Mitura K, Romanczuk M.
Department of General Surgery, Siedlce Hospital, Siedlce, Poland.
INTRODUCTION: Ectopic pregnancy may lead to massive haemorrhage, infertility or death. Prompt diagnosis and treatment are crucial to save patients who would otherwise die. Serum amylase and lipase measurements are known biochemical markers of pancreatic inflammation and a recognized finding that may help diagnose acute pancreatitis. To the best of our knowledge (Medline, Pubmed, Cochrane Library have been researched) the following study presents the first case of ruptured ectopic pregnancy accompanied by markedly elevated amylase and lipase levels mimicking acute pancreatitis ever reported.
CASE REPORT: A previously healthy, nulliparous 35-year-old woman was admitted to hospital with a 2-day history of abdominal pain and vomiting. Her last menstrual period was 7 weeks before presentation. At the admission, the patient was hemodynamically stable. The abdomen was soft with tenderness in its mesogastric area. Blood tests revealed markedly elevated activities of the pancreatic enzymes. Acute pancreatitis was the early clinical diagnosis and subsequent therapy was initiated. After 12 hours the condition of the patient suddenly worsened. She was clinically shocked with pallor, hypotension and tachycardia. Laboratory tests revealed anaemia and increased activities of pancreatic enzymes. An ultrasound examination demonstrated an accumulation of intraperitoneal fluid in the pelvis. Subsequently, the patient was subjected to immediate laparotomy. The peritoneal cavity contained large amount of blood. A cystic mass was found and extracted from the ruptured and bleeding right fallopian tube. Histological examination confirmed a rupture of an ectopic pregnancy of a 6-week-old foetus with an intact gestational sac. The patient made an uneventful recovery and was discharged from hospital after 8 days.
CONCLUSIONS: Our case proves that a misdiagnosed ruptured ectopic pregnancy in the event of elevated activities of pancreatic enzymes may lead to delayed diagnosis of haemorrhage to peritoneum, resulting in hemodynamic instability
Thursday
Monday
The level and clinical significance of pancreatic enzymes in survivors of acute paraquat poisoning
INTRODUCTION: Acute paraquat poisoning is often fatal. When ingested, paraquat affects multiple organs including the lung, gastrointestinal tract, pancreas, kidney, heart, and central nervous system. Our center previously found that initial pancreatic function was related to the prognosis of patients with acute paraquat poisoning. However, pancreatic injury after paraquat intoxication has been incompletely studied.
METHODS: This study analyzed the clinical outcome and extent of pancreatic injury in 34 survivors of acute paraquat poisoning. Paraquat exposure was assessed based on a quantitative measure of the plasma level of paraquat by high-performance liquid chromatography. The subsequent variations in the level of pancreatic enzymes, clinical symptoms, and abdominal computed tomography were obtained. Outcomes after acute paraquat poisoning were categorized as pancreatic enzyme elevation group (elevation group: amylase >160 IU/L and lipase >100 IU/L) and nonelevation group.
RESULTS: Pancreatic enzyme elevations occurred in seven cases (20.6%), and the level of pancreatic enzymes peaked at day 7. The elevation in pancreatic enzymes after paraquat ingestion was positively correlated with the plasma paraquat level (p < 0.05 at days 4 and 7). Creatinine was higher in the elevation group. Abdominal computed tomography of the seven cases showed no evidence of pancreatitis, and significant abdominal pain was not observed.
DISCUSSION: Pancreatic enzyme elevation reflects the systemic toxicity and multiorgan involvement following acute paraquat poisoning. CONCLUSIONS: Pancreatic injury was subtle and the elevation of pancreatic enzymes in survivors is clinically benign.
Gil HW, Yang JO, Lee EY, Hong SY.
Department of Internal Medicine, Cheonan Hospital, Soonchunhyang University, Cheonan, Republic of Korea
METHODS: This study analyzed the clinical outcome and extent of pancreatic injury in 34 survivors of acute paraquat poisoning. Paraquat exposure was assessed based on a quantitative measure of the plasma level of paraquat by high-performance liquid chromatography. The subsequent variations in the level of pancreatic enzymes, clinical symptoms, and abdominal computed tomography were obtained. Outcomes after acute paraquat poisoning were categorized as pancreatic enzyme elevation group (elevation group: amylase >160 IU/L and lipase >100 IU/L) and nonelevation group.
RESULTS: Pancreatic enzyme elevations occurred in seven cases (20.6%), and the level of pancreatic enzymes peaked at day 7. The elevation in pancreatic enzymes after paraquat ingestion was positively correlated with the plasma paraquat level (p < 0.05 at days 4 and 7). Creatinine was higher in the elevation group. Abdominal computed tomography of the seven cases showed no evidence of pancreatitis, and significant abdominal pain was not observed.
DISCUSSION: Pancreatic enzyme elevation reflects the systemic toxicity and multiorgan involvement following acute paraquat poisoning. CONCLUSIONS: Pancreatic injury was subtle and the elevation of pancreatic enzymes in survivors is clinically benign.
Gil HW, Yang JO, Lee EY, Hong SY.
Department of Internal Medicine, Cheonan Hospital, Soonchunhyang University, Cheonan, Republic of Korea
Tuesday
Amylase and lipase measurements in paediatric patients with traumatic pancreatic injuries.
Department of Paediatrics, University of Hawaii John A. Burns School of Medicine, Honolulu, HI 96826, United States. WMatsuno@Creighton.edu
INTRODUCTION: Pancreatic injuries occur in up to 10% of paediatric patients who suffer blunt trauma. Initial amylase and lipase measurements have not been helpful as a screening tool to detect pancreatic injuries. However, one primarily adult study suggests that a delayed measurement may be useful. MATERIALS AND METHODS: A retrospective chart review was conducted of patients admitted to a Level I paediatric trauma centre from April 1996 to November 2006 with traumatic pancreatic injuries.
RESULTS: The trauma database identified 51 patients with traumatic pancreatic injuries. Inclusion and exclusion criteria were met by 26 patients. Patients with initial amylase and lipase levels measured greater than 2h post-injury were more consistently elevated compared to those patients who had levels measured at 2h or less post-injury. There was a significant association between time of measurement and an increased amylase level (p=0.012). No significant association was found for lipase measurements (p=0.178).
DISCUSSION AND CONCLUSIONS: In children with blunt pancreatic injury, elevated serum amylase levels were seen in a significantly higher percentage of patients with initial measurements at greater than 2h post-injury compared to those measured at 2h or less. Lipase measurements demonstrated a similar trend. Delayed amylase and lipase measurements may be helpful to detect pancreatic injuries, but further study is needed.
INTRODUCTION: Pancreatic injuries occur in up to 10% of paediatric patients who suffer blunt trauma. Initial amylase and lipase measurements have not been helpful as a screening tool to detect pancreatic injuries. However, one primarily adult study suggests that a delayed measurement may be useful. MATERIALS AND METHODS: A retrospective chart review was conducted of patients admitted to a Level I paediatric trauma centre from April 1996 to November 2006 with traumatic pancreatic injuries.
RESULTS: The trauma database identified 51 patients with traumatic pancreatic injuries. Inclusion and exclusion criteria were met by 26 patients. Patients with initial amylase and lipase levels measured greater than 2h post-injury were more consistently elevated compared to those patients who had levels measured at 2h or less post-injury. There was a significant association between time of measurement and an increased amylase level (p=0.012). No significant association was found for lipase measurements (p=0.178).
DISCUSSION AND CONCLUSIONS: In children with blunt pancreatic injury, elevated serum amylase levels were seen in a significantly higher percentage of patients with initial measurements at greater than 2h post-injury compared to those measured at 2h or less. Lipase measurements demonstrated a similar trend. Delayed amylase and lipase measurements may be helpful to detect pancreatic injuries, but further study is needed.
Thursday
The effects of a new human leukocyte elastase inhibitor (recombinant guamerin) on cerulein-induced pancreatitis in rats
Background
Pancreatic and neutrophil elastase can aggravate or induce acute pancreatitis. Although increased elastase levels in the plasma of pancreatitis patients and animal models have been reported, the mechanism by which elastase is involved in the pathogenesis of acute pancreatitis has not yet been elucidated. We aimed to investigate the effects and the possible mechanism of a new human leukocyte elastase inhibitor (recombinant guamerin) in the treatment of cerulein-induced acute pancreatitis in rats.
Methods
Fifty Sprague–Dawley rats were divided into three groups: a saline-infused control group (I), a cerulein-induced acute pancreatitis group (II), and a cerulein plus guamerin infusion group (III). Guamerin (1–2 μmol/kg/h) was infused continuously in group III. The severity of pancreatitis was determined biochemically, histologically, and by cytokine changes between groups I, II and III.
Results
Significant differences in serum amylase , lipase , and pancreatic wet weight were observed in each group, respectively (group I; 2346.2 IU/L, 9.9 IU/L, 1.4 ± 0.3 g, group II; 13,596.8 IU/L, 7439.4 IU/L, 2.2 ± 0.5 g, group III; 9443.2 IU/L, 4516.3 IU/L, 1.7 ± 0.6 g). Serum IL-6 and TNF- [AU1]level peaked 1–4 h and 1–2 h. After the induction of pancreatitis, IL-6 and TNF- levels were decreased in group III than group II, (group I; 13.1/4.0 pg/mL, group II; 198.5/63.2 pg/mL, group III; 102.1/13.1 pg/mL), but no significant difference in IL-1β was observed. Histologic gradings and severity, such as vacuolization, inflammation, lobular disarray, and edema of the pancreas, were significantly lower in the cerulein plus guamerin infusion group III.
