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Takesada Mori - One of the best experts on this subject based on the ideXlab platform.
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elevation of circulating monitor peptide pancreatic secretory trypsin inhibitor i PstI 61 after turpentine induced inflammation in rats hepatocytes produce it as an acute phase reactant
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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Elevation of circulating monitor peptide/pancreatic secretory trypsin inhibitor-I (PstI-61) after turpentine-induced inflammation in rats: hepatocytes produce it as an acute phase reactant.
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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specific expression of the pancreatic secretory trypsin inhibitor PstI gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
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Specific expression of the pancreatic‐secretory‐trypsin‐inhibitor (PstI) gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
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expression of pancreatic secretory trypsin inhibitor PstI in colorectal cancer
British Journal of Cancer, 1990Co-Authors: Masahiko Higashiyama, Takushi Monden, Naohiro Tomita, M Murotani, Yasuhito Kawasaki, Hideki Morimoto, Atsuo Murata, Takashi Shimano, Michio Ogawa, Takesada MoriAbstract:We examined the expression of pancreatic secretory trypsin inhibitor (PstI) in colorectal cancer by immunohistochemical staining using an anti-PstI antiserum, an in situ hybridisation technique utilising sulphonated PstI cDNA probe, and a Northern blot hybridisation method, using a 32P-labelled PstI cDNA probe. Immunohistochemically, PstI was detected in 80 of 95 (84%) colorectal cancer cases. Analyses with in situ hybridisation as well as Northern blot hybridisation demonstrated PstI mRNAs in immunohistochemically positive cases, showing PstI could be produced in colorectal cancerous cells. Histologically well or moderately differentiated adenocarcinoma showed higher incidence of PstI immunoreactivity than the other types. Furthermore, the intensity of the immunohistochemical staining for PstI increased the more cases advanced, particularly in regard to depth of invasion and tumour size. Thus, PstI expression is widespread in colorectal cancer, and occurs more commonly in advanced cases. Considering the suggestion that PstI is a growth-stimulating factor as an well as inhibitor to proteolytic proteinase, the present findings may indicate that PstI expressed in colorectal cancerous cells may play a role possibly closely associated with tumour development.
Atsuo Murata - One of the best experts on this subject based on the ideXlab platform.
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elevation of circulating monitor peptide pancreatic secretory trypsin inhibitor i PstI 61 after turpentine induced inflammation in rats hepatocytes produce it as an acute phase reactant
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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Elevation of circulating monitor peptide/pancreatic secretory trypsin inhibitor-I (PstI-61) after turpentine-induced inflammation in rats: hepatocytes produce it as an acute phase reactant.
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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specific expression of the pancreatic secretory trypsin inhibitor PstI gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
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Specific expression of the pancreatic‐secretory‐trypsin‐inhibitor (PstI) gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
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expression of pancreatic secretory trypsin inhibitor PstI in colorectal cancer
British Journal of Cancer, 1990Co-Authors: Masahiko Higashiyama, Takushi Monden, Naohiro Tomita, M Murotani, Yasuhito Kawasaki, Hideki Morimoto, Atsuo Murata, Takashi Shimano, Michio Ogawa, Takesada MoriAbstract:We examined the expression of pancreatic secretory trypsin inhibitor (PstI) in colorectal cancer by immunohistochemical staining using an anti-PstI antiserum, an in situ hybridisation technique utilising sulphonated PstI cDNA probe, and a Northern blot hybridisation method, using a 32P-labelled PstI cDNA probe. Immunohistochemically, PstI was detected in 80 of 95 (84%) colorectal cancer cases. Analyses with in situ hybridisation as well as Northern blot hybridisation demonstrated PstI mRNAs in immunohistochemically positive cases, showing PstI could be produced in colorectal cancerous cells. Histologically well or moderately differentiated adenocarcinoma showed higher incidence of PstI immunoreactivity than the other types. Furthermore, the intensity of the immunohistochemical staining for PstI increased the more cases advanced, particularly in regard to depth of invasion and tumour size. Thus, PstI expression is widespread in colorectal cancer, and occurs more commonly in advanced cases. Considering the suggestion that PstI is a growth-stimulating factor as an well as inhibitor to proteolytic proteinase, the present findings may indicate that PstI expressed in colorectal cancerous cells may play a role possibly closely associated with tumour development.
Michio Ogawa - One of the best experts on this subject based on the ideXlab platform.
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the protective effects of long acting recombinant human pancreatic secretory trypsin inhibitor r44s PstI in a rat model of cerulein induced pancreatitis
Journal of International Medical Research, 1996Co-Authors: Yz Chen, Satoshi Ikei, Yasuo Yamaguchi, H Sameshma, Hiroki Sugita, M Moriyasu, Michio OgawaAbstract:: The effects of pancreatic secretory trypsin inhibitor (PstI) on cerulein-induced pancreatitis were studied in a rat model. Arg44 of PstI was replaced by Ser using site-directed mutagenesis (R44S-PstI). R44S-PstI has a longer half-life than the natural form. Pancreatitis was induced by four intramuscular injections of cerulein (50 microgram/kg at 1 h intervals). Continuous intravenous infusion of R44S-PstI began at a dose of 20 micrograms/kg/h 30 min before the first cerulein injection, and was completed 3 h after the last cerulein injection. Tumour necrosis factor (TNF-alpha) production by isolated peritoneal macrophages from rats with cerulein-induced pancreatitis increased following lipopolysaccharide stimulation, compared to control rats (P < 0.01). R44S-PstI administration significantly decreased the TNF-alpha production by peritoneal macrophages from rats with cerulein-induced pancreatitis (P < 0.05). In addition, R44S-PstI significantly reduced serum amylase activity (P < 0.01) and pancreatic wet weight after pancreatitis induction (P < 0.05). Histological examination revealed marked acinar cell vacuolization, interstitial oedema, and cellular infiltration in cerulein-induced pancreatitis, but a lesser degree of histological change in rats that were treated with R44S-PstI. Prophylactic use of intravenous R44S-PstI infusion may reduce the severity of acute pancreatitis either histologically or serologically.
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elevation of circulating monitor peptide pancreatic secretory trypsin inhibitor i PstI 61 after turpentine induced inflammation in rats hepatocytes produce it as an acute phase reactant
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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Elevation of circulating monitor peptide/pancreatic secretory trypsin inhibitor-I (PstI-61) after turpentine-induced inflammation in rats: hepatocytes produce it as an acute phase reactant.
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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specific expression of the pancreatic secretory trypsin inhibitor PstI gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
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Specific expression of the pancreatic‐secretory‐trypsin‐inhibitor (PstI) gene in hepatocellular carcinoma
International Journal of Cancer, 1993Co-Authors: Yoshitaka Ohmachi, Atsuo Murata, Michio Ogawa, Takesada Mori, Tadashi Yasuda, Takushi Yasuda, Morito Monden, Kenichi MatsubaraAbstract:: Twenty hepatocellular carcinomas (HCC) were analyzed by Northern blotting to test the expression of pancreatic secretory trypsin inhibitor (PstI). This gene was expressed in all HCCs, but not in other tumors, including mammary, thyroid, pulmonary and ovarian cancers. Some gastric and colonic cancers weakly expressed PstI. Among cell lines examined in a similar manner, PstI was expressed in all of 4 derived from hepatoma. On the other hand, among 15 cell lines derived from cancers other than hepatoma, only 3, derived from pancreatic, colonic and gastric cancers, weakly expressed PstI. A CAT assay using a deletion set of the 5' region from the cloned PstI gene has shown that in hepatoma cell lines, the expression of this gene is dependent on the presence of 2 regulatory regions that include an IL-6 responsive elements and an AP-I-binding site. However, in non-hepatoma cell lines, the 2 regulatory regions are not necessary for expression. The blood level of PstI in 27 patients with HCC was significantly increased, and it was positively correlated with tumor size, suggesting that specific expression of PstI in HCC causes this effect and that elevated blood level of PstI without inflammation indicates the presence of HCC.
Daniel Bimmler - One of the best experts on this subject based on the ideXlab platform.
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biochemistry and biology of spink PstI and monitor peptide
Endocrinology and Metabolism Clinics of North America, 2006Co-Authors: Rolf Graf, Daniel BimmlerAbstract:: This article summarizes structural and functional properties of pancreatic secretory trypsin inhibitor (PstI), which has been identified in many species. Its prominent role is to protect the pancreas from prematurely activated trypsinogen before entry into the duodenum. In the rat there are two isoforms, one of which is PstI-I, a 61-amino acid peptide involved in the feedback regulation of pancreatic enzymes. Independent investigations in neoplastic diseases led to the discovery of tumor-associated trypsin inhibitor,which is identical to PstI.
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increased secretion of the pancreatic secretory trypsin inhibitor PstI i monitor peptide during development of chronic pancreatitis in the wbn kob rat
Pancreatology, 2002Co-Authors: Rolf Graf, Marc Schiesser, Daniel BimmlerAbstