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 757 records · Page 42Linked to original sources
PubMed1986

Differential effects of defined chemical modifications on antigenic and pharmacological activities of scorpion alpha and beta toxins.

Specific chemical modifications of scorpion alpha and beta toxins have been used to study the involvement of particular residues in both the pharmacological and the antigenic sites of these toxins. Modification by 1,2-cyclohexanedione of arginine-27 of a beta toxin, Centruroides suffusus suffusus toxin II, drastically decrease the antigenic activity without any influence on the pharmacological activity. Conversely, modification by the same reagent of arginine-2 of an alpha toxin, Androctonus australis Hector toxin III, led to a 100-times less pharmacologically potent derivative and did not induce a significant loss of antigenic activity. Excision of the N-terminal pentapeptide of another alpha toxin, Buthus occitanus mardochei toxin III, by pepsin digestion led to a non-toxic derivative retaining full antigenic activity. Thus, the N-terminal part of the conserved hydrophobic surface of the toxin is highly implicated in the pharmacological activity, whereas the region of arginine-27, located in the alpha helix situated on the back surface, opposite the conserved hydrophobic region, is fully implicated in the antigenic activity and is far from the pharmacological site. These results are good arguments in favor of the idea that in scorpion toxins the surfaces implicated in the pharmacological and the antigenic activities do not overlap. Since the antigenic sites are present in highly variable sequence the development of an efficient polyvalent serotherapy is questionable.

Amino Acids↗
PubMed1989

Structure/activity relationships of scorpion alpha-toxins. Multiple residues contribute to the interaction with receptors.

Chemical modifications of tyrosine and tryptophan residues of scorpion alpha-neurotoxins II and III from Androctonus australis Hector were performed as well as modification of the two arginines and the alpha-amino group of toxin I. The pharmacological potencies of each derivative were assessed in vivo by LD50 measurement and in vitro by competition experiments with 125I-toxin for synaptosomal receptors. Arginine residues in positions 2 and 60 and the alpha-amino group of Androctonus toxin I were derivatized by p-hydroxyphenylglyoxal; the corresponding modified toxins exhibit low pharmacological potencies. Tryptophan 38 of toxin II and tryptophan 45 of toxin III were modified by nitrophenylsulfenyl chloride, leading respectively to a poorly and a fully active derivative. The tetranitromethane modification of tyrosine residues in positions 60, 5 and 14 of toxin III induced respectively 60%, 40% and 30% of loss of biological activity. Circular dichroic analysis indicated that for every derivative, except the nitrophenylsulfenyl derivative of Trp-45 of AaH III, the conformation of the toxin was not altered by derivatization. Conformational integrity was also confirmed by full activity of the derivatives in radioimmunoassays. Taken together, the results suggest that aromatic residues belonging to the conserved hydrophobic surface, to the C-terminal and to the loop region 37-44 are involved in the molecular mechanisms by which scorpion alpha-toxins act. Charged residues in the N-terminal and C-terminal also contribute to the high efficacy of the binding process. It appears that all important residues are clustered on one face of the toxin, suggesting a multipoint interaction with the proteins of the sodium channel.

Amino Acid Sequence↗
PubMed1992

Amino acid sequence and immunological characterization with monoclonal antibodies of two toxins from the venom of the scorpion Centruroides noxius Hoffmann.

Two toxins, which we propose to call toxins 2 and 3, were purified to homogeneity from the venom of the scorpion Centruroides noxius Hoffmann. The full primary structures of both peptides (66 amino acid residues each) was determined. Sequence comparison indicates that the two new toxins display 79% identity and present a high similarity to previously characterized Centruroides toxins, the most similar toxins being Centruroides suffusus toxin 2 and Centruroides limpidus tecomanus toxin 1. Six monoclonal antibodies (mAb) directed against purified fraction II-9.2 (which contains toxins 2 and 3) were isolated in order to carry out the immunochemical characterization of these toxins. mAb BCF2, BCF3, BCF7 and BCF9 reacted only with toxin 2, whereas BCF1 and BCF8 reacted with both toxins 2 and 3 with the same affinity. Simultaneous binding of mAb pairs to the toxin and cross-reactivity of the venoms of different scorpions with the mAb were examined. The results of these experiments showed that the mAb define four different epitopes (A-D). Epitope A (BCF8) is topographically unrelated to epitopes B (BCF2 and BCF7), C (BCF3) and D (BCF9) but the latter three appear to be more closely related or in close proximity to each other. Epitope A was found in all Centruroides venoms tested as well as on four different purified toxins of C. noxius, and thus seems to correspond to a highly conserved structure. Based on the cross-reactivity of their venoms with the mAb, Centruroides species could be classified in the following order: Centruroides elegans, Centruroides suffusus suffusus = Centruroides infamatus infamatus, Centruroides limpidus tecomanus, Centruroides limpidus limpidus, and Centruroides limpidus acatlanensis, according to increasing immunochemical relatedness of their toxins to those of Centruroides noxius. All six mAb inhibited the binding of toxin 2 to rat brain synaptosomal membranes, but only mAb BCF2, which belongs to the IgG2a subclass, displayed a clear neutralizing activity in vivo.

