Defibrinogenation with Thrombin-Like Snake Venom Enzymes

Stocker, Kurt

doi:10.1007/978-3-642-66863-0_13

Cited by 33 publications

(21 citation statements)

References 111 publications

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“…24 BX is used clinically as a defibrinogenic agent for humans. 15,16 BX at a dose of 60 U ⅐ kg Ϫ1 ⅐ d Ϫ1 in rats decreases fibrinogen concentration and lowers the whole-blood viscosity without any influences on inflammatory events. 16,25 A dose of 60 U/kg BX significantly reduced the fibrinogen concentration in rats for 24 hours (Figure 6).…”

Section: Discussionmentioning

confidence: 95%

Prevention of Rat Cerebral Aneurysm Formation by Inhibition of Nitric Oxide Synthase

et al. 2000

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Background-Cerebral saccular aneurysm is a major cause of subarachnoid hemorrhage, one of the cerebrovascular diseases with the highest mortality. The mechanisms underlying the development of aneurysms, however, still remain unclear. We have made a series of reports on an animal model of experimentally induced cerebral aneurysms that resemble human cerebral aneurysms in their location and morphology, suggesting that the arterial wall degeneration associated with aneurysm formation develops near the apex of arterial bifurcation as a result of an increase in wall shear stress. Using the animal model and human specimens, we examined the role of nitric oxide (NO) in the degenerative changes and cerebral aneurysm formation. Methods and Results-Inducible NO synthase (iNOS) was immunohistochemically located at the orifice of human and rat aneurysms. Nitrotyrosine distribution was also seen in the human aneurysm. Although no iNOS immunostaining was found in normal arteries, iNOS immunoreactivity was observed in parallel with the development of early aneurysmal changes in rats. In contrast, during the early development of aneurysm, endothelial NOS immunostaining in the endothelium was weakened compared with that in the control arteries. An NOS inhibitor, aminoguanidine, attenuated both early aneurysmal changes and the incidence of induced aneurysms. A defibrinogenic agent, batroxobin, which may diminish shear stress by reduction of blood viscosity, prevented iNOS induction as well as early aneurysmal changes. Conclusions-The evidence suggests that NO, particularly that derived from iNOS, is a key requirement for the development of cerebral aneurysm. The iNOS induction may be caused by an increase in shear stress near the apex.

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Section: Discussionmentioning

confidence: 95%

Prevention of Rat Cerebral Aneurysm Formation by Inhibition of Nitric Oxide Synthase

et al. 2000

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“…The following snake venoms have been described to contain PC activators [12][13][14][15][16][17] First results on the isolation of thrombomodulin-independent and fast-activating PC activator from A. contortrix contortrix (southern copperhead snake), and related PC-activating properties of enzymes from venom of Agkistrodon subspecies and in venom of A. piscivorus (eastern cottonmouth snake), Agkistrodon bilineatus (tropical moccasin snake), B. moojeni, B. pradoi (Prado's pit viper), Vipera lebetina (desert adder) and Cerastes cerastes (Egyptian sand viper) were presented in 1985 at the Symposium on Animal Venoms and Hemostasis in San Diego, Calif. [18].…”

Section: Pc Activatorsmentioning

confidence: 99%

Protein C Activators from Snake Venoms and Their Diagnostic Use

Gempeler-Messina¹,

Volz²,

Bühler³

et al. 2001

Pathophysiol Haemos Thromb

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Proteinases converting the zymogen protein C (PC) of vertebrates into activated PC have been detected in several snake venoms. Most PC activators have been purified from venom of snake species belonging to the genera of the Agkistrodon complex. Unlike the physiological, thrombin-catalyzed PC activation reaction which requires thrombomodulin as a cofactor, most snake venom activators directly convert the zymogen PC into the catalytically active form which can easily be determined by means of coagulation or chromogenic substrate techniques. Due to this feature, the fast-acting PC activator Protac^®from Agkistrodon contortrix contortrix (southern copperhead snake) venom has found a broad application in diagnostic practice for the determination of disorders in the PC pathway. Recently, screening assays for the PC pathway have been introduced, based on the observation that the PC pathway is probably the most important physiological barrier against thrombosis.

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“…This immunologic resistance may be overcome by replacing batroxobin by ancrod in the therapy, which demonstrates that these two enzymes are serologically not cross-reacting [2]. Therefore, purified batroxobin of B. moojeni is currently used for therapeutic defibrinogenation in patients suffering from thrombotic diseases.…”

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confidence: 99%

Carbohydrate Structure Analysis of Batroxobin, a Thrombin-Like Serine Protease from Bothrops moojeni Venom

Lochnit¹,

Geyer²

1995

Eur J Biochem

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The carbohydrate side chains of batroxobin were liberated from tryptic glycopeptides by treatment with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F, pyridylaminated and separated by two-dimensional HPLC. Neutral oligosaccharide derivatives obtained after desialylation were characterized by methylation analysis, liquid secondary-ion mass spectrometry, digestion with exoglycosidases and endoglycosidases and, in part, by acetolysis, whereas sialic acid constituents were identified by reverse-phase HPLC after conjugation with 1,2-diamino-4,5-methylene-dioxybenzene. The overall glycosylation status of the protein was studied by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). The results revealed that batroxobin is heterogeneously glycosylated carrying predominantly diantennary, partially incomplete complex-type glycans in addition to hybrid-type species. Most glycans were core-fucosylated at C6 of the innermost GlcNAc. As a characteristic feature, galactose was completely replaced by GalNAc beta 4-substituents in complex-type antennae, the GlcNAc-residues of which were, in part, fucosylated at C3. Furthermore, evidence was obtained that suggested the presence of a novel type of glycoprotein-N-glycan comprising two GalNAc beta 4GlcNAc beta 4GlcNAc beta 2Man-antennae. Sialic acid residues represented a mixture of N-acetylneuraminic acid (Neu5Ac) and N-acetyl-4-O-acetylneuraminic acid (Neu4,5Ac2), which were exclusively linked to C3 of subterminal GalNAc. A precise assignment of these sialic acid derivatives to distinct oligosaccharide structures or antennae, however, was not carried out. Finally, MALDI-TOF-MS demonstrated that both potential N-glycosylation sites of batroxobin are substituted by carbohydrate chains. In conclusion, our studies revealed that this snake venom glycoprotein is characterized by a unique oligosaccharide pattern partly comprising novel structural elements.

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Defibrinogenation with Thrombin-Like Snake Venom Enzymes

Cited by 33 publications

References 111 publications

Prevention of Rat Cerebral Aneurysm Formation by Inhibition of Nitric Oxide Synthase

Prevention of Rat Cerebral Aneurysm Formation by Inhibition of Nitric Oxide Synthase

Protein C Activators from Snake Venoms and Their Diagnostic Use

Carbohydrate Structure Analysis of Batroxobin, a Thrombin-Like Serine Protease from Bothrops moojeni Venom

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