RESUMO
The food enzyme pullulanase (pullulan 6-α-glucanohydrolase; EC 3.2.1.41) is produced with the non-genetically modified Pullulanibacillus naganoensis strain AE-PL by Amano Enzyme Inc. A safety evaluation of this food enzyme was made previously, in which EFSA concluded that this food enzyme did not give rise to safety concerns when used in one food manufacturing process. Subsequently, the applicant has requested to extend its use to include seven additional processes and to revise the previous use level. In this assessment, EFSA updated the safety evaluation of this food enzyme when used in a total of eight food manufacturing processes. As the food enzyme-total organic solids (TOS) are not carried into the final foods in two food manufacturing processes, the dietary exposure was estimated only for the remaining six processes. The dietary exposure was calculated to be up to 0.004 mg TOS/kg body weight (bw) per day in European populations. The Panel evaluated the repeated dose 90-day oral toxicity study in rats submitted in the previous application and identified a no observed adverse effect level of 643 mg TOS/kg bw per day, the highest dose tested. When compared with the calculated dietary exposure, this resulted in a margin of exposure of at least 160,750. Based on the data provided for the previous evaluation and the revised margin of exposure in the present evaluation, the Panel concluded that this food enzyme does not give rise to safety concerns under the revised intended conditions of use.
RESUMO
The food enzyme inulinase (1-ß-d-fructan fructanohydrolase; EC 3.2.1.7) is produced with the non-genetically modified Aspergillus welwitschiae strain NZYM-KF by Novozymes A/S. The food enzyme is free from viable cells of the production organism. It is intended to be used in the processing of fructo-polysaccharides for the production of fructo-oligosaccharides. Since residual amounts of total organic solids (TOS) are removed during the food manufacturing process, toxicological studies other than allergenicity were considered unnecessary and dietary exposure was not calculated. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and two matches with tomato allergens were found. The Panel considered that the risk of allergic reactions upon dietary exposure to this food enzyme, particularly in individuals sensitised to tomato, cannot be excluded, but is expected not to exceed that of tomato. As the prevalence of allergic reactions to tomato is low, also the likelihood of such reactions to occur to the food enzyme is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.
RESUMO
The food enzyme with phospholipase A1 (phosphatidycholine 1-acylhydrolase, EC 3.1.1.32) and lysophospholipase (2-lysophosphatidylcholine acylhydrolase, EC 3.1.1.5) activities is produced with the genetically modified Aspergillus niger strain PLN by DSM. The genetic modifications do not give rise to safety concerns. The food enzyme is free from viable cells of the production organism and its DNA. It is intended to be used for the production of refined edible fats and oils by degumming. Since residual amounts of total organic solids are removed during this process, dietary exposure was not calculated and toxicological studies were considered unnecessary for the assessment of this food enzyme. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no matches were found. The Panel considered that the risk of allergic reactions upon dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.
RESUMO
The food enzyme phosphodiesterase I (oligonucleotide 5'-nucleotidohydrolase; EC 3.1.4.1) is produced with the non-genetically modified Leptographium procerum strain FDA by DSM Food Specialties B.V. The food enzyme is free from viable cells of the production organism. It is intended to be used in the processing of yeast and yeast products. Dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.171 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1000 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 5848. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
The food enzyme glutaminase (l-glutamine amidohydrolase EC 3.5.1.2) is produced with the genetically modified Bacillus licheniformis strain NZYM-JQ by Novozymes A/S. The genetic modifications do not give rise to safety concerns. The production strain met the requirements for the qualified presumption of safety (QPS). The food enzyme is free from viable cells of the production organism and its DNA. The enzyme under assessment is intended to be used in six food manufacturing processes. Dietary exposure was estimated to be up to 0.148 mg TOS/kg body weight per day in European populations. Given the QPS status of the production strain and the absence of concern resulting from the food enzyme manufacturing process, toxicological studies were not considered necessary. A search was made for the similarity of the amino acid sequence to those of known allergens and one match with a pollen allergen was found. The Panel considered that the risk of allergic reactions by dietary exposure cannot be excluded, particularly for individuals sensitised to birch and oak pollen. The Panel concluded that the food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
This assessment addresses a food enzyme preparation consisting of the immobilised non-viable cells of the non-genetically modified bacterium identified by the applicant (Samyang Corporation) as Microbacterium foliorum strain SYG27B. This strain produces the enzyme D-psicose 3-epimerase (EC 5.1.3.30). The food enzyme preparation is used for the isomerisation of fructose to produce the speciality carbohydrate D-allulose (synonym D-psicose). Since the hazard identification and characterisation could not be made and the identity of the production organism could not be established, the Panel was unable to complete the assessment of this food enzyme preparation containing D-psicose 3-epimerase.
RESUMO
The food enzyme mucorpepsin (EC 3.4.23.23) is produced with the non-genetically modified Rhizomucor miehei strain FRO by DSM Food Specialties B.V. The enzyme can be chemically modified to produce a thermolabile form. The food enzyme is free from viable cells of the production organism. It is intended to be used in three food manufacturing processes: processing of dairy products for the production of (1) cheese, (2) edible rennet casein, (3) fermented dairy products. Dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to about 0.072 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 2000 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, results in a margin of exposure of at least 27,778. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and five matches were found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but is considered low, except for individuals sensitised to mustard proteins, for whom the risk will not exceed that of mustard consumption. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
The food enzyme ß-galactosidase (ß-d-galactoside galactohydrolase; EC 3.2.1.23) is produced with the non-genetically modified Papiliotrema terrestris strain AE-BLC by Amano Enzyme Inc. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in the production of galacto-oligosaccharides (GOS) from lactose. Dietary exposure to the food enzyme-total organic solids (TOS) was estimated to be up to 0.441 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1800 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 4082. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
The food enzyme endo-1,4-ß-xylanase (4-ß-d-xylan xylanohydrolase; EC 3.2.1.8) is produced with the non-genetically modified Trichoderma citrinoviride strain 278 by Kerry Ingredients & Flavours Ltd. The food enzyme was considered free from viable cells of the production organism. It is intended to be used in eight food manufacturing processes: processing of cereals and other grains for the production of baked products; production of cereal-based products other than baked, brewed products, starch and gluten fractions, distilled alcohol; processing of fruits and vegetables for the production of juices, wine and wine vinegar and processing of yeast and yeast products. Since residual amounts of total organic solids (TOS) are removed during two processes, dietary exposure was only calculated for the remaining six food manufacturing processes. Exposure was estimated to be up to 4.808 mg TOS/kg body weight (bw) per day in European populations. The Panel was unable to reach a conclusion on genotoxicity and systemic toxicity. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure cannot be excluded (except for distilled alcohol production), but the likelihood is low. In the absence of an acceptable full set of toxicological data, the Panel was unable to complete the safety assessment of the food enzyme.
RESUMO
The food enzyme catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) is produced with the non-genetically modified Aspergillus tubingensis strain AE-CN by Amano Enzyme Inc. The absence of viable cells of the production organism in the food enzyme was not demonstrated. The food enzyme is intended to be used in five food manufacturing processes: production of baked products, processing of egg and egg products, production of fruit and vegetable products other than juices, production of cheese and production of fish roes. The dietary exposure to the food enzyme total organic solids (TOS) was estimated to be up to 0.325 mg TOS/kg body weight (bw) per day in European populations. The results of the in vitro genotoxicity studies indicated the presence of a clastogenic agent in the food enzyme which could not be dismissed due to limitations in the in vivo studies. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 323 mg TOS/kg bw per day, the highest dose tested. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and one match was found. The Panel considered that the risk of allergic reactions by dietary exposure cannot be excluded, but the likelihood is low. Because of the results of the genotoxicity studies, and as the absence of viable cells from the production strain was not demonstrated, the Panel was unable to establish the safety of the food enzyme.
