Objective: The study of the serum lipase and total amylase and its isoenzymes as biochemical markers of pancreatic injury in patients treated with valproic acid and other enzyme-inducing antiepileptic drugs .
Method: The serum activities of lipase and total amylase and its isoenzymes were determined in 41 patients treated in monotherapy with valproic acid, 50 patients in mono/polytherapy with phenytoin, phenobarbital and carbamazepine, and 30 healthy controls.
Results: In the first group of patients a clinically significant difference in relation to the control group was not obtained for any of the enzyme activities studied; however, in the group of patients treated with enzyme-inducing antiepileptic drugs clinically significant differences were obtained for lipase and pancreatic amylase . In this group of patients, the activity of pancreatic amylase was clearly increased in two cases (4%), suggesting the existence of a pancreatic damage. In the patients studied, the total amylase showed a poor specificity as a biochemical marker for pancreatic injury, and the greater serum activity observed in one case corresponds to an increase of the salivar isoenzyme. The sensitivity of the lipase is smaller than amylase pancreatic isoenzyme.
Conclusions: In patients treated with antiepileptic drugs, the determination of the pancreatic isoenzyme of amylase would be of interest even in absence of clinical signs for acute pancreatitis.
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Detection of salivary alpha-amylase and lysozyme exposed on the pellicle formed in situ on different materials
Amylase and lysozyme are components of the salivary pellicle, exposing considerable enzymatic activity in the immobilized state. The purpose of the present study was to elucidate the influence of different solid substrata on the amount and distribution of amylase and lysozyme exposed on the surface of the salivary pellicle formed in situ.
Slabs of titanium, feldspar ceramic, and bovine enamel were fixed on the buccal sites of individual splints worn by three subjects for 3 or 30 min, respectively, to allow pellicle formation. Subsequently, slabs were removed from the splints and rinsed with running water. Detection of amylase and lysozyme was performed by FEI-SEM after gold-immunolabeling of the enzymes.
Both enzymes were found to be distributed randomly at the pellicle surface. Irrespective of formation time and substratum, significantly more labeled lysozyme molecules (5.23 +/- 4.5 microm(-2)) were detected compared with amylase (3.4 +/- 2.9 microm(-2)). Neither the substratum nor the pellicle formation time had significant impact on the amount of the respective enzyme that could be detected. This study for the first time provides evidence, that amylase and lysozyme are exposed at the surface of the salivary pellicle formed in situ on titanium and ceramics. Both enzymes are distributed randomly on the surface of the pellicle, irrespective of the underlying substratum.
PMID: 17380501 [PubMed - indexed for MEDLINE]
Department of Operative Dentistry and Periodontology, University of Freiburg, Hugstetter Street 55, D-79106 Freiburg, Germany. christian.hannig@uniklinik-freiburg.de
Slabs of titanium, feldspar ceramic, and bovine enamel were fixed on the buccal sites of individual splints worn by three subjects for 3 or 30 min, respectively, to allow pellicle formation. Subsequently, slabs were removed from the splints and rinsed with running water. Detection of amylase and lysozyme was performed by FEI-SEM after gold-immunolabeling of the enzymes.
Both enzymes were found to be distributed randomly at the pellicle surface. Irrespective of formation time and substratum, significantly more labeled lysozyme molecules (5.23 +/- 4.5 microm(-2)) were detected compared with amylase (3.4 +/- 2.9 microm(-2)). Neither the substratum nor the pellicle formation time had significant impact on the amount of the respective enzyme that could be detected. This study for the first time provides evidence, that amylase and lysozyme are exposed at the surface of the salivary pellicle formed in situ on titanium and ceramics. Both enzymes are distributed randomly on the surface of the pellicle, irrespective of the underlying substratum.
PMID: 17380501 [PubMed - indexed for MEDLINE]
Department of Operative Dentistry and Periodontology, University of Freiburg, Hugstetter Street 55, D-79106 Freiburg, Germany. christian.hannig@uniklinik-freiburg.de
Serum amylase is a sensitive tumor marker for amylase-producing small cell lung cancer?
Amylase Case Study,
Abstract A 68-year-old male smoker was diagnosed as having amylase -producing small-cell lung cancer (SCLC). The serum amylase level was elevated, at 1756 IU/l, and the isozyme pattern was salivary type. Serum levels of “the tumor markers ” Carcinoembryonic antigen CEA and Neuron Specific Enolase NSE were 10.0 ng/ml and 22.6 ng/ml, respectively, but the level of pro-GRP was within the normal range. He was treated with combination chemotherapy of carboplatin and irinotecan. After completion of the chemotherapy, the serum amylase level decreased below the cutoff range and a computed tomography (CT) scan of the chest revealed marked reductions of the tumor in the primary site and in the lymph node metastasis.
In November 2003, he was noted to have a slightly raised amylase level, of 168 IU/l, and raised levels of tumor markers. At this time, a CT scan, bone scintigraphy, and magnetic resonance imaging (MRI) of the brain demonstrated no recurrence. However, in December, MRI of the brain showed multiple metastases, and the recurrence of SCLC was thus confirmed. For the treatment of disease progression, the same regimen of chemotherapy as that given initially was administered. CT imaging revealed a partial response in the primary site and lymph node metastasis, and the serum amylase level decreased to 91 IU/l. After the completion of the second chemotherapy regimen, he underwent cranial irradiation and further chemotherapy. However, unfortunately, he died owing to deterioration of lung cancer . In this patient, the serum amylase level was found to be a highly sensitive marker of lung cancer. Source:Noriko Yanagitani1 , Kyoichi Kaira1, Noriaki Sunaga1, Yoichi Naito1, Yoko Koike1, Shinichi Ishihara1, Tamotsu Ishizuka1, Ryusei Saito2 and Masatomo Mori1 (1) Department of Medicine and Molecular Science, Gunma University Graduate School of Medicine , 3-39-15 Showa-machi, Maebashi, Gunma 371-8511, Japan
(2) The National Nishigunma Hospital, Shibukawa, Gunma, Japan
Abstract A 68-year-old male smoker was diagnosed as having amylase -producing small-cell lung cancer (SCLC). The serum amylase level was elevated, at 1756 IU/l, and the isozyme pattern was salivary type. Serum levels of “the tumor markers ” Carcinoembryonic antigen CEA and Neuron Specific Enolase NSE were 10.0 ng/ml and 22.6 ng/ml, respectively, but the level of pro-GRP was within the normal range. He was treated with combination chemotherapy of carboplatin and irinotecan. After completion of the chemotherapy, the serum amylase level decreased below the cutoff range and a computed tomography (CT) scan of the chest revealed marked reductions of the tumor in the primary site and in the lymph node metastasis.
In November 2003, he was noted to have a slightly raised amylase level, of 168 IU/l, and raised levels of tumor markers. At this time, a CT scan, bone scintigraphy, and magnetic resonance imaging (MRI) of the brain demonstrated no recurrence. However, in December, MRI of the brain showed multiple metastases, and the recurrence of SCLC was thus confirmed. For the treatment of disease progression, the same regimen of chemotherapy as that given initially was administered. CT imaging revealed a partial response in the primary site and lymph node metastasis, and the serum amylase level decreased to 91 IU/l. After the completion of the second chemotherapy regimen, he underwent cranial irradiation and further chemotherapy. However, unfortunately, he died owing to deterioration of lung cancer . In this patient, the serum amylase level was found to be a highly sensitive marker of lung cancer. Source:Noriko Yanagitani1 , Kyoichi Kaira1, Noriaki Sunaga1, Yoichi Naito1, Yoko Koike1, Shinichi Ishihara1, Tamotsu Ishizuka1, Ryusei Saito2 and Masatomo Mori1 (1) Department of Medicine and Molecular Science, Gunma University Graduate School of Medicine , 3-39-15 Showa-machi, Maebashi, Gunma 371-8511, Japan
(2) The National Nishigunma Hospital, Shibukawa, Gunma, Japan
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