Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “SCORPIONS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 217 records · Page 12Linked to original sources
PubMed2000

Purification, cDNA cloning and function assessment of BmK abT, a unique component from the Old World scorpion species.

A new neurotoxic component named BmK abT was purified from the venom of Chinese scorpion Buthus martensi Karsch. The molecular weight of BmK abT was determined to be 7212 Da on a mass spectrum. The minimum lethal dose of BmK abT was tested to be about 1.5 microg per mouse by intracerebroventricular injection, and the dose induced significant paralysis effect on cockroach was about 5 microg by i.p. injection. The partial amino acid sequence indicated that it was a distinctive polypeptide in the scorpion neurotoxin family. Thereafter, the whole amino acid sequence of mature BmK abT was deduced from cDNA sequence by 5'- and 3'-rapid amplification of cDNA ends. Finally, it was defined to be composed of 63 residues with amidation at the C-terminal residue. By sequence comparison, BmK abT was found to be most similar to Ts VII, a beta-toxin from the New World scorpion. The patch-clamp recording on DRG neurons, unexpectedly, showed this toxin could prolong the action potential and increase the amplitude of the peak Na+ currents, which are the typical characters of alpha-toxin. These results suggested that BmK abT was a new toxic component found in the Old World scorpion species structurally similar to beta-toxins, but functionally similar to alpha-toxins.

Action Potentials↗
PubMed2002

Scorpion toxins from Tityus cambridgei that affect Na(+)-channels.

By means of high performance liquid chromatography (HPLC) the soluble venom of the Amazonian scorpion Tityus cambridgei was fractionated into over 50 different components. Four toxic and/or lethal peptides to mice were obtained in pure form and sequenced. Mass spectrometry analysis showed molecular weights of 7310, 7151, 7259 and 7405, respectively, for toxins Tc48a, Tc49a, Tc54 and Tc49b. The N-terminal amino acid sequence was obtained for the three first toxins mentioned, whereas the full primary structure was determined for Tc49b. It contains 64 amino acid residues, closely packed by four disulfide bridges. Sequence comparison analysis showed similarities around 50% with other toxins from scorpions of the genus Tityus of Brazil. It is lethal to mice at doses of 20 microg per 20 g mouse. The toxin was shown to affect the Na(+)-currents permeability of rat cerebellum granular cells in culture. Almost a complete elimination of current was observed with 100 nM toxin concentration. This effect was partially reversible. Furthermore, this toxin does not modify the function of the Shaker B K(+)-channels expressed on Sf9 cells, nor does it modify the Na(+)-channel function in a similar manner as those reported for the alpha-scorpion toxins purified from other scorpions.

Amino Acid Sequence↗
PubMed2002

Intraspecific variability and pharmacokinetic characteristics of Androctonus mauretanicus mauretanicus scorpion venom.

We evaluated the degree of venom toxicity and protein content of several specimens of Androctonus mauretanicus mauretanicus. The quantity of protein of individual venom obtained after manual extraction from 31 different scorpions varied from a minimum of 0.15 mg to a maximum of 1.53 mg. We determined the venom toxicity, in mice, by estimating the number of LD(50)s of 20 scorpions chosen randomly among the 31 scorpions. It ranged from less than 40 LD(50)s to a maximum of 272 LD(50)s. The correlation between protein content and venom lethality is not systematic. We also determined the pharmacokinetics of the venom and its specific anti-venom in rabbits to compare their distribution and elimination properties. After a subcutaneous injection, high concentrations of venom were measured by ELISA in the vascular space rapidly after the injection (T(max) = 0.5 h). The terminal half-life was 2.8 h, close the one determined after intravenous injection (t(1/2beta) = 3.2 h). The total volume of distribution (Vd(ss) or Vd(beta)) was between 317 and 380 ml/kg. The total body clearance was 82 ml/kg/h. For scorpion anti-venom, the terminal half-life, after intravenous injection, was 20.25 h; the volume of distribution was 83 ml/kg and the total body clearance was 3 ml/kg/h. After intramuscular administration, T(max) was reached at 36 h. The results show that venom lethality varies from specimen to specimen and that pharmacokinetic parameters of venom and anti-venom are totally different. This must be taken under consideration in anti-venom production (anti-venom titre) as well as in therapeutic protocols (dose, injection route) to improve serotherapy.

