Crotalus Durissus Collilineatus Venom Research Articles

Fraction of C. d. collilineatus venom containing crotapotin protects PC12 cells against MPP + toxicity by activating the NGF-signaling pathway.

Parkinson's disease (PD) is the second most prevalent neurodegenerative disease. There is no effective treatment for neurodegenerative diseases. Snake venoms are a cocktail of proteins and peptides with great therapeutic potential and might be useful in the treatment of neurodegenerative diseases. Crotapotin is the acid chain of crotoxin, the major component of Crotalus durissus collilineatus venom. PD is characterized by low levels of neurotrophins, and synaptic and axonal degeneration; therefore, neurotrophic compounds might delay the progression of PD. The neurotrophic potential of crotapotin has not been studied yet. We evaluated the neurotrophic potential of crotapotin in untreated PC12 cells, by assessing the induction of neurite outgrowth. The activation of the NGF signaling pathway was investigated through pharmacological inhibition of its main modulators. Additionally, its neuroprotective and neurorestorative effects were evaluated by assessing neurite outgrowth and cell viability in PC12 cells treated with the dopaminergic neurotoxin MPP+ (1-methyl-4-phenylpyridinium), known to induce Parkinsonism in humans and animal models. Crotapotin induced neuritogenesis in PC12 cells through the NGF-signaling pathway, more specifically, by activating the NGF-selective receptor trkA, and the PI3K/Akt and the MAPK/ERK cascades, which are involved in neuronal survival and differentiation. In addition, crotapotin had no cytotoxic effect and protected PC12 cells against the inhibitory effects of MPP+ on cell viability and differentiation. These findings show, for the first time, that crotapotin has neurotrophic/neuroprotective/neurorestorative potential and might be beneficial in Parkinson's disease. Additional studies are necessary to evaluate the toxicity of crotapotin in other cell models.

Structural studies with crotoxin B from Crotalus durissus collilineatus venom suggest a heterodimeric assembly formed by two new isoforms

In accidents involving Crotalus snakes, the crotoxin complex (CTX) plays lethal action due to its neurotoxic activity. On the other hand, CTX have potential biotechnological application due to its anti-tumoral, anti-inflammatory, antimicrobial, analgesic and immunomodulatory properties. CTX is a heterodimer composed of Crotoxin A (CA or crotapotin), the acidic nontoxic and non-enzymatic component and; Crotoxin B (CB), a basic, toxic and catalytic PLA2. Currently, there are two classes of CTX isoforms, whose differences in their biological activities have been attributed to features presented in CB isoforms. Here, we present the crystal structure of CB isolated from the Crotalus durissus collilineatus venom. It amino acid sequence was assigned using the SEQUENCE SLIDER software, which revealed that the crystal structure is a heterodimer composed of two new CB isoforms (colCB-A and colCB-B). Bioinformatic and biophysical analyses showed that the toxin forms a tetrameric assembly in solution similar to CB from Crotalus durissus terrificus venom, despite some differences observed at the dimeric interface. By the previously proposed classification, the colCB-B presents features of the class I isoforms while colCB-A cannot be classified into classes I and II based on its amino acid sequence. Due to similar features observed for other CB isoforms found in the NCBI database and the results obtained for colCB-A, we suggest that there are more than two classes of CTX and CB isoforms in crotalic venoms.

Insights into structure and function of CdcVEGFs, the vascular endothelial growth factor from Crotalus durissus collilineatus snake venom

Vascular endothelial growth factors (VEGFs) are crucial molecules involved in the modulation of angiogenesis. Snake venom-derived VEGFs (svVEGFs) are known to contribute significantly to the envenoming due to their capacity of increasing vascular permeability. In our work, we isolated and analyzed the biochemical and functional properties of the VEGF from Crotalus durissus collilineatus venom (CdcVEGF). The venom was fractionated by reversed phase chromatography on FPLC system (Fast Protein Liquid Chromatography) and the eluted fractions were submitted to an ELISA assay using an anti-VEGF-F antibody, for identification of svVEGF. Positive fractions for svVEGF were submitted to SDS-PAGE and to an anion exchange chromatography to isolate the molecule. The subfractions were analyzed by ELISA and SDS-PAGE and six of them presented svVEGFs, named CdcVEGF1 (Q23-3), CdcVEGF2 (Q24-3), CdcVEGF3 (Q24-4), CdcVEGF4 (Q25-3), CdcVEGF5 (Q25-4), and CdcVEGF6 (Q25-5). Their structural characterization was accomplished by mass spectrometry analysis using MALDI-TOF to determine their molecular masses and UPLC-ESI-QTOF to determine their amino acid sequence. Interestingly, all isolated CdcVEGFs induced angiogenesis on HUVEC cells through tube formation on Matrigel when compared to culture medium (negative control). Moreover, CdcVEGF2 and CdcVEGF3 also induced a significant increase in tube formation when compared to the positive control (basic fibroblast growth factor - bFGF). Additionally, crotalid antivenom produced by the Instituto Butantan was able to recognize CdcVEGFs, demonstrating to be immunogenic. This study demonstrates that snake venom cocktail can reveal novel and important molecules, which are potential molecular tools to study diverse biological processes, such as angiogenesis.

Unraveling the structure and function of CdcPDE: A novel phosphodiesterase from Crotalus durissus collilineatus snake venom

This study reports the isolation, structural, biochemical, and functional characterization of a novel phosphodiesterase from Crotalus durissus collilineatus venom (CdcPDE). CdcPDE was successfully isolated from whole venom using three chromatographic steps and represented 0.7% of total protein content. CdcPDE was inhibited by EDTA and reducing agents, demonstrating that metal ions and disulfide bonds are necessary for its enzymatic activity. The highest enzymatic activity was observed at pH 8–8.5 and 37 °C. Kinetic parameters indicated a higher affinity for the substrate bis(p-nitrophenyl) phosphate compared to others snake venom PDEs. Its structural characterization was done by the determination of the protein primary sequence by Edman degradation and mass spectrometry, and completed by the building of molecular and docking-based models. Functional in vitro assays showed that CdcPDE is capable of inhibiting platelet aggregation induced by adenosine diphosphate in a dose-dependent manner and demonstrated that CdcPDE is cytotoxic to human keratinocytes. CdcPDE was recognized by the crotalid antivenom produced by the Instituto Butantan. These findings demonstrate that the study of snake venom toxins can reveal new molecules that may be relevant in cases of snakebite envenoming, and that can be used as molecular tools to study pathophysiological processes due to their specific biological activities.

Beyond hemostasis: a snake venom serine protease with potassium channel blocking and potential antitumor activities

Snake venom serine proteases (SVSPs) are complex and multifunctional enzymes, acting primarily on hemostasis. In this work, we report the hitherto unknown inhibitory effect of a SVSP, named collinein-1, isolated from the venom of Crotalus durissus collilineatus, on a cancer-relevant voltage-gated potassium channel (hEAG1). Among 12 voltage-gated ion channels tested, collinein-1 selectively inhibited hEAG1 currents, with a mechanism independent of its enzymatic activity. Corroboratively, we demonstrated that collinein-1 reduced the viability of human breast cancer cell line MCF7 (high expression of hEAG1), but does not affect the liver carcinoma and the non-tumorigenic epithelial breast cell lines (HepG2 and MCF10A, respectively), which present low expression of hEAG1. In order to obtain both functional and structural validation of this unexpected discovery, where an unusually large ligand acts as an inhibitor of an ion channel, a recombinant and catalytically inactive mutant of collinein-1 (His43Arg) was produced and found to preserve its capability to inhibit hEAG1. A molecular docking model was proposed in which Arg79 of the SVSP 99-loop interacts directly with the potassium selectivity filter of the hEAG1 channel.

Cell migration inhibition activity of a non-RGD disintegrin from Crotalus durissus collilineatus venom