Amino Acid Sequence↗
PubMed1996

1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus.

We describe the secondary structure and the overall fold of toxin III from the venom of the scorpion Leiurus quinquestriatus quinquestriatus determined using two-dimensional-1H-NMR spectroscopy. This protein, which contains 64 amino acids and 4 disulfide bridges, belongs to the long-chain toxin category and is highly toxic to both mammals and insects. The overall fold was determined on the basis of 1208 inter-proton-distance restraints derived from NOE measurements and 90 psi, phi dihedral-angle restraints derived from NOE connectivities and 3JNH-alphaH coupling constants using the HABAS program. This fold, which mainly consists of an alpha-helix packed against a small antiparallel three-stranded beta-sheet, and of several turns and loops, is similar to that of other long-chain scorpion toxins. Aromatic and non-polar residues form several patches on the surface of the protein which alternate with patches of charged and polar residues. Such a topology should be important in the interactions of toxin III with sodium channels in membranes. Two weakly constrained loops introduce some flexibility to the structure which could be related to the activity of this toxin. The central core of toxin III is compared with the cysteine-stabilized alpha beta motif (an alpha-helix connected to a beta-sheet through two disulfide bridges) found in insect defensins and plant thionins. Defensins and thionins are small proteins (approximately 40--50 amino acid residues) containing three or four disulfide bridges, respectively. This comparison confirms that the cysteine-stabilized alpha beta motif is a common core to a number of small proteins from different origins and having different activities.

Amino Acid Sequence↗
PubMed1996

A recombinant insect-specific alpha-toxin of Buthus occitanus tunetanus scorpion confers protection against homologous mammal toxins.

We have constructed a cDNA library from venom glands of the scorpion Buthus occitanus tunetanus and cloned a DNA sequence that encodes an alpha-toxin. This clone was efficiently expressed in Escherichia coli as a fusion protein with two Ig-binding (Z) domains of protein A from Staphylococcus aureus. After CNBr treatment of the fusion protein and HPLC purification, we obtained approximately 1 mg recombinant apha-toxin/l bacterial culture. The toxin, called Bot XIV, displays no toxicity towards mammals but is active towards insects as shown by its paralytic activity against Blatella germanica cockroach and by electrophysiological studies on Periplaneta americana cockroaches. The Bot XIV protein fused to two Z domains is highly immunogenic in mice and induces production of antisera that specifically recognize and neutralize highly toxic components that had been injected into mice. This fusion protein could be very useful for development of potent protective antisera against scorpion venoms.

Amino Acid Sequence↗
PubMed1997

Solution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom--structural heterogeneity induced by proline cis/trans isomerization.

Lqh-8/6 is a minor fraction isolated from the venom of the scorpion Leiurus quinquestriatus hebraeus. Here we describe the purification, amino acid sequencing and solution structure determination by NMR and molecular modeling of this peptide. Lqh-8/6 is a small polypeptide (38 residues) which contains 8 half-cystines and is highly similar to another venom component, chlorotoxin. Standard homonuclear methods were used to sequentially assign the proton NMR spectra and to collect spatial restraints for structure determination. Two populations, identified early in the assignment step, are in slow interconversion on the NMR timescale. The two conformers were shown to originate from a cis/trans peptidyl-prolyl isomerization. Using a distance geometry program and simulated annealing protocol under the NMR restraints we obtained 10 final structures for the major conformation (trans isomer). None of the structures showed NOE violations larger than 0.05 nm, and the rmsd value relative to the mean structure (considering the main chain atoms in well-defined secondary structure) is 0.07 nm. The three-dimensional structure contains a short alpha-helix strapped on a small antiparallel beta-strand and an N-terminal extended fragment. The sequence/structure and structure/function relationships of the new scorpion toxin-like peptide are discussed in the context of the present structure determination. This toxin shows a stable, highly populated cis conformer of a peptidyl-prolyl peptide bond.