Animals↗
PubMed1998

Maurotoxin, a four disulfide bridges scorpion toxin acting on K+ channels.

Maurotoxin, a toxin from the venom of the Tunisian chactoid scorpion Scorpio maurus, has been purified to homogeneity by gel filtration/reversed-phase HPLC, and characterized. It is a basic and C-terminal amidated 34-residue polypeptide cross-linked by four disulfide bridges. From Edman sequencing results, only six different pairings between the first six half-cystines were retained whereas a disulfide bridge was predicted between the two half-cystines in positions 31 and 34. Modelling based on the structure of charybdotoxin favored two different pairings, one of which possessed two disulfides in common with the general motif of scorpion toxins. The solid-phase technique was used to obtain synthetic maurotoxin, sMTX. The half-cystine pairings of sMTX were determined by enzymatic cleavage and were found to be Cys3 Cys24, Cys9-Cys29, Cys13-Cys19, and Cys31-34, in agreement with experimental data obtained with natural maurotoxin. Both natural and synthetic maurotoxins were lethal to mice following intracerebroventricular injection (LD50, 80 ng/mouse). They blocked the Kv1.1, Kv1.2, and Kv1.3 channels expressed in Xenopus oocytes with almost identical half-effects (IC50) in the range of 40, 0.8 and 150 nM, respectively. They also competed with 125I-apamin (SKca channel blocker) and 125I-kaliotoxin (Kv channel blocker) for binding to rat brain synaptosomes with IC50 of about 5 and 0.03 nM. As the natural and synthetic maurotoxins exhibit indistinguishable physicochemical and pharmacological properties, they are likely to adopt the same half-cystine pairing pattern which is unique among known scorpion toxins. However, this disulfide organization is different from those reported for Pandinus imperator and Heterometrus spinnifer toxins 1 (Pi1 and HsTx1), two novel four-disulfide bridged K+ channel-acting scorpion toxin sharing about 50-70% sequence identity with maurotoxin.

Amino Acid Sequence↗
PubMed1993

Scorpion envenomation in eastern Saudi Arabia.

STUDY OBJECTIVE: To prospectively collect data on the initial presentation of victims of scorpion envenomation during the deployment of US forces to Saudi Arabia in support of Operation Desert Shield. DESIGN: A four-month prospective analysis of the circumstances, initial clinical signs and symptoms, treatment rendered, and subsequent clinical course of patients suffering scorpion envenomation. Data were analyzed using descriptive statistics. Scorpions were identified from physical remains. SETTING: Open desert in eastern Saudi Arabia 250 miles northeast of Riyadh. Ten battalion aid stations supporting a US armored cavalry division provided first-echelon medical care to 7,000 soldiers. TYPE OF PARTICIPANTS: The 40 male and three female patients were American military personnel between 19 and 33 years old. INTERVENTION: The constraints of military action precluded an interventional protocol. Each medical officer rendered appropriate medical care according to experience. MEASUREMENT AND MAIN RESULTS: During 118 days of encampment, 57 cases were reported, with 43 containing sufficient data for inclusion in the study. Thirty-six (63%) cases occurred during six weeks of initial fortification activity in open desert. Thirty-five victims (79%) presented for medical care within one hour after envenomation. The most common local symptoms and signs were pain (100%) and erythema (63%). The prevalent systemic symptom was apprehension (44%), with tachycardia (72%) and hypertension (58%) the prevalent systemic signs. With one exception, neurologic and cardiorespiratory complications were transient and responded well to fluid support and low doses of beta-sympathomimetics, parasympathetic antagonists, H1 blockers, and analgesics. CONCLUSION: The local and systemic response by victims in this study are consistent with previously documented cases of scorpion envenomation. In adult patients without serious prior adverse medical conditions, intervention is best limited to supportive measures.

Adrenergic beta-Agonists↗
PubMed2005

Gastrointestinal manifestations in severe scorpion envenomation.