Conclusions
Recombinant guamerin, a new human leukocyte elastase inhibitor, may decrease the severity of pancreatitis and diminish pancreatic acinar cell injury by inhibition of neutrophilic infiltration and cytokine activation in the initial stage of cerulein-induced acute pancreatitis in rats.
ARTICLE
Pancreatic and neutrophil elastase can aggravate or induce acute pancreatitis. Although increased elastase levels in the plasma of pancreatitis patients and animal models have been reported, the mechanism by which elastase is involved in the pathogenesis of acute pancreatitis has not yet been elucidated. We aimed to investigate the effects and the possible mechanism of a new human leukocyte elastase inhibitor (recombinant guamerin) in the treatment of cerulein-induced acute pancreatitis in rats.
Methods
Fifty Sprague–Dawley rats were divided into three groups: a saline-infused control group (I), a cerulein-induced acute pancreatitis group (II), and a cerulein plus guamerin infusion group (III). Guamerin (1–2 μmol/kg/h) was infused continuously in group III. The severity of pancreatitis was determined biochemically, histologically, and by cytokine changes between groups I, II and III.
Results
Significant differences in serum amylase , lipase , and pancreatic wet weight were observed in each group, respectively (group I; 2346.2 IU/L, 9.9 IU/L, 1.4 ± 0.3 g, group II; 13,596.8 IU/L, 7439.4 IU/L, 2.2 ± 0.5 g, group III; 9443.2 IU/L, 4516.3 IU/L, 1.7 ± 0.6 g). Serum IL-6 and TNF- [AU1]level peaked 1–4 h and 1–2 h. After the induction of pancreatitis, IL-6 and TNF- levels were decreased in group III than group II, (group I; 13.1/4.0 pg/mL, group II; 198.5/63.2 pg/mL, group III; 102.1/13.1 pg/mL), but no significant difference in IL-1β was observed. Histologic gradings and severity, such as vacuolization, inflammation, lobular disarray, and edema of the pancreas, were significantly lower in the cerulein plus guamerin infusion group III.
Conclusions
Recombinant guamerin, a new human leukocyte elastase inhibitor, may decrease the severity of pancreatitis and diminish pancreatic acinar cell injury by inhibition of neutrophilic infiltration and cytokine activation in the initial stage of cerulein-induced acute pancreatitis in rats.
ARTICLE
Monday
Enzymatic preparation of chitooligosaccharides by commercial lipase
The effect of a commercial lipase on chitosan degradation was investigated. When four chitosans with various degrees of deacetylation were used as substrates, the lipase showed higher optimal pH toward chitosan with higher DD (degree of deacetylation). The optimal temperature of the lipase was 55 °C for all chitosans. The enzyme exhibited higher activity to chitosans which were 82.8% and 73.2% deacetylated. Kinetics experiments show that chitosans with DD of 82.8% and 73.2% which resulted in lower Km values had stronger affinity for the lipase. The chitosan hydrolysis carried out at 37 °C produced larger quantity of COS (chitooligosaccharides) than that at 55 °C when the reaction time was longer than 6 h, and COS yield of 24 h hydrolysis at 37 °C was 93.8%. Products analysis results demonstrate that the enzyme produced glucosamine and chitooligosaccharides with DP (degree of polymerization) of 2–6 and above, and it acted on chitosan in both exo- and endo-hydrolytic manner.
Dong-Xia Leea, Wen-Shui Xiaa, b, , and Jia-Li Zhang
ARTICLE
Dong-Xia Leea, Wen-Shui Xiaa, b, , and Jia-Li Zhang
ARTICLE
Bile-salt stimulated lipase in human milk binds DC-SIGN and inhibits HIV-1 transmission
Background
Approximately 20% of HIV-1 infected breastfeeding mothers transmit virus to their infants. It has been hypothesized that dendritic cells expressing C-type lectins, such as DC-SIGN, play an important role in the establishment of infection with HIV-1 and several other pathogens.
Within our laboratory we have identified that Bile Salt Stimulated Lipase (BSSL) is able to bind to DC-SIGN and block HIV-1 transmission via dendritic cells. The C-terminal part of BSSL contains a highly polymorphic repeat section coded by exon 11 of the gene and is composed of an array of 11 amino acid repeats.
Materials and methods
We have studied a large number of human breast milk samples from HIV-1 negative mothers. The BSSL protein was analyzed by size fractionation and iso-electric focusing. We studied the genomic structure of the gene through PCR amplification and sequencing of the BSSL repeats for a group of selected mothers.
