Immunolocalization of venom metalloproteases in venom glands of adult and of newborn snakes of Bothrops jararaca

Carneiro, Sylvia Mendes; Assakura, Marina T.; Barrence, Fernanda A.; Cardoso, Silvia Regina Travaglia; Camargo, Antonio Carlos de Martins; Sesso, Antônio

doi:10.1016/s004081660200068x

Cited by 11 publications

(5 citation statements)

References 47 publications

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“…However, in the secretory vesicles, both sera revealed a few spots 7 days after stimulus of the venom gland and the number of these spots increased in quiescent cells, particularly in tissues treated with sera against the mature protein. Accumulation of mature SVMPs in secretory vesicles during the venom production cycle has already been shown, and our results are consistent with previous data. It is important to note that immunofluorescence and immunoelectron microscopy reactions with anti-Jar were always more intense than with anti-PD-Jar.…”

Section: Discussionsupporting

confidence: 94%

“…Indirect immunolabeling was accomplished using protein G-colloidal gold 10 nm (Amersham) after ethanol dehydration. Immunolabeling was carried out on silver sections on nickel grids, according to Carneiro and colleagues 44 using rabbit-anti-PD-Jar, rabbit-anti-Jar, or normal rabbit sera. Grids were washed with blocking solution and incubated with protein G-gold 10 nm, washed again with distilled water, stained with uranyl acetate and lead citrate, and viewed with an LEO 906E transmission electron microscope (Zeiss, Germany).…”

Section: Immunoelectron Microscopymentioning

confidence: 99%

See 1 more Smart Citation

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

Portes-Junior

Yamanouye²,

Carneiro³

et al. 2014

J. Proteome Res.

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Snake venom metalloproteinases (SVMPs) are zinc-dependent enzymes responsible for most symptoms of human envenoming. Like matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase (ADAM) proteins, SVMPs are synthesized as zymogens, and enzyme activation is regulated by hydrolysis of their prodomain, but the processing of SVMPs is still unclear. In this study, we attempted to identify the presence of prodomain in different compartments of snake venom glands as zymogens or in the free form to elucidate some mechanism involved in SVMP activation. Using antibodies obtained by immunization with a recombinant prodomain, bands of zymogen molecular mass and prodomain peptides were detected mostly in gland extracts all along the venom production cycle and in the venom collected from the lumen at the peak of venom production. Prodomain was detected in secretory cells mostly in the secretory vesicles near the Golgi. We hypothesize that the processing of SVMPs starts within secretory vesicles and continues in the lumen of the venom gland just after enzyme secretion and involves different steps compared to ADAMs and MMPs but can be used as a model for studying the relevance of peptides resulting from prodomain processing and degradation for controlling the activity of metalloproteinases.

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Section: Discussionsupporting

confidence: 94%

Section: Immunoelectron Microscopymentioning

confidence: 99%

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

Portes-Junior

Yamanouye²,

Carneiro³

et al. 2014

J. Proteome Res.

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“…The protein re-synthesis triggered by venom expulsion peaks between days 3–7 of the cycle of venom replenishment [ 24 ]. Protein synthesis is thought to be maintained at a high rate until completion, and studies have suggested that secretory cells can remain active for up to 30 to 60 days post venom extraction, indicating that the complete cycle of venom synthesis may be longer than previously expected [ 25 ]. After synthesis, the venom is stored in the basal lumen and ductules of the venom gland and is therefore available when needed [ 17 ].…”

Section: Snake Venom Apparatus and Venom Productionmentioning

confidence: 99%

Current Knowledge on Snake Dry Bites

Pucca

Knudsen

Oliveira

et al. 2020

Toxins

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Snake ‘dry bites’ are characterized by the absence of venom being injected into the victim during a snakebite incident. The dry bite mechanism and diagnosis are quite complex, and the lack of envenoming symptoms in these cases may be misinterpreted as a miraculous treatment or as proof that the bite from the perpetrating snake species is rather harmless. The circumstances of dry bites and their clinical diagnosis are not well-explored in the literature, which may lead to ambiguity amongst treating personnel about whether antivenom is indicated or not. Here, the epidemiology and recorded history of dry bites are reviewed, and the clinical knowledge on the dry bite phenomenon is presented and discussed. Finally, this review proposes a diagnostic and therapeutic protocol to assist medical care after snake dry bites, aiming to improve patient outcomes.

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“…Electron microscopy in combination with immunohistochemistry techniques, namely immuno-electron-microscopy, has been widely used in clinical laboratories, as a fast, sensitive, and cost-effective tool for trace analysis. In particular, such techniques are useful in ultrastructural localization and receptor identification (21)(22)(23)(24)(25). 1β,2β-Diacetyloxy-8r,13-diisobutanoyloxy-6r-succinoyl-9benzoyloxy-4r-hydroxy-β-dihydroagarofuran.…”

Section: Introductionmentioning

confidence: 99%

Preparation of Monoclonal Antibody against Celangulin V and Immunolocalization of Receptor in the Oriental Armyworm, Mythimna separata Walker (Lepidoptera: Noctuidae)

Zhāng

Xue

et al. 2006

J. Agric. Food Chem.

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The botanical insecticide celangulin V (CA-V) is an insect digestive poison acting on midgut tissue of the target insect larvae. With the aim of localizing the receptor enacted by CA-V, monoclonal antibodies (MAbs) specific to the compound were developed. A hapten was synthesized by introducing a succinoyl into the CA-V structure and conjugated with three carrier proteins. From mice immunized with one conjugate, three MAbs were obtained with a potential capacity of detecting protein-bound residue forms of CA-V in the biological tissues. The oriental armyworm larvae ingested CA-V were examined by the technique of immuno-electron-microscopy (IEM) using the anti-CA-V MAb as the primary antibody and goat anti-mouse/IgG labeled with colloidal gold as the secondary antibody. Electron micrographs of the armyworm midgut tissues showed that the CA-V was associated with the midgut epithelia of the insects. These results demonstrated the existence of a receptor enacted by CA-V on the midgut cells of the oriental armyworm larvae.

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Immunolocalization of venom metalloproteases in venom glands of adult and of newborn snakes of Bothrops jararaca

Cited by 11 publications

References 47 publications

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

Unraveling the Processing and Activation of Snake Venom Metalloproteinases

Current Knowledge on Snake Dry Bites

Preparation of Monoclonal Antibody against Celangulin V and Immunolocalization of Receptor in the Oriental Armyworm, Mythimna separata Walker (Lepidoptera: Noctuidae)

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