OBJECTIVES: To evaluate the type and incidence of gastrointestinal manifestations secondary to scorpion envenomation and their prognostic significance. PATIENTS AND METHODS: All patients admitted to our ICU for scorpion envenomation were included in this retrospective chart review of a 13-year period (1990 - 2002). RESULTS: During the study period, 951 patients were admitted for scorpion envenomation and 72 (7.6%) died. Ages ranged from 0.5 to 90 years with a mean of 14.7 +/- 17.4 years. Gastrointestinal symptoms were present in 700 patients (73.6%): nausea in 24 (2.5%), vomiting in 687 (72.2%) and diarrhea in 41 patients (4.3%). At univariate analysis, the presence of diarrhea was associated with a fatal outcome (P < 0.05). Diarrhea was also correlated with other indicators of severe envenomation and poor prognosis: respiratory failure (P = 0.01), neurological failure (P < 0.0001), liver failure (P < 0.0001) and low blood pressure requiring catecholamine support (P = 0.02). The multivariate analysis showed that young age (age less than 5 years), fever > 38.5 degrees C, neurological failure and pulmonary edema were independent factors of severity. Digestive disorders were more frequent in children and in this subgroup diarrhea appeared to be associated with poor outcome. In a subset of patients for whom data were available, fatal cases demonstrated significantly higher liver enzymes levels on admission. CONCLUSION: In Tunisia, gastrointestinal symptoms are often observed in severe scorpion envenomations, especially in young patients. In children, diarrhea and elevated liver enzymes are associated with poor prognosis.

Adolescent↗
PubMed1998

Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom.

The primary structures of four low molecular mass peptides (Bs 6, 8, 10 and 14) from scorpion Buthus sindicus were elucidated via combination of Edman degradation and matrix-assisted laser desorption ionization mass spectrometry. Bs 8 and 14 are cysteine-rich, thermostable peptides composed of 35-36 residues with molecular weights of 3.7 and 3.4 kDa, respectively. These peptides show close sequence homologies (55-78%) with other scorpion chlorotoxin-like short-chain neurotoxins (SCNs) containing four intramolecular disulfide bridges. Despite the sequence variation between these two peptides (37% heterogeneity) their general structural organization is very similar as shown by their clearly related circular dichroism spectra. Furthermore, Bs6 is a minor component, composed of 38 residues (4.1 kDa) containing six half-cystine residues and having close sequence identities (40-80%) with charybdotoxin-like SCNs containing three disulfide bridges. The non-cysteinic, bacic and thermolabile Bs10 is composed of 34 amino acid residues (3.7 kDa), and belongs to a new class of peptides, with no sequence resemblance to any other so far reported sequence isolated from scorpions. Surprisingly, Bs10 shows some limited sequence analogy with oocyte zinc finger proteins. Results of these studies are discussed with respect to their structural similarities within the scorpion LCNs, SCNs and other biologically active peptides.

Animals↗
PubMed2001

Solution structure of an insect-specific neurotoxin from the New World scorpion Centruroides sculpturatus Ewing.

We report the high-resolution solution structure of the 6.3 kDa neurotoxic protein CsE-v5 from the scorpion Centruroides sculpturatus Ewing (CsE, range southwestern U.S.). This protein is the second example of an Old World-like neurotoxin isolated from the venom of this New World scorpion. However, unlike CsE-V, which is the first Old World-like toxin isolated and shows both anti-insect and anti-mammal activity, CsE-v5 shows high specificity for insect sodium channels. Sequence-specific proton NMR assignments and distance and angle constraints were obtained from 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed to produce a final family of 20 structures without constraint violations, along with an energy-minimized average structure. The protein structure is well-defined (0.66 and 0.97 D rmsd for backbone and all heavy atoms, respectively) with a compact hydrophobic core and several extending loops. A large hydrophobic patch, containing four aromatic rings and other aliphatic residues, makes up a large area of one side of the protein. CsE-v5 shows secondary structural features characteristic of long-chain scorpion toxins: a two and a half-turn alpha-helix, a three-strand antiparallel beta-sheet, and four beta-turns. Among the proteins studied to date from the CsE venom, CsE-v5 is the most compact protein with nearly 50% of the amide protons having long exchange lifetimes, but CsE-v5 is unusual in that it has loop structures similar to both Old and New World toxins. Further, it also lacks prolines in its C-terminal 14 residues. It shows some important differences with respect to CsE-V not only in its primary sequence, but also in its electrostatic potential surface, especially around areas in register with residues 8, 9, 17, 18, 32, 43, and 57. The loss of anti-mammal activity in CsE-v5 and the differences in its anti-insect activity compared to that of other proteins such as CsE-V, v1, and v3 from this New World scorpion may be related to residue variations at these locations.