Amino Acid Sequence↗
PubMed1997

Characterization of four toxins from Buthus martensi scorpion venom, which act on apamin-sensitive Ca2+-activated K+ channels.

Four peptidyl inhibitors of the small-conductance Ca2+-activated K+ channels (SK(Ca)) have been isolated from the venom of the Chinese scorpion Buthus martensi. These peptides were identified by screening C18 HPLC fractions of the crude venom by means of mass analysis by matrix-assisted-laser-desorption/ionization time-of-flight mass spectrometry, and toxicological tests in mice. Edman degradation analysis of the purified peptides showed sequences of 28-31 amino acids including 6 cysteine residues. Three of the sequences were similar to the P01 peptides from Androctonus scorpions, showing 76% sequence similarity for the most closely related, named BmP01, and 46% for the other two, named BmP02 and BmP03. Like the P01 peptides, these molecules showed a low toxic activity in mice after intracerebroventricular injection, and competed (K0.5 > 1 microM) with iodinated apamin for binding to its receptor site from rat brain, which has been proved to be the SK(Ca) channels. The fourth toxin was structurally related to the P05/leiurotoxin I toxin family, with 90% similarity, and was named BmP05. This toxin exhibited a high toxic activity with lethal effects in mice. Due to its small representation in the venom [less than 0.01% (by mass)], its biological properties have been assessed on the synthetic analogue of BmP05, which was assembled on a solid phase by means of Fmoc methodology. The synthetic peptide was physicochemically identical to the natural peptide, as shown by comparison of their molecular masses and amino acid compositions, and by their coelution after coinjection on capillary electrophoresis. These results confirmed the primary structure of BmP05 including an amidated C-terminus. Similarly to natural BmP05, synthetic BmP05 produced toxic and lethal effects after intracerebroventricular injection in mice (LD50 = 37 ng), and was able to compete with iodinated apamin for binding to its receptor in rat brain (K0.5 = 20 pM).

Amino Acid Sequence↗
PubMed1997

Biochemical and pharmacological characterization of a depressant insect toxin from the venom of the scorpion Buthacus arenicola.

A depressant toxin active on insects, Buthacus arenicola IT2, was isolated from the venom of the North African scorpion B. arenicola and its structural and pharmacological properties were investigated. B. arenicola IT2 is a single polypeptide of 61 amino acid residues, including 8 half-cystines but no methionine and histidine, with a molecular mass of 6835 Da. Its amino acid sequence is 79-95% identical to other depressant toxins from scorpions. When injected into the cockroach Blatella germanica, B. arenicola IT2 induced a slow depressant flaccid paralysis with a LD50 of 175 ng. B. arenicola IT2 has two non-interacting binding sites in cockroach neuronal membranes: one of high affinity (Kd1 = 0.11 +/- 0.04 nM) and low capacity (Bmax1 = 2.2 +/- 0.6 pmol/mg), and one of low affinity (Kd2 = 24 +/- 7 nM) and high capacity (Bmax2 = 226 +/- 92 pmol/mg). Its binding to these two sites was completely inhibited by Leiurus quinquestriatus quinquestriatus IT2, a depressant toxin from L. quinquestriatus quinquestriatus. Reciprocal-binding experiments between B. arenicola IT2 and the excitatory insect-toxin A. australis Hector IT revealed competition between the two toxins for the high-affinity sites of B. arenicola IT2. B. arenicola IT2 has a higher affinity than L. quinquestriatus hebraeus IT2, a depressant toxin from L. quinquestriatus hebraeus. Thus, B. arenicola IT2 represents an interesting tool to study the receptor site for depressant toxins on insect sodium channels.

Amino Acid Sequence↗
PubMed2004

Phaiodactylipin, a glycosylated heterodimeric phospholipase A from the venom of the scorpion Anuroctonus phaiodactylus.

