a promising therapeutic drug target. In this review, we describe the key role of mitochondria in living cells, a number of mitochondrial drug delivery systems and mitochondria-targeted therapeutic strategies. In particular, we discuss mitochondrial delivery of macromolecules, such as proteins and nucleic acids. The discussion of protein delivery is limited primarily to the mitochondrial import machinery. In the section on mitochondrial gene delivery and therapy, we discuss mitochondrial diseases caused by mutations in mitochondrial DNA, several gene delivery strategies and approaches to mitochondrial gene therapy. This review also summarizes our current efforts regarding liposome-based delivery system including use of a multifunctional envelope-type nano device (MEND) and mitochondrial liposome-based delivery as anti-cancer therapies. Furthermore, we introduce the novel MITO-Porter-a liposome-based mitochondrial delivery system that functions using a membrane-fusion mechanism.Yamada, Y., et al. 3

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“…Melittin is also a potent inhibitor of the H ϩ /K ϩ -ATPase and the Na ϩ /K ϩ -ATPase (7-10). Mastoparan (MP) is an amphiphilic tetradecapeptide isolated from wasp venom (11). It is known to possess a variety of biological activities including mast cell degranulation, mobilization of Ca 2ϩ from cerebellar microsomes and sarcoplasmic reticulum, activation of the ryanodine receptor and modulation of various enzymes, for example the Na ϩ /K ϩ -ATPase of rat brain (12)(13)(14).…”

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confidence: 99%

The Mechanism of Inhibition of the Ca2+-ATPase by Mastoparan

Longland

Mezna

Michelangeli

1999

Journal of Biological Chemistry

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A new mast cell degranulating peptide homologous to mastoparan in the venom of Japanese hornet (Vespa xanthoptera).

Cited by 83 publications

References 0 publications

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Dominulin A and B: Two new antibacterial peptides identified on the cuticle and in the venom of the social paper waspPolistes dominulususing MALDI-TOF, MALDI-TOF/TOF, and ESI-ion trap

Mitochondrial drug delivery systems for macromolecule and their therapeutic application to mitochondrial diseases

The Mechanism of Inhibition of the Ca2+-ATPase by Mastoparan

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