Amino Acid Sequence↗
PubMed2002

Roles of disulfide bridges in scorpion toxin BmK M1 analyzed by mutagenesis.

The unique fold of scorpion toxins is a natural scaffold for protein engineering, in which multiple disulfide bonds are crucial structural elements. To understand the respective roles of these disulfide bridges, a mutagenesis analysis for the four disulfide bonds, 12-63, 16-36, 22-46 and 26-48, of a representative toxin BmK M1 from the scorpion Buthus martensii Karsch was carried out. All cysteines were replaced by serine with double mutations. The recombinant mutants were expressed in the Saccharomyces cerevisiae S-78 system. Toxic activities of the expressed mutants were tested on ICR mice in vivo and on neuronal Na+ channels (rNav1.2) by electrophysiological analysis. Recombinant variants M1 (C22S,C46S) and M1 (C26S,C48S) were not expressed at all; M1 (C16S,C36S) could be expressed at trace levels but was extremely unstable. Variant M1 (C12S,C63S) could be expressed in an amount comparable with that of unmodified rBmK M1, but had no detectable bioactivities. The results indicated that among the four disulfide bonds for long-chain scorpion toxins, loss of either bridge C22-C46 or C26-C48 is fatal for the general folding of the molecule. Bridge C16-C36 mainly contributes to the global stability of the folded scaffold, and bridge C12-C63 plays an essential role in the functional performance of scorpion toxins.

Amino Acid Sequence↗
PubMed2001

Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.

Two novel antimicrobial peptides have been identified and characterized from venom of the African scorpion Pandinus imperator. The peptides, designated pandinin 1 and 2, are alpha-helical polycationic peptides, with pandinin 1 belonging to the group of antibacterial peptides previously described from scorpions, frogs and insects, and pandinin 2 to the group of short magainin-type helical peptides from frogs. Both peptides demonstrated high antimicrobial activity against a range of Gram-positive bacteria (2.4-5.2 microM), but were less active against Gram-negative bacteria (2.4-38.2 microM), and only pandinin 2 affected the yeast Candida albicans. Pandinin 2 also demonstrated strong haemolytic activity (11.1-44.5 microM) against sheep erythrocytes, in contrast with pandinin 1, which was not haemolytic. CD studies and a high-resolution structure of pandinin 2 determined by NMR, showed that the two peptides are both essentially helical, but differ in their overall structure. Pandinin 2 is composed of a single alpha-helix with a predominantly hydrophobic N-terminal sequence, whereas pandinin 1 consists of two distinct alpha-helices separated by a coil region of higher flexibility. This is the first report of magainin-type polycationic antimicrobial peptides in scorpion venom. Their presence brings new insights into the mode of action of scorpion venom and also opens new avenues for the discovery of novel antibiotic molecules from arthropod venoms.

Amino Acid Sequence↗
PubMed1997

Identification of structural elements of a scorpion alpha-neurotoxin important for receptor site recognition.

alpha-Neurotoxins from scorpion venoms constitute the most studied group of modifiers of the voltage-sensitive sodium channels, and yet, their toxic site has not been characterized. We used an efficient bacterial expression system for modifying specific amino acid residues of the highly insecticidal alpha-neurotoxin LqhalphaIT from the scorpion Leiurus quinquestriatus hebraeus. Toxin variants modified at tight turns, the C-terminal region, and other structurally related regions were subjected to neuropharmacological and structural analyses. This approach highlighted both aromatic (Tyr10 and Phe17) and positively charged (Lys8, Arg18, Lys62, and Arg64) residues that (i) may interact directly with putative recognition points at the receptor site on the sodium channel; (ii) are important for the spatial arrangement of the toxin polypeptide; and (iii) contribute to the formation of an electrostatic potential that may be involved in biorecognition of the receptor site. The latter was supported by a suppressor mutation (E15A) that restored a detrimental effect caused by a K8D substitution. The feasibility of producing anti-insect scorpion neurotoxins with augmented toxicity was demonstrated by the substitution of the C-terminal arginine with histidine. Altogether, the present study provides for the first time an insight into the putative toxic surface of a scorpion neurotoxin affecting sodium channel gating.