Phaiodactylipin was purified from the venom of the scorpion Anuroctonus phaiodactylus. It is the first protein to be purified from a scorpion of the family Iuridae and has a molecular mass of 19 172 atomic mass units. The mature protein is composed of two subunits, the large one consisting of 108 amino acid residues, whereas the small subunit has only 18 residues, and the structure is stabilized by five disulfide bridges. The heterodimer is expressed from a single message containing 769 base pairs and a signal peptide with 16 and/or 25 amino acid residues. During maturation an internal hexapeptide is excised. There are three putative sites of N-glycosylation, one of which is situated in the small subunit region. The carbohydrate composition of this site was determined by mass spectrometry analysis and was found to contain three hexoses, two N-acetyl-hexoses and two deoxyhexoses. The protein has a calcium dependent phospholipase A(2) type of activity. It is lethal to arthropods (insects and isopods), but not toxic to mammals, using doses up to 20 microg per 20 g mouse body weight. For crickets, a dose of 5 microg per animal is lethal; however, when injected into mice it is capable of causing only muscular inflammation, without rupture of the basal membrane of cells. It has a direct hemolytic effect in human erythrocytes and retards the coagulation time of blood. It is an unusual phospholipase A(2), with only 36% and 50% amino acid sequence identities to the closest known phospholipases, imperatoxin I and phospholipin, respectively. Identities with bee and Heloderma venom phospholipase are only in the order of 28%.

Amino Acid Sequence↗
PubMed1999

Pulmonary oedema produced by scorpion venom augments a phenyldiguanide-induced reflex response in anaesthetized rats.

1. The involvement of pulmonary oedema produced by scorpion venom in augmenting a phenyldiguanide (PDG)-induced reflex response was evaluated in urethane-anaesthetized rats. 2. PDG-induced bradycardiac, hypotensive and apnoeic responses, expressed as time-response area, exhibited similarities before or after venom treatment. Hence, the time-response area of bradycardia was taken as a reflex parameter. Pulmonary oedema was determined by physical evaporation and histological methods. 3. Exposure to Indian red scorpion (Buthus tamulus, BT; i.v.) venom for 30 min increased the pulmonary water content (P < 0.05; Student's t test) and augmented the PDG-induced bradycardiac reflex response by more than 2 times (P < 0.001). The increase of pulmonary water content was maximal with 100 microg kg-1 of venom and the augmentation was maximal with 10 microg kg-1. In a separate series of experiments, the venom (100 microg kg-1)-induced pulmonary oedema was confirmed by histological and physical methods. In this group also, the venom augmented the reflex to the same magnitude. 4. Pulmonary oedema (physical and histological) and augmentation of the bradycardiac reflex response after BT venom (100 microg kg-1; i.v.) were absent in animals pretreated with aprotinin, a kallikrein-kinin inhibitor (6000 KIU; i. v.). 5. Ondansetron (10 microg kg-1; i.v.), a 5-HT3 receptor antagonist, failed to block the venom-induced pulmonary oedema (physical and histological) but blocked the venom-induced augmentation of the reflex. 6. The results of this study indicate that the venom-induced augmentation of the PDG reflex is associated with pulmonary oedema involving kinins utilizing 5-HT3 receptors.

Anesthetics, Intravenous↗
PubMed1986

Interactions of scorpion toxins with the sodium channel.

It is evident from the data reviewed that scorpion toxins can be distinguished on the basis of three properties: their effects on Na currents, their specific binding to excitable membranes, and the effects of depolarization and pH on binding and on effect. Additional work with other scorpion toxins is required to establish the degree of correlation between the three properties for each class of toxin. Further investigations with this family of homologous proteins will undoubtedly contribute not only to our understanding of the toxins themselves but also to our understanding of the structure and function of the Na channel.

Amino Acid Sequence↗
PubMed1980

The effect of scorpion venoms on the sodium currents of the squid giant axon.