BackgroundIn recent decades, snake venom disintegrins have received special attention due to their potential use in anticancer therapy. Disintegrins are small and cysteine-rich proteins present in snake venoms and can interact with specific integrins to inhibit their activities in cell-cell and cell-ECM interactions. These molecules, known to inhibit platelet aggregation, are also capable of interacting with certain cancer-related integrins, and may interfere in important processes involved in carcinogenesis. Therefore, disintegrin from Crotalus durissus collilineatus venom was isolated, structurally characterized and evaluated for its toxicity and ability to interfere with cell proliferation and migration in MDA-MB-231, a human breast cancer cell line.MethodsBased on previous studies, disintegrin was isolated by FPLC, through two chromatographic steps, both on reversed phase C-18 columns. The isolated disintegrin was structurally characterized by Tris-Tricine-SDS-PAGE, mass spectrometry and N-terminal sequencing. For the functional assays, MTT and wound-healing assays were performed in order to investigate cytotoxicity and effect on cell migration in vitro, respectively.ResultsDisintegrin presented a molecular mass of 7287.4 Da and its amino acid sequence shared similarity with the disintegrin domain of P-II metalloproteases. Using functional assays, the disintegrin showed low cytotoxicity (15% and 17%, at 3 and 6 μg/mL, respectively) after 24 h of incubation and in the wound-healing assay, the disintegrin (3 μg/mL) was able to significantly inhibit cell migration (24%, p < 0.05), compared to negative control.ConclusionThus, our results demonstrate that non-RGD disintegrin from C. d. collilineatus induces low cytotoxicity and inhibits migration of human breast cancer cells. Therefore, it may be a very useful molecular tool for understanding ECM-cell interaction cancer-related mechanisms involved in an important integrin family that highlights molecular aspects of tumorigenesis. Also, non-RGD disintegrin has potential to serve as an agent in anticancer therapy or adjuvant component combined with other anticancer drugs.

Identification of antinociceptive fraction of snake venom from Crotalus durissus collilineatus crotamine-negative and its acute toxicity evaluation

The crude venom of the snake Crotalus durissus collilineatus (CDC) promotes neurological signs and symptoms in accidents involving humans and animals and the victims reports analgesia at the bite site, without tissue destruction. Studies shows that CDC has analgesic activity, among others. The crude venom is considered unsuitable for therapeutic purposes, with encouragement to the fractionation and purification of the same. Thus, the aim with CDC venom is: to perform fractionation by preparative HPLC; to test the antinociceptive activity of fractions and acute toxicity of active fractions. The CDC was fractionated on preparative HPLC-PDA (Oliveira et al., 2015) and the fractions were tested for their antinociceptive activity for writhing test by acetic acid (0.6%) in mice. For one of the fractions, which showed high analgesic effect both p.o. and i.p. routes, it evaluated the acute toxicity by the up and down method (OECD, 2001). In the fractionation by HPLC-PDA, CDC yielded 10 peaks (P1P10). SDS-PAGE showed that there was a good separation of components of the venom. All peaks were evaluated for their ability to reduce writhing, and the only one that apparently showed antinociceptive effect was Fr5 fraction (40 μg/kg). The Fr5 was able to reduce by 47% the number of contortions (i.p.) and 87% (p.o.), compared to control. The Fr5 fraction showed no morbidity and no mortality in the acute toxicity test (dose of 1000 μg/kg, p.o.); so it was not possible to estimate the LD50. According to the results, it can be stated that the venom and Fr5 of Crotalus durissus collilineatus snake of crotamine-negative type, may exhibit antinociceptive activity by suppressing nociception induced by acetic acid, suggesting it is related to effects on peripheral sites spinal and presents low acute toxicity values in experimental animals.

In silico glycosylation studies of native and recombinant forms of Collinein-1, a serine proteinase from Crotalus durissus collilineatus venom

In silico glycosylation studies of native and recombinant forms of Collinein-1, a serine proteinase from Crotalus durissus collilineatus venom

Effect of umbelliferone (7-hydroxycoumarin, 7-HOC) on the enzymatic, edematogenic and necrotic activities of secretory phospholipase A2 (sPLA2) isolated from Crotalus durissus collilineatus venom