Amino Acid Sequence↗
PubMed1991

Insulin reverses haemodynamic changes and pulmonary oedema in children stung by the Indian red scorpion Mesobuthus tamulus concanesis, Pocock.

The efficacy of insulin administration in reversing haemodynamic changes in pulmonary oedema in victims of poisonous scorpion sting is assessed by a study based on animal experiments in which insulin administration reversed metabolic and electrocardiographic changes induced by scorpion envenomation. Six previously healthy children aged 18 months to 11 years were admitted to hospital five to 17 hours after scorpion sting. Frusemide for raised central venous pressure and pulmonary oedema, crystalloid infusion for reduced central venous pressure, and hydrocortisone and dopamine for hypotension were used as standard therapy. Insulin (0.3 units g-1 of glucose) was administered when the standard therapy failed to produce an improvement, and at the earliest sign of haemodynamic instability. Reversal of pulmonary oedema and haemodynamic changes, and attainment or normal respiratory rate, blood pressure and central venous pressure, were observed. It is concluded that insulin administration may be useful in reversing haemodynamic changes and pulmonary oedema in victims of scorpion stings.

Animals↗
PubMed1991

Scorpion sting: a management problem.

Admissions for scorpion sting in 1 year and deaths resulting from scorpion sting over 3 years were analysed. Features that indicated the severity of the clinical condition were identified. Pulmonary oedema and shock were the usual causes of death. Poor management of fluid therapy was responsible for the frequently unsatisfactory resolution of envenoming, especially when purified human plasma was used. The role of the scorpion antivenom used is questioned and controversy regarding the most appropriate sedative to use in the management of scorpion sting is still not resolved. An in-depth study of these management issues is urgently required.

Animals↗
PubMed1991

Cardiovascular manifestations of severe scorpion sting in India (review of 34 children).

Scorpion sting in children is a hazardous and potentially fatal condition. Of 34 children admitted to hospital in Mahad, Maharashtra State, India following scorpion sting, 14 had hypertension (130/90-170/130 mmHg), five had myocardial failure, acute pulmonary oedema developed in nine, two had tachycardia (110-200/min) and four died. Analysis of data suggests that cardiovascular morbidity and mortality depend upon the time lapse between sting and administration of vasodilators. Current management of human scorpionism consists of early admission to hospital and immediate reduction of raised blood pressure with sublingual nifedipine while peripheral action of venom is antagonized by the post-synaptic alpha blocker prazosin; in addition, digoxin, frusemide, aminophylline and oxygen are administered. The patient is kept under close surveillance in an intensive care unit. Massive life-threatening pulmonary oedema is treated with a sodium nitroprusside drip. We suggest that aggressive medical management directed at the organ system specifically affected by scorpion venom can be effective.

Adolescent↗
PubMed2001

Precursor of a novel scorpion venom peptide (BmKn1) with no disulfide bridge from Buthus martensii Karsch.

A full-length cDNA sequence encoding the precursor of a novel venom peptide (named BmKn1) with no disulfide bridge was first isolated from the venom gland cDNA library of Chinese scorpion Buthus martensii Karsch. The encoded precursor consisted of 70 amino acid residues including two parts: a signal peptide of 23 residues, and a putative mature venom peptide (BmKn1) of 47 residues. The sequence of BmKn1 showed no similarity to those of other scorpion venom peptides. BmKn1 may be the first member of a new venom peptide family from scorpion. Future research will be interesting to unravel further the pharmacological function of this novel scorpion venom peptide.

Amino Acid Sequence↗
PubMed2004

NMR solution structure of Cn12, a novel peptide from the Mexican scorpion Centruroides noxius with a typical beta-toxin sequence but with alpha-like physiological activity.

Cn12 isolated from the venom of the scorpion Centruroides noxius has 67 amino-acid residues, closely packed with four disulfide bridges. Its primary structure and disulfide bridges were determined. Cn12 is not lethal to mammals and arthropods in vivo at doses up to 100 microg per animal. Its 3D structure was determined by proton NMR using 850 distance constraints, 36 phi angles derived from 36 coupling constants obtained by two different methods, and 22 hydrogen bonds. The overall structure has a two and half turn alpha-helix (residues 24-32), three strands of antiparallel beta-sheet (residues 2-4, 37-40 and 45-48), and a type II turn (residues 41-44). The amino-acid sequence of Cn12 resembles the beta scorpion toxin class, although patch-clamp experiments showed the induction of supplementary slow inactivation of Na(+) channels in F-11 cells (mouse neuroblastoma N18TG-2 x rat DRG2), which means that it behaves more like an alpha scorpion toxin. This behaviour prompted us to analyse Na(+) channel binding sites using information from 112 Na(+) channel gene clones available in the literature, focusing on the extracytoplasmic loops of the S5-S6 transmembrane segments of domain I and the S3-S4 segments of domain IV, sites considered to be responsible for binding alpha scorpion toxins.

Amino Acid Sequence↗
PubMed2004

Phaiodotoxin, a novel structural class of insect-toxin isolated from the venom of the Mexican scorpion Anuroctonus phaiodactylus.

A peptide called phaiodotoxin was isolated from the venom of the scorpion Anuroctonus phaiodactylus. It is lethal to crickets, but non toxic to mice at the doses assayed. It has 72 amino acid residues, with a molecular mass of 7971 atomic mass units. Its covalent structure was determined by Edman degradation and mass spectrometry; it contains four disulfide-bridges, of which one of the pairs is formed between cysteine-7 and cysteine-8 (positions Cys63-Cys71). The other three pairs are formed between Cys13-Cys38, Cys23-Cys50 and Cys27-Cys52. Comparative sequence analysis shows that phaiodotoxin belongs to the long-chain subfamily of scorpion peptides. Several genes coding for this peptide and similar ones were cloned by PCR, using cDNA prepared from the RNA of venomous glands of this scorpion. Electrophysiological assays conducted with this toxin in several mammalian cell lines (TE671, COS7, rat GH3 and cerebellum granular cells), showed no effect on Na+ currents. However, it shifts the voltage dependence of activation and inactivation of insect Na+ channels (para/tipE) to more negative and positive potentials, respectively. Therefore, the 'window' current is increased by 225%, which is thought to be the cause of its toxicity toward insects. Phaiodotoxin is the first toxic peptide ever purified from a scorpion of the family Iuridae.

Amino Acid Sequence↗
PubMed1995

Right ventricular dysfunction following severe scorpion envenomation.

OBJECTIVE: Evaluation of right ventricular (RV) performance in patients presenting with pulmonary edema following scorpion envenomation. DESIGN: Cohort study. SETTING: Medical intensive care unit of a teaching hospital. PATIENTS: Eight consecutive adult patients stung by yellow scorpion Androctonus australis and presenting with pulmonary edema at hospital admission. INTERVENTIONS: In all patients, standard hemodynamic parameters and RV volumes were measured using a pulmonary artery catheter equipped with a rapid responding thermistor enabling measurement of RV ejection fraction (RVEF). MEASUREMENTS: Hemodynamic evaluation was performed at the time of hospital admission prior to any therapeutic intervention and just before the removal of the pulmonary catheter (2.3 +/- 0.5 days after admission) in the surviving patients (n = 7). RESULTS: All patients had a decreased RVEF (24 +/- 7%) and cardiac index (2.44 +/- 0.5 L/min/m2) and increased pulmonary artery occlusion pressure (23 +/- 6 mm Hg). Right ventricular end-systolic pressure/volume ratio was decreased (.56 +/- .19 mm Hg/mL/m2), suggesting an altered RV contractility. Follow-up evaluation performed in survivors, without any inotropic support, showed hemodynamic changes reflecting a trend toward full recovery. Right ventricular ejection fraction and cardiac index improved markedly (from 24 +/- 7% to 39 +/- 10% and from 2.44 +/- 0.5 to 4 +/- .3 L/min/m2, respectively). Pulmonary artery occlusion pressure, peak systolic pulmonary artery pressure, and mean pulmonary artery pressure decreased significantly from baseline values (12 +/- 3 mm Hg, 29 +/- 5 mm Hg, and 20 +/- 4 mm Hg, respectively). Right ventricular end systolic pressure/volume ratio remained almost constant, suggesting that afterload enhancement accounted predominantly for RVEF improvement. CONCLUSION: These data show that RV function impairment is associated with left ventricular dysfunction, suggesting similarities between left ventricular and RV alterations following severe scorpion envenomation providing further arguments to the hypothesis of scorpionic myocarditis.

Adult↗