RESUMO
The food enzyme α-l-rhamnosidase (α-l-rhamnoside rhamnohydrolase; EC 3.2.1.40) is produced with the non-genetically modified Penicillium adametzii strain AE-HP by Amano Enzymes Inc. The food enzyme is considered free from viable cells of the production organism. It is intended to be used in the processing of fruits and vegetables for the production of juices and other fruit products. The dietary exposure to the food enzyme-TOS was estimated to be up to 0.022 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 300 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, results in a margin of exposure of at least 13,636. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and no match was found. The Panel considered that a risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
The food enzyme with the declared activities endo-polygalacturonase ((1-4)-α-D-galacturonan glycanohydrolase; EC 3.2.1.15) and pectin lyase ((1-4)-6-O-methyl-α-D-galacturonan lyase; EC 4.2.2.10) is produced with the non-genetically modified Aspergillus tubingensis strain NZYM-PE by Novozymes A/S. It is intended to be used in four food manufacturing processes: fruit and vegetable processing for juice production, fruit and vegetable processing for products other than juices, refined olive oil production and wine and wine vinegar production. Since residual amounts of total organic solids (TOS) are removed during production, dietary exposure was not calculated for refined olive oil production. For the remaining three food processes, it was estimated to be up to 0.132 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level (NOAEL) of 1,430 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, resulted in a margin of exposure above 10,833. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and 13 matches were found, including one food allergen (papaya). The Panel considered that, under the intended conditions of use, the risk of allergic reactions upon dietary exposure to this food enzyme cannot be excluded, in particular for individuals sensitised to papaya, but that the risk will not exceed that of consumption of papaya. In addition, oral allergy reactions cannot be excluded in pollen-sensitised individuals. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns, under the intended conditions of use.
RESUMO
The food enzyme α-amylase (4-α-d-glucan glucanohydrolase; EC 3.2.1.1) is produced with the non-genetically modified Aspergillus niger strain AS 29-286 by Shin Nihon Chemical Co., Ltd. The food enzyme is considered free from viable cells of the production organism. It is intended to be used in seven food manufacturing processes: baking processes, fruit and vegetable processing for juice production, fruit and vegetable processing for products other than juices, distilled alcohol production, starch processing for the production of maltodextrins, brewing processes and non-wine vinegar production. Since residual amounts of total organic solids (TOS) are removed during distilled alcohol production and starch processing for the production of maltodextrins, dietary exposure was calculated only for the remaining five food manufacturing processes. It was estimated to be up to 2.158 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,774 mg TOS/kg bw per day, the highest dose tested, which when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 822. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and four matches with respiratory allergens were found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions upon dietary exposure cannot be excluded, but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
The food enzyme glucan 1,4-α-glucosidase (4-α-d-glucan α-glucohydrolase; EC 3.2.1.3) is produced with the non-genetically modified Aspergillus niger strain NZYM-BO by Novozymes A/S. It was considered free from viable cells of the production organism. It is intended to be used in seven food manufacturing processes: baking processes, brewing processes, cereal-based processes, distilled alcohol production, fruit and vegetable processing for juice production, production of dairy analogues and starch processing for the production of glucose syrups and other starch hydrolysates. Since residual amounts of total organic solids (TOS) are removed by distillation and during starch processing, dietary exposure was not calculated for these two food manufacturing processes. For the remaining five food manufacturing processes, dietary exposure to the food enzyme-TOS was estimated to be up to 2.97 mg TOS/kg body weight (bw) per day in European populations. Genotoxicity tests did not indicate a safety concern. The systemic toxicity was assessed by means of a repeated dose 90-day oral toxicity study in rats. The Panel identified a no observed adverse effect level of 1,920 mg TOS/kg bw per day, the highest dose tested, which, when compared with the estimated dietary exposure, resulted in a margin of exposure of at least 646. A search for the similarity of the amino acid sequence of the food enzyme to known allergens was made and one match with a respiratory allergen was found. The Panel considered that, under the intended conditions of use, the risk of allergic reactions by dietary exposure to this food enzyme cannot be excluded (except for distilled alcohol production), but the likelihood is low. Based on the data provided, the Panel concluded that this food enzyme does not give rise to safety concerns under the intended conditions of use.
RESUMO
Highly Al-substituted C-coated Na3V2-xAlx(PO4)3 compounds with a sodium superionic conductor structure are synthesized by a single and easily scalable sol-gel route. The effect of the experimental conditions is examined. Their structural, chemical, and morphological features are described. The first-principles method is used to determine the theoretical voltage vs Na content profile during Na extraction. The electrochemical Na extraction is characterized by the presence of two plateaus. The first one at ca. 3.4 V is assigned to the V4+/V3+ redox pair and shows good cyclability. The second plateau at ca. 3.9-4.0 V can be assigned to the V5+/V4+ pair, as evidenced by X-ray photoelectron spectroscopy. This second plateau is less reversible during further discharge.
