Prepromelittin: Specific Cleavage of the Pre‐ and the Propeptide in Vitro

Kreil, Günther; Mollay, Christa; Kaschnitz, R.; Haiml, Liselotte; Vilas, Ulrike

doi:10.1111/j.1749-6632.1980.tb47262.x

Cited by 46 publications

(17 citation statements)

References 24 publications

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“…Insect venom DPPIV may function through the conversion of venom components into their active forms in the venom gland on the one hand and the enhancement or decrease of the chemotactic activity of immune cells after the insect sting on the other hand. The former may be confirmed by the hypothesis that promelittin is processed into its active form in a stepwise manner by enzymes of the DPPIV type in vitro (57). Given a relative protein content of 1% Api m 5 in native HBV and an amount of 50-140 mg protein delivered per honeybee sting (58), 0.5-1.5 mg DPPIV is injected into the skin per stinging event.…”

Section: Discussionmentioning

confidence: 81%

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

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Seismann

Bockisch

et al. 2010

The Journal of Immunology

112

107

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Section: Discussionmentioning

confidence: 81%

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Blank

Seismann

Bockisch

et al. 2010

The Journal of Immunology

112

107

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“…This extra piece is cleaved by signal peptidase (15) during translocation of the protein across the endoplasmic reticulum (ER) membrane. The nascent protein is core glycosylated in this organelle (9).…”

mentioning

confidence: 99%

A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulum.

Haguenauer‐Tsapis¹,

Nagy²,

Ryter³

1986

Mol. Cell. Biol.

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We studied ultrastructural localization of acid phosphatase in derepressed Saccharomyces cerevisiae cells transformed with a multicopy plasmid carrying either the wild-type PHOS gene or a PHOS gene deleted in the region overlapping the signal peptidase cleavage site. Wild-type enzyme was located in the cell wail, as was 50% of the modifled protein, which carried high-mannose-sugar chains. The remaining 50% of the protein was active and core glycosylated, and it accumulated in the endoplasmic reticulum cisternae. The signal peptide remained uncleaved in both forms. Cells expressing the modified protein exhibited an exaggerated endoplasmic reticulum with dilated lumen.

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“…Despite this not being reported for other ACTX peptides, post-translational pyroglutamate formation has been described with contulakin-G from the cone snail Conus geographus [7], several members of the charybdotoxin-like -KTx 1 subfamily of scorpion toxins (for a review see [44]) and dendrotoxin from the mamba Dendroaspis augusticeps [8]. C-terminal trimming has also been reported for a number of peptide toxin components, including the spider toxins Tx1, Tx3-2 and Pn3A from the Brazilian armed spider P. nigriventer [9,17], the bee toxin melittin [20], -CTX GVIA from C.…”

Section: R E V I E W C O P Ymentioning

confidence: 99%

Discovery of an MIT-like atracotoxin family: Spider venom peptides that share sequence homology but not pharmacological properties with AVIT family proteins

et al. 2005

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Abbreviations: ACh, acetylcholine; ACTX, atracotoxin; BCA, bicinchoninic acid; Bv8, 8kDa protein from the skin secretions of toads (Bombina variegata); CHO, Chinese hamster ovary; DDH, disulfidedirected -hairpin; EST, expressed sequence tag; FLIPR, fluorometric imaging plate reader; HEK, human embryonic kidney; ICK, inhibitory cystine-knot; MIT1, mamba intestinal toxin 1 from the venom of the black mamba snake Dendroaspis p. polylepis; PK, prokineticin (also known as endocrine-gland vascular endothelial growth factor or EG-VEGF); PKR, prokineticin receptor; RACE, rapid amplification of cDNA ends; TCEP, Tris(2-carboxyethyl)phosphine; TFA, trifluoroacetic acid. Atracinae), that appear to undergo N-and/or C-terminal post-translational modifications and conform to an ancestral protein fold. These peptides all show significant amino acid sequence homology to atracotoxin-Hvf17 (ACTX-Hvf17), a non-toxic peptide isolated from the venom of H. versuta, and a variety of AVIT family proteins including mamba intestinal toxin 1 (MIT1) and its mammalian and piscine orthologs prokineticin 1 (PK1) and prokineticin 2 (PK2). These AVIT family proteins target prokineticin receptors involved in the sensitization of nociceptors and gastrointestinal smooth muscle activation. Given their sequence homology to MIT1, we have named these spider venom peptides the MIT-like atracotoxin (ACTX) family. Using isolated rat stomach fundus or guinea-pig ileum organ bath preparations we have shown that the prototypical ACTX-Hvf17, at concentrations up to 1 GM, did not stimulate smooth muscle contractility, nor did it inhibit contractions induced by human PK1 (hPK1). KeywordsThe peptide also lacked activity on other isolated smooth muscle preparations including rat aorta.Furthermore, a FLIPR Ca 2+ flux assay using HEK293 cells expressing prokineticin receptors showed that ACTX-Hvf17 fails to activate or block hPK1 or hPK2 receptors. Therefore, while the MIT-like ACTX family appears to adopt the ancestral disulfide-directed -hairpin protein fold of MIT1, a motif believed to be shared by other AVIT family peptides, variations in the amino acid sequence and surface charge result in a loss of activity on prokineticin receptors.

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Prepromelittin: Specific Cleavage of the Pre‐ and the Propeptide in Vitro

Cited by 46 publications

References 24 publications

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

Identification, Recombinant Expression, and Characterization of the 100 kDa High Molecular Weight Hymenoptera Venom Allergens Api m 5 and Ves v 3

A deletion that includes the segment coding for the signal peptidase cleavage site delays release of Saccharomyces cerevisiae acid phosphatase from the endoplasmic reticulum.

Discovery of an MIT-like atracotoxin family: Spider venom peptides that share sequence homology but not pharmacological properties with AVIT family proteins

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