1. The effect of externally applied scorpion venoms (0.1--0.5 mg/ml., species Leiurus quinquestriatus and Centruroides sculpturatus) on the Na currents of intracellularly perfused squid giant axons has been studied with the voltage-clamp method. 2. The venoms from the two species had the same effect. They reduced the size of the peak conductance but had little effect on its kinetics (time to peak, time constant of inactivation) and on its steady-state inactivation. The venoms increased markedly, however, the maintained conductance and the time constants of its turning-on and turning-off. 3. The voltage dependence of the maintained conductance was determined (a) by fitting a modified Hodgkin--Huxley equation to the Na currents and (b) by measuring the tail currents at the end of depolarizing pulses. The maintained conductance rose with increasing depolarization from a minimum at -20 mV to a maximum at 40 mV. The peak conductance, by contrast, was constant in the positive potential range. 4. The ratio maintained conductance in venom to maintained conductance in control varied between 2 and 7 (depending on the venom concentration and the time of treatment) and was not significantly dependent on membrane potential. 5. Peak current and maintained current reversed sign at the same potential and were both blocked by tetrodotoxin. 6. During a pulse to -2 mV preceded by a pre-pulse to -42 mV the Na conductance showed a rapid initial increase followed by a slower decay and a subsequent slow increase, reflecting the activation and inactivation of the peak conductance and the slow development of the maintained conductance. 7. Many of the observations are compatible with the idea that scorpion venoms increase the number of channels which go from the peak conductance state into the maintained conductance state (open in equilibrium or formed from closed in equilibrium or formed from open transition of the inactivation gate, see Chandler & Meves (1970 a, b)). But the alternative hypothesis that peak conductance and maintained conductance reflect two separate populations of Na channels cannot be ruled out.

Animals↗
PubMed1987

Properties of maintained sodium current induced by a toxin from Androctonus scorpion in frog node of Ranvier.

1. The effects of toxin II from scorpion Androctonus australis Hector (AaH II) on the Na current of frog myelinated nerve fibres were analysed under voltage-clamp conditions. 2. Like other alpha-scorpion toxins and Anemonia toxin II, AaH II both increased the inactivation time constants of peak Na current and induced a non-inactivatable Na current (maintained current). 3. In the presence of AaH II, the slope of the maintained conductance-voltage curve was less steep than that corresponding to the peak conductance and the maintained current reversed at a voltage about 20 mV more negative than the peak current. 4. When the peak current was inactivated by pre-depolarizations, 'on' and 'off' relaxation kinetics of the maintained current were an exponential function whose time constant changed with voltage in a bell-shaped manner. At 0 mV, the time constant was about 10 ms. 5. The effects of AaH II could be decomposed into fast effects (increase in inactivation time constants of the peak current) which developed within about 5 s and slow effects (increase in maintained current and changes in initial amplitudes of fast and slow phases of peak current inactivation) which developed within about 30 s. 6. These two types of AaH II effects could be completely removed by conditioning depolarizations giving rise to outward currents. 7. A model is proposed in which the binding of the toxin with its receptor is modulated by membrane potential and internal cations, the appearance of the maintained current is modulated by the environment of channels and the change in inactivation time constants is modulated by membrane potential. The maintained current would correspond to the transformation of a fraction of channels into a non-inactivable (late) form.

Animals↗
PubMed2005

Beta-scorpion toxin effects suggest electrostatic interactions in domain II of voltage-dependent sodium channels.

Beta-scorpion toxins specifically modulate the voltage dependence of sodium channel activation by acting through a voltage-sensor trapping model. We used mutagenesis, functional analysis and the action of beta-toxin as tools to investigate the existence and role in channel activation of molecular interactions between the charged residues of the S2, S3 and S4 segments in domain II of sodium channels. Mutating to arginine the acidic residues of the S2 and S3 transmembrane segments in domain II, or making charge-reversal mutation of the two outermost gating charges of the IIS4 voltage sensor, shifts the voltage dependence of channel activation to more positive potentials and enhances the effect of beta-scorpion toxin. Thus, mutations of acidic residues in IIS2 and IIS3 segments are able to promote voltage-sensor trapping in a way that is similar to the mutations of the arginines in the IIS4 segment. In order to disclose the network of interactions among acidic and basic residues we performed functional analysis of charge-inversion double mutants: our data suggest that the first arginine of the voltage sensor S4 in domain II (R850) interacts specifically with E805, D814 and E821 in the S2 and S3 segments, whereas the second arginine (R853) only interacts with D827 in the S3 segment. Our results suggest that the S2, S3 and S4 segments in domain II form a voltage-sensing structure, and that molecular interactions between the charged residues of this structure modulate the availability of the IIS4 voltage sensor for trapping by beta-toxins. They also provide unique insights into the molecular events that occur during channel activation, as well as into the structure of the channel.

Amino Acids, Acidic↗
PubMed2004

Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes.

The physiological function of T lymphocytes can be modulated selectively by peptide toxins acting on Kv1.3 K(+) channels. Because Kv1.3-specific peptide toxins are considered to have a significant therapeutic potential in the treatment of autoimmune diseases, the discovery of new toxins is highly motivated. Through chromatographic procedures and electrophysiological assays, using patch-clamp methodology, the isolation of a novel peptide named anuroctoxin was accomplished using the venom of the Mexican scorpion Anuroctonus phaiodactylus. It has 35 amino acid residues with a molecular weight of 4082.8, tightly bound by four disulfide bridges whose complete covalent structure was determined. It has a pyroglutamic acid at the N-terminal region and an amidated C-terminal residue. Sequence comparison and phylogenetic clustering analysis classifies anuroctoxin into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx 6.12). Patch-clamp experiments show that anuroctoxin is a high-affinity blocker of Kv1.3 channels of human T lymphocytes with a K(d) of 0.73 nM, and it does not block the Ca(2+)-activated IKCa1 K(+) channels. These two channels play different but important roles in T-lymphocyte activation. Furthermore, the toxin practically does not inhibit Shaker IR, mKv1.1, and rKv2.1 channels, whereas the affinity of anuroctoxin for hKv1.2 is almost an order of magnitude smaller than for Kv1.3. The pharmacological profile and the selectivity of this new toxin for Kv1.3 over IKCa1 may provide an important tool for the modulation of the immune system, especially in cases in which selective inhibition of Kv1.3 is required.

Animals↗
PubMed2006

Subtype specificity of scorpion beta-toxin Tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3.

Voltage-gated sodium (Nav) channels are modulated by a variety of specific neurotoxins. Scorpion beta-toxins affect the voltage-dependence of channel gating: In their presence, Nav channels activate at subthreshold membrane voltages. Previous mutagenesis studies have revealed that the beta-toxin Css4 interacts with the extracellular linker between segments 3 and 4 in domain 2 of Nav channels with the effect to trap this voltage sensor in an open position (Neuron 21: 919-931, 1998 ). The voltage sensor of domain 2 was thus identified to constitute a major part of neurotoxin receptor site 4. In this work, we studied the effects of the beta-toxin Tz1 from the Venezuelan scorpion Tityus zulianus on various mammalian Nav channel types expressed in HEK 293 cells. Although skeletal muscle channels (Nav1.4) were strongly affected by Tz1, the neuronal channels Nav1.6 and Nav1.2 were less sensitive, and the cardiac Nav1.5 and the peripheral nerve channel Nav1.7 were essentially insensitive. Analysis of channel chimeras in which whole domains of Nav1.2 were inserted into a Nav1.4 background revealed that the Nav1.2 phenotype was not conferred to Nav1.4 by domain 2 but by domain 3. The interaction epitope could be narrowed down to residues Glu1251, Lys1252, and His1257 located in the C-terminal pore loop in domain 3. The receptor site for beta-toxin interaction with Nav channels thus spans domains 2 and 3, where the pore loop in domain 3 specifies the pharmacological properties of individual neuronal Nav channel types.

Amino Acid Sequence↗
PubMed1970

Defibrination syndrome due to scorpion venom poisoning.

Disseminated intravascular coagulation occurred in dogs given scorpion venom subcutaneously in doses of 3 mg./kg. body weight. Treatment with heparin reversed the coagulation abnormality of the syndrome and 10 out of 12 dogs survived. Necropsy findings in human patients stung by scorpions suggest that this syndrome also occurs in man.

Animals↗
PubMed1977

Exocrine pancreatic response to the venom of the scorpion, Tityus trinitatis.

This paper records for the first time the exocrine pancreatic response to scorpion venom, in this case that of Tityus trinitatis, a scorpion endemic in Trinidad. The crude venom injected intravenously into fasting anaesthetised dogs induced a secretion of the exocrine pancreas. The secretion evoked was rich in enzymes.

Amylases↗