RESUMO
Directive 2010/63/EU introduced requirements for the classification of the severity of procedures to be applied during the project authorisation process to use animals in scientific procedures and also to report actual severity experienced by each animal used in such procedures. These requirements offer opportunities during the design, conduct and reporting of procedures to consider the adverse effects of procedures and how these can be reduced to minimize the welfare consequences for the animals. Better recording and reporting of adverse effects should also help in highlighting priorities for refinement of future similar procedures and benchmarking good practice. Reporting of actual severity should help inform the public of the relative severity of different areas of scientific research and, over time, may show trends regarding refinement. Consistency of assignment of severity categories across Member States is a key requirement, particularly if re-use is considered, or the safeguard clause is to be invoked. The examples of severity classification given in Annex VIII are limited in number, and have little descriptive power to aid assignment. Additionally, the examples given often relate to the procedure and do not attempt to assess the outcome, such as adverse effects that may occur. The aim of this report is to deliver guidance on the assignment of severity, both prospectively and at the end of a procedure. A number of animal models, in current use, have been used to illustrate the severity assessment process from inception of the project, through monitoring during the course of the procedure to the final assessment of actual severity at the end of the procedure (Appendix 1).
Assuntos
Bem-Estar do Animal , Animais de Laboratório , Modelos Animais , Bem-Estar do Animal/normas , Animais , Animais de Laboratório/lesões , Métodos , Estudos Retrospectivos , Índices de Gravidade do TraumaRESUMO
Brain trimming through defined neuroanatomical landmarks is recommended to obtain consistent sections in rat toxicity studies. In this article, we describe a matrix-guided trimming protocol that uses channels to reproduce coronal levels of anatomical landmarks. Both setup phase and validation study were performed on Han Wistar male rats (Crl:WI(Han)), 10-week-old, with bodyweight of 298 ± 29 (SD) g, using a matrix (ASI-Instruments(®), Houston, TX) fitted for brains of rats with 200 to 400 g bodyweight. In the setup phase, we identified eight channels, that is, 6, 8, 10, 12, 14, 16, 19, and 21, matching the recommended landmarks midway to the optic chiasm, frontal pole, optic chiasm, infundibulum, mamillary bodies, midbrain, middle cerebellum, and posterior cerebellum, respectively. In the validation study, we trimmed the immersion-fixed brains of 60 rats using the selected channels to determine how consistently the channels reproduced anatomical landmarks. Percentage of success (i.e., presence of expected targets for each level) ranged from 89 to 100%. Where 100% success was not achieved, it was noted that the shift in brain trimming was toward the caudal pole. In conclusion, we developed and validated a trimming protocol for the rat brain that allow comparable extensiveness, homology, and relevance of coronal sections as the landmark-guided trimming with the advantage of being quickly learned by technicians.
Assuntos
Encéfalo/anatomia & histologia , Encéfalo/ultraestrutura , Neuroanatomia/métodos , Toxicologia/métodos , Pontos de Referência Anatômicos , Animais , Corantes , Dissecação/métodos , Masculino , Tamanho do Órgão , Ratos , Ratos Wistar , Reprodutibilidade dos Testes , Fixação de TecidosRESUMO
AIM: in the present study, we report the circadian profiles of a wide panel of hormones measured in rats and common marmosets (Callithrix jacchus), under physiological conditions, paying special attention to minimising the stress imposed on the animals. MATERIALS AND METHODS: blood collections were performed over a 24-hour period for the analysis of stress and pituitary hormones, metabolic markers and cytokines from male cannulated rats connected to a fully automatic system, and healthy marmosets in which gender differences were also evaluated. RESULTS: in rats, a significant time effect was observed for corticosterone, prolactin (PRL), thyroid stimulating hormone (TSH), growth hormone, follicle-stimulating hormone, brain-derived neurotrophic factor, total ghrelin, insulin, leptin, insulin-like growth factor-1, adiponectin and interleukin-10. In marmosets, a significant time effect for cortisol, adrenocorticotropic hormone (ACTH), PRL and TSH, with gender effect for ACTH and PRL only, was observed. On the contrary, luteinizing hormone in the rat and active ghrelin, peptide YY, pancreatic polypeptide and gastric inhibitory polypeptide in the marmoset did not show any significant circadian variation. CONCLUSION: the present work confirmed that, due to time-of-day dependent modulation of hormones, circadian rhythmicity is relevant in physiological studies and should also be taken into consideration when performing pharmacological studies.
Assuntos
Ritmo Circadiano , Citocinas/sangue , Hormônios Peptídicos/sangue , Animais , Fator Neurotrófico Derivado do Encéfalo/sangue , Callithrix , Corticosterona/sangue , Feminino , Hidrocortisona/sangue , Fator de Crescimento Insulin-Like I/metabolismo , Masculino , Ratos , Ratos Sprague-Dawley , Especificidade da EspécieRESUMO
OBJECTIVE: The main objective of the study was to determine the effects of three different infusion rates of fentanyl and remifentanil on the minimum alveolar concentration (MAC) of isoflurane in the rat. A secondary objective was to assess the cardiovascular and respiratory effects of the two opioid drugs. ANIMAL POPULATION: Thirty-seven male Wistar rats were randomly allocated to one of six treatment groups. MATERIAL AND METHODS: For all treatment groups anaesthesia was induced with 5% isoflurane in oxygen using an induction chamber. A 14-gauge catheter was used for endotracheal intubation, and anaesthesia was maintained with isoflurane delivered in oxygen via a T-piece breathing system. A baseline determination of the minimum alveolar concentration of isoflurane (MACISO) was made for each animal. Fentanyl (15, 30, 60 micro g kg-1 hour-1) or remifentanil (60, 120, 240 micro g kg-1 hour-1) were infused intravenously into a previously cannulated tail vein. Thirty minutes after the infusion started, a second MACISO (MACISO+drug) was determined. The carotid artery was cannulated to monitor the arterial pressure and to take samples for arterial gas measurements. Cardiovascular (heart rate and arterial pressure) and respiratory (respiratory rate and presence/absence of apnoea) effects after opioid infusion were also recorded. RESULTS: Fentanyl (15, 30, 60 micro g kg-1 hour-1) and remifentanil (60, 120, 240 micro g kg-1 hour-1) similarly reduced isoflurane MAC in a dose-dependent fashion: by 10% at lower doses, 25% at medium doses and by 60% at higher doses of both the drugs. Both opioids reduced the respiratory rate in a similar way for all doses tested. No episodes of apnoea were recorded in the remifentanil groups, while administration of fentanyl resulted in apnoea in three animals (one at each dose level). The effects on the cardiovascular system were similar with both drugs. CONCLUSIONS: We conclude that the intraoperative use of remifentanil in the rat reduces the MAC of isoflurane, and that this anaesthetic sparing effect is dose-dependent and similar to that produced by fentanyl at the doses tested. CLINICAL RELEVANCE: The use of remifentanil during inhalant anaesthesia in the rat can be considered an intravenous alternative to fentanyl, providing similar reduction in isoflurane requirements. Due to its rapid offset, it is recommended that alternative pain relief be instituted before it is discontinued.
Assuntos
Anestésicos Inalatórios/farmacocinética , Fentanila/farmacologia , Isoflurano/farmacocinética , Pulmão/metabolismo , Piperidinas/farmacologia , Ratos/fisiologia , Analgésicos Opioides/administração & dosagem , Analgésicos Opioides/farmacologia , Anestesia/veterinária , Anestésicos Intravenosos/administração & dosagem , Anestésicos Intravenosos/farmacologia , Animais , Relação Dose-Resposta a Droga , Interações Medicamentosas , Fentanila/administração & dosagem , Infusões Intravenosas/veterinária , Masculino , Piperidinas/administração & dosagem , Ratos Wistar , RemifentanilRESUMO
This study was carried out to determine whether cyanoacrylate gel was suitable for use as a substitute for dental cement during brain implant surgery of rats. Intracerebroventricular (ICV) cannulations were performed in 24 rats by two surgeons, one with 3 years' experience in this type of surgery, and one novice, with only basic training performed on cadavers. Each surgeon prepared six randomly allocated animals using dental cement to secure the cannula and six with cyanoacrylate gel. Time to complete surgery was recorded. Wound healing was scored and body weight recorded for each animal every day for 7 days, then on day 14 after surgery. The use of gel led to an overall reduction in surgical time of 8 min (approximately 30%) per animal when compared with dental cement. No significant differences in the animals' recovery (wound healing and body weight) were found between surgeons or techniques. We find the use of cyanoacrylate gel to be a suitable and less time-consuming alternative to dental cement for ICV cannulations in rats.