Results
Milk samples from a large number of different mothers (n=25) were identified that demonstrated variant levels of inhibition to viral transfer. We have studied specific BSSL genotypic as well as phenotypic properties in order to identify what provides for the large variation of milk binding DC-SIGN. The tested milk samples were divided into weak binding and strong binding groups based on their DC-SIGN binding capacity. When comparing the PCR results for the BSSL repeat number we identified a link between the number of repeat domains and inhibition, with the more repeats binding less efficiently. A selection of weak and strong binders with identical repeat numbers was also made. Sequencing of this selected group revealed a mutation in the repeat section of an extreme weak binder on an interesting position with regards to BSSL glycosylation. Further analysis at the proteomic level was performed with a higher molecular mass for BSSL in the weak binding group being identified. Analysis of the DIGE results showed a shift in pI of BSSL in the weak binding group for 3 out of 5 cases.
Conclusions
Our results demonstrate that multiple factors contribute to the differential binding of human milk to DC-SIGN. Variation in the DC-SIGN binding capacities of BSSL may provide for alterations in transmission patterns of pathogens or in altering the immune mediated responses mounted in children against milk-borne pathogens. Furthermore, understanding these differences in BSSL could aide in the development of new agents aimed at preventing pathogen transmission across a mucosal barrier.
Approximately 20% of HIV-1 infected breastfeeding mothers transmit virus to their infants. It has been hypothesized that dendritic cells expressing C-type lectins, such as DC-SIGN, play an important role in the establishment of infection with HIV-1 and several other pathogens.
Within our laboratory we have identified that Bile Salt Stimulated Lipase (BSSL) is able to bind to DC-SIGN and block HIV-1 transmission via dendritic cells. The C-terminal part of BSSL contains a highly polymorphic repeat section coded by exon 11 of the gene and is composed of an array of 11 amino acid repeats.
Materials and methods
We have studied a large number of human breast milk samples from HIV-1 negative mothers. The BSSL protein was analyzed by size fractionation and iso-electric focusing. We studied the genomic structure of the gene through PCR amplification and sequencing of the BSSL repeats for a group of selected mothers.
Results
Milk samples from a large number of different mothers (n=25) were identified that demonstrated variant levels of inhibition to viral transfer. We have studied specific BSSL genotypic as well as phenotypic properties in order to identify what provides for the large variation of milk binding DC-SIGN. The tested milk samples were divided into weak binding and strong binding groups based on their DC-SIGN binding capacity. When comparing the PCR results for the BSSL repeat number we identified a link between the number of repeat domains and inhibition, with the more repeats binding less efficiently. A selection of weak and strong binders with identical repeat numbers was also made. Sequencing of this selected group revealed a mutation in the repeat section of an extreme weak binder on an interesting position with regards to BSSL glycosylation. Further analysis at the proteomic level was performed with a higher molecular mass for BSSL in the weak binding group being identified. Analysis of the DIGE results showed a shift in pI of BSSL in the weak binding group for 3 out of 5 cases.
Conclusions
Our results demonstrate that multiple factors contribute to the differential binding of human milk to DC-SIGN. Variation in the DC-SIGN binding capacities of BSSL may provide for alterations in transmission patterns of pathogens or in altering the immune mediated responses mounted in children against milk-borne pathogens. Furthermore, understanding these differences in BSSL could aide in the development of new agents aimed at preventing pathogen transmission across a mucosal barrier.
Friday
Immobilized Lipase Candida sp. 99-125 Catalyzed Methanolysis of Glycerol Trioleate: Solvent Effect
The immobilized lipase Candida sp. 99-125 catalyzed methanolysis of glycerol trioleate was studied in twelve different solvents in order to deduce the solvent effect through an attempt to correlate the highest yield with such solvent properties as hydrophobicity (log P), dielectric constant (ε), and Hildebrand solubility parameter (δ). The results showed that the conversion of glycerol trioleate and yield of oleic acid methyl ester were quite dependent on the solvent. The catalyst lipase in various solvents also needed different optimum amount of water to keep its maximum activity, and generally this lipase in more hydrophobic solvents required more water. The correlation between the highest yield and log P value was found to be reasonable except deviation of data points of certain solvents, while no obvious correlation existed between the other two parameters, dielectric constant (ε) and Hildebrand solubility parameter (δ), and the enzyme activity. The study revealed that more hydrophobic solvents such as n-hexane or cyclohexane were more suitable solvents for Candida sp. 99-125 catalyzed transesterification of glycerol trioleate to oleic acid methyl ester.
Jike Lua, Kaili Niea, Fang Wanga and Tianwei Tan, a,
aBeijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China
Jike Lua, Kaili Niea, Fang Wanga and Tianwei Tan, a,
aBeijing Bioprocess Key Laboratory, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, PR China
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