Flavonoids, coumarins and other polyphenolic compounds are powerful antioxidants both in hydrophilic and lipophylic environments with diverse pharmacological properties including anti-inflammatory activity. Despite being widely used as powerful therapeutic agents for blood coagulation disorders, more specifically to control some serine protease enzymes, the mechanism of anti-inflammatory activity of coumarins is unknown, unlike that of flavonoids. Although their controlling effect on serine proteases is well acknowledged, their action on secretory phospholipase A2 (sPLA2) remains obscure. The present study describes the interaction between umbelliferone (7-HOC) and the sPLA2 from Crotalus durissus collilineatus venom. In vitro inhibition of sPLA2 enzymatic activity by 7-HOC was estimated using 4N3OBA as substrate, resulting in an irreversible decrease in such activity proportional to 7-HOC concentration. The biophysical interaction between 7-HOC and sPLA2 was examined by fluorescent spectral analysis and circular dichroism studies. Results from both techniques clearly showed that 7-HOC strongly modified the secondary structure of this enzyme and CD spectra revealed that it strongly decreased sPLA2 alpha-helical conformation. In addition, two-dimensional electrophoresis indicated an evident difference between HPLC-purified native and 7-HOC-treated sPLA2s, which were used in pharmacological experiments to compare their biological activities. In vivo anti-inflammatory activity was assessed by the sPLA2-induced mouse paw edema model, in which 7-HOC presented an effect similar to those of dexamethasone and cyproheptadine against the pro-inflammatory effect induced by native sPLA2 on the mouse paw edema, mast cell degranulation and skin edema. On the other hand, 7-HOC exhibited a more potent inhibitory effect on sPLA2 than that of p-bromophenacyl bromide ( p-BPB). Our data suggest that 7-HOC interacts with sPLA2 and causes some structural modifications that lead to a sharp decrease or inhibition of the edematogenic and myotoxic activities of this enzyme, indicating its potential use to suppress inflammation induced by sPLA2 from the snake venom.

Biological and Structural Characterization of Crotoxin and New Isoform of Crotoxin B PLA2 (F6a) from Crotalus durissus collilineatus Snake Venom

A new crotoxin B isoform PLA2 (F6a), from Crotalus durissus collilineatus was purified from by one step reverse phase HPLC chromatography using μ-Bondapack C-18 column analytic. The new crotoxin B isoform PLA2 (F6a), complex crotoxin, the catalytic subunit crotoxin B isoform PLA2 (F6a) and two crotapotin isoforms (F3 and F4), were isolated from the venom of Crotalus durissus collilineatus. The crotapotins isoforms F3 and F4 had similar chemical properties, the two proteins different in their ability to inhibit of isoforms of PLA2 (F6 and F6a). The molecular masses estimated by MALDI-TOF mass spectrometry were: crotoxin B: 14,943.14 Da, crotapotin F3: 8,693.24 Da, and crotapotin F4: 9 314.56 Da. The new crotoxin B isoform PLA2 (F6a) contained 122 amino acid residues and a pI of 8.58. Its amino acid sequence presents high identity with those of other PLA2s, particularly in the calcium binding loop and active site helix 3. It also presents similarities in the C-terminal region with other myotoxic PLA2s. The new crotoxin B isoform PLA2 (F6a) contained 122 amino acid residues, with a primary structure of HLLQFNKMIK FETRRNAIPP YAFYGCYCGW GGRGRPKDAT DRCCFVHDCC YGKLAKCNTK WDFYRYSLKS GYITCGKGTW CEEQICECDR VAAECLRRSL STYRYGYMIY PDSRCRGPSE TC. A neuromuscular blocking activity was induced by crotoxin and new crotoxin B isoform PLA2 (F6a) in the isolated mouse phrenic nerve diaphragm and the biventer cervicis chick nerve-muscle preparation. Whole crotoxin was devoid of cytolytic activity upon myoblasts and myotubes in vitro, whereas new crotoxin B isoform PLA2 (F6a) was clearly cytotoxic to these cells.

A novel peptide from the ACEI/BPP-CNP precursor in the venom of Crotalus durissus collilineatus

In crotaline venoms, angiotensin-converting enzyme inhibitors [ACEIs, also known as bradykinin potentiating peptides (BPPs)], are products of a gene coding for an ACEI/BPP-C-type natriuretic peptide (CNP) precursor. In the genes from Bothrops jararaca and Gloydius blomhoffii, ACEI/BPP sequences are repeated. Sequencing of a cDNA clone from venom glands of Crotalus durissus collilineatus showed that two ACEIs/BPPs are located together at the N-terminus, but without repeats. An additional sequence for CNP was unexpectedly found at the C-terminus. Homologous genes for the ACEI/BPP-CNP precursor suggest that most crotaline venoms contain both ACEIs/BPPs and CNP. The sequence of ACEIs/BPPs is separated from the CNP sequence by a long spacer sequence. Previously, there was no evidence that this spacer actually coded any expressed peptides. Aird and Kaiser (1986, unpublished) previously isolated and sequenced a peptide of 11 residues (TPPAGPDVGPR) from Crotalus viridis viridis venom. In the present study, analysis of the cDNA clone from C. d. collilineatus revealed a nearly identical sequence in the ACEI/BPP-CNP spacer. Fractionation of the crude venom by reverse phase HPLC (C 18), and analysis of the fractions by mass spectrometry (MS) indicated a component of 1020.5 Da. Amino acid sequencing by MS/MS confirmed that C. d. collilineatus venom contains the peptide TPPAGPDGGPR. Its high proline content and paired proline residues are typical of venom hypotensive peptides, although it lacks the usual N-terminal pyroglutamate. It has no demonstrable hypotensive activity when injected intravenously in rats; however, its occurrence in the venoms of dissimilar species suggests that its presence is not accidental. Evidence suggests that these novel toxins probably activate anaphylatoxin C3a receptors.

Effects of Crotalus durissus collilineatus venom in the isolated rat kidney

Ophidian accidents caused by the subspecies Crotalus durissus are responsible for high morbity and mortality rates. Acute renal failure is a common complication observed in these accidents. The aim of the present study was to investigate the renal effects promoted by the venom of C. d. collilineatus and its fractions, crotoxin and phospholipase A 2. C. d. collilineatus (Cdc; 30 μg mL −1), crotoxin (CTX; 10 μg mL −1) and phospholipase A 2 (PLA 2; 10 μg mL −1) were tested in isolated rat kidney. The first 30 min of each experiment were used as an internal control and Cdc or its fractions, CTX and PLA 2 were added to the system after this period. All experiments lasted 120 min. The venom of Cdc decreased perfusion pressure (PP; control 120=110.3±3.69 mmHg; Cdc 120=96.7±8.1 mmHg), renal vascular resistance (RVR; control 120=6.42±0.78 mmHg mL g −1 min −1; Cdc 120=4.8±0.56 mmHg/mL g −1 min −1), urinary flow (UF; control 120=0.19±0.03 mL g −1 min −1; Cdc 120=0.12±0.01 mL g −1 min −1), and glomerular filtration rate (GFR; control 120=0.79±0.07 mL g −1 min −1; Cdc 120=0.53±0.09 mL g −1 min −1), but had no effect on the percent of sodium tubular transport (%TNa +), percent of chloride tubular transport (%TK +) and percent of potassium tubular transport (%TCl −). CTX and PLA 2 reduced the GFR, while UF, PP and RVR remained stable during the full 120 min of perfusion. Crotoxin administration also diminished the %TK + (control 120=69.94±6.49; CTX 120=33.28±4.78) and %TCl − (control 120=79.53±2.67; CTX 120=64.62±6.93). PLA 2 reduced the %TK +, but exerted no effect on the %TNa + or on that of TCl −. In conclusion, the C. d. collilineatus venom altered the renal functional parameters evaluated. We suggest that crotoxin and phospholipase A 2 were involved in this process, since the renal effects observed would be due to the synergistic action of the components of the venom.

Biological and Structural Characterization of a New PLA2 from the Crotalus durissus collilineatus Venom

In the present article we report on the biological characterization and amino acid sequence of a new basic Phospholipases A2 (PLA2) isolated from the Crotalus durissus collilineatus venom (Cdcolli F6), which showed the presence of 122 amino acid residues with a pI value of 8.3, molecular mass of 14 kDa and revealed an amino acid sequence identity of 80% with crotalic PLA2s such as Mojave B, Cdt F15, and CROATOX. This homology, however, dropped to 50% if compared to other sources of PLA2s such as from the Bothrops snake venom. Also, this PLA2 induced myonecrosis, although this effect was lower than that of BthTx-I or whole crotoxin and it was able to induce a strong blockage effect on the chick biventer neuromuscular preparation, independently of the presence of the acid subunid (crotapotin). The neurotoxic effect was strongly reduced by pre-incubation with heparin or with anhydrous acetic acid and p-BPB showed a similar reduction. The p-BPB did not reduce significantly the myotoxic activity induced by the PLA2, but the anhydrous acetic acid treatment and the pre-incubation of PLA2 with heparin reduced significantly its effects. This protein showed a strong antimicrobial activity against Xanthomonas axonopodis passiforae (Gram-negative), which was drastically reduced by incubation of this PLA2 with p-BPB, but this effect was marginally reduced after treatment with anhydrous acetic acid. Our findings here allow to speculate that basic amino acid residues on the C-terminal and molecular regions near catalytic site regions such as Calcium binding loop or beta-wing region may be involved in the binding of this PLA2 to the molecular receptor to induce the neurotoxic effect. The bactericidal effect, however, was completely dependent on the enzymatic activity of this protein.

Isolation and preliminary enzymatic characterization of a novel PLA2 from Crotalus durissus collilineatus venom.

A crotoxin homolog was purified from the Crotalus durissus collilineatus venom using molecular exclusion and reverse-phase HPLC. This crotoxin contained one PLA2 (Cdcolli III F6) and four crotapotin isoforms, whereas crotoxin from Crotalus durissus terrificus venom had three PLA2 iso forms and two crotapotin isoforms. SDS-PAGE showed that the C. d. collilineatus PLA2 and crotapotin had relative molecular mass of 15 and 9 kDa, respectively. Neither the PLA2 (Cdcolli III F6) nor the crotapotins (Cdcolli III F3 and F4) had any neurotoxicity in mouse phrenic nerve-diaphragm preparations when tested alone. However, when PLA2 and crotapotin were coincubated before testing, the neurotoxicity was restored to a level similar to test in the venom in native crotoxin. The two crotapotins (Cdcolli III F3 and F4) differed in their ability to inhibit PLA2 activity, perhaps because of variations in their affinities for this enzyme. Cdcolli III F6 showed allosteric enzymatic behavior, with maximal activity at pH 8.3 and 36 degrees C. Full PLA2 activity required the presence of a low Ca2+ concentration and was inhibited by Cu2+ and Zn2+ and by Cu2+ and Mg2+ in the presence and absence of Ca2+, respectively. These results indicate that crotoxin from C. d. collineatus venom is very similar enzymatically to crotoxin from C. d. terrificus.

Isolation and characterization of a convulxin-like protein from Crotalus durissus collilineatus venom.

A convulxin (Cvx)-like protein was isolated from Crotalus durissus collilineatus venom by a combination of molecular exclusion and reversed-phase HPLC chromatographies. The molecular mass of the Cvx-like protein in the absence and presence of DTT was 78 kDa and 12-13 kDa, respectively. The Cvx-like protein consisted of two nonidentical polypeptide chains (alpha and beta). The N-terminal amino-acid sequences of the alpha and beta subunits were GLHCPSDWYAYDGHCYKIFNEEMNWED and GFCCPSHWSSYSRYCYKFFSQEMNWEDAEK, respectively, with both subunits having a high content of Glu, Ser, Cys, and Asp. The Cvx-like protein showed high homology with other venom C-type lectins, but had low hemagglutinating activity on intact and trypsinized erythrocytes. The Cvx-like protein stimulated insulin receptor phosphorylation and potentiated insulin secretion from isolated islets in the presence of sub- (2.8 mM) or supra-physiological (16.7 mM) glucose concentrations. These results suggest that the increase in insulin secretion induced by Cvx-like protein may be mediated by a protein tyrosine kinase-dependent pathway and may involve other membrane receptors, such as GP VI or Scr family proteins.

Metabolism of amino acids by the perfused rat kidney.

ARTICLESMetabolism of amino acids by the perfused rat kidneyRF PittsRF PittsSearch for more papers by this authorPublished Online:01 Apr 1971https://doi.org/10.1152/ajplegacy.1971.220.4.862MoreSectionsPDF (1 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformation Cited ByAn Update on Kidney Ammonium Transport Along the NephronAdvances in Kidney Disease and Health, Vol. 30, No. 2Ammonia Transporters and Their Role in Acid-Base BalanceI. David Weiner and Jill W. Verlander1 February 2017 | Physiological Reviews, Vol. 97, No. 2Rh vs pH: the role of Rhesus glycoproteins in renal ammonia excretion during metabolic acidosis in a freshwater teleost fish1 January 2014 | Journal of Experimental Biology, Vol. 45Renal and vascular effects of the natriuretic peptide isolated from Crotalus durissus cascavella venomToxicon, Vol. 52, No. 7Purification and biological effects of l-amino acid oxidase isolated from Bothrops insularis venomToxicon, Vol. 51, No. 2Purification and biological activity of the thrombin-like substance isolated from Bothrops insularis venomToxicon, Vol. 49, No. 3The role of indomethacin and tezosentan on renal effects induced by Bothrops moojeni Lys49 myotoxin IToxicon, Vol. 47, No. 8Effects of Crotalus durissus collilineatus venom in the isolated rat kidneyToxicon, Vol. 47, No. 3A new C-type animal lectin isolated from Bothrops pirajai is responsible for the snake venom major effects in the isolated kidneyThe International Journal of Biochemistry & Cell Biology, Vol. 37, No. 1Renal metabolism of amino acids: its role in interorgan amino acid exchangeThe American Journal of Clinical Nutrition, Vol. 79, No. 2The renal effects of Bothrops jararacussu venom and the role of PLA2 and PAF blockersToxicon, Vol. 39, No. 12Glomerular Effects of Cholera Toxin in Isolated Perfused Rat Kidney: A Potential Role for Platelet Activating FactorPharmacology & Toxicology, Vol. 85, No. 5Effects of microcystin-LR in isolated perfused rat kidneyBrazilian Journal of Medical and Biological Research, Vol. 32, No. 8Effects of Crotalus durissus cascavella venom in the isolated rat kidneyToxicon, Vol. 36, No. 10Human kidney and liver gluconeogenesis: evidence for organ substrate selectivityMichael Stumvoll, Christian Meyer, Gabriele Perriello, Maryl Kreider, Stephen Welle, and John Gerich1 May 1998 | American Journal of Physiology-Endocrinology and Metabolism, Vol. 274, No. 5Promoting Effect of Monosodium Aspartate, But Not Glycine, on Renal Pelvis and Urinary Bladder Carcinogenesis in Rat Induced by N-Butyl-N-(4-Hydroxybutyl)nitrosamine2 July 2016 | Toxicologic Pathology, Vol. 24, No. 5Renal Ammonia Production and Excretion1 January 2011Effects du tumor necrosis factor (TNF) sur le métabolisme des acides aminés et des protéinesNutrition Clinique et Métabolisme, Vol. 4, No. 2Contribution of amino acids in protective solutions to postischemic functional recovery of canine kidneysResearch in Experimental Medicine, Vol. 189, No. 6Physiologic importance of glutamineMetabolism, Vol. 38, No. 8Inter-organ metabolism of amino acids in vivoDiabetes / Metabolism Reviews, Vol. 5, No. 3Renal MetabolismGlucose metabolism in renal tubular functionKidney International, Vol. 29, No. 1Early events in the initiation of ammonia formation in kidney.Journal of Biological Chemistry, Vol. 258, No. 5Molecular specificity of the tubular resorption of ?acidic? amino acidsPfl�gers Archiv European Journal of Physiology, Vol. 396, No. 3Influence of pyruvate on ammonia metabolism by renal cortical mitochondriaKidney International, Vol. 22, No. 3Regulation of renal ammoniagenesis during acidosis: The pyridine nucleotide hypothesis revisitedLife Sciences, Vol. 27, No. 24Effect of L-leucine on p-aminohippurate accumulation by mammalian renal cortical slicesBiochimica et Biophysica Acta (BBA) - General Subjects, Vol. 587, No. 1Alanine transport by the isolated perfused rat kidneyLife Sciences, Vol. 18, No. 11Renal transport of amino acids21 June 2005Renal Transport of Amino Acids More from this issue > Volume 220Issue 4April 1971Pages 862-867 Copyright & PermissionsCopyright © 1971 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1971.220.4.862PubMed5551140History Published online 1 April 1971 Published in print 1 April 1971 Metrics

Micropuncture study of isolated perfused rat kidney.

ARTICLESMicropuncture study of isolated perfused rat kidneyJ Bahlmann, G Giebisch, B Ochwadt, and W SchoeppeJ Bahlmann, G Giebisch, B Ochwadt, and W SchoeppePublished Online:01 Jan 1967https://doi.org/10.1152/ajplegacy.1967.212.1.77MoreSectionsPDF (1 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformation Cited ByThe α7-nAChR/heme oxygenase-1/carbon monoxide pathway mediates the nicotine counteraction of renal inflammation and vasoconstrictor hyporeactivity in endotoxic male rats2 January 2020 | Inflammation Research, Vol. 69, No. 2A Long Affair with Renal TubulesAnnual Review of Physiology, Vol. 73, No. 1Application of Isolated Organ Perfusion Techniques in Toxicology21 June 2013Effects of Crotalus durissus collilineatus venom in the isolated rat kidneyToxicon, Vol. 47, No. 3Action of anti-bothropic factor isolated from Didelphis marsupialis on renal effects of Bothrops erythromelas venomToxicon, Vol. 46, No. 6Thalidomide and pentoxifylline block the renal effects of supernatants of macrophages activated with Crotalus durissus cascavella venomBrazilian Journal of Medical and Biological Research, Vol. 37, No. 10Effects of Thalassophryne nattereri fish venom in isolated perfused rat kidneyToxicon, Vol. 42, No. 5Structural and biological characterization of a crotapotin isoform isolated from Crotalus durissus cascavella venomToxicon, Vol. 42, No. 1Renal effects of supernatant from rat peritoneal macrophages activated by microcystin-LR: role protein mediatorsToxicon, Vol. 41, No. 3Renal Effects of Supernatant from Macrophages Activated by Crotalus durissus cascavella Venom: The Role of Phospholipase A 2 and Cyclooxygenase4 April 2003 | Pharmacology & Toxicology, Vol. 92, No. 1Determination of Crotalus durissus cascavella venom components that induce renal toxicity in isolated rat kidneysToxicon, Vol. 40, No. 8Actions of Crotalus durissus terrificus venom and crotoxin on the isolated rat kidneyBrazilian Journal of Medical and Biological Research, Vol. 34, No. 10The role of phospholipase A 2 and cyclooxygenase in renal toxicity induced by microcystin-LRToxicon, Vol. 39, No. 5Pretransplantation assessment of renal viability with NADH fluorimetryKidney International, Vol. 57, No. 2Glomerular Effects of Cholera Toxin in Isolated Perfused Rat Kidney: A Potential Role for Platelet Activating FactorPharmacology & Toxicology, Vol. 85, No. 5Effects of microcystin-LR in isolated perfused rat kidneyBrazilian Journal of Medical and Biological Research, Vol. 32, No. 8Nadh Fluorimetry to Predict Ischemic Injury in Transplant KidneysEffects of Crotalus durissus cascavella venom in the isolated rat kidneyToxicon, Vol. 36, No. 10Renal Micropuncture Techniques1 January 2011The Effects of Escherichia coli Heat-Stable Enterotoxin in Renal Sodium Tubular TransportPharmacology & Toxicology, Vol. 70, No. 3Use of the Isolated Perfused Kidney as a Tool in Drug Disposition Studies22 September 2008 | Drug Metabolism Reviews, Vol. 14, No. 5Methodology for Study of Isolated Perfused Rat Kidney in VitroThe O2 Supply of the Isolated Cell-Free Perfused Rat KidneyMicrocirculation and Tubular Urine Flow in the Mammalian Kidney Cortex (in vivo Microscopy)The Mechanism of Action of Mercuric Chloride on the Isolated Perfused Rat Kidney2 March 2011 | European Journal of Clinical Investigation, Vol. 5, No. 4The Mechanism of Action of Mercuric Chloride on the Isolated Perfused Rat KidneyEuropean Journal of Clinical Investigation, Vol. 5, No. 1The basic requirements for the function of the isolated cell free perfused rat kidneyPfl�gers Archiv European Journal of Physiology, Vol. 354, No. 4[1] The perfused rat kidneyThe isolated perfused kidney: Possibilities, limitations and resultsKidney International, Vol. 7, No. 1Improved net sodium transport of the isolated rat kidneyZeitschrift für Die Gesamte Experimentelle Medizin einschließlich experimentelle Chirurgie, Vol. 156, No. 4Proximal Tubular Malfunction as a Mechanism for Diuresis after Renal HomotransplantationNew England Journal of Medicine, Vol. 278, No. 9The Influence of the Neurohypophysial Hormones and Similar Polypeptides on the Kidneys More from this issue > Volume 212Issue 1January 1967Pages 77-82 Copyright & PermissionsCopyright © 1967 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1967.212.1.77PubMed6016017History Published online 1 January 1967 Published in print 1 January 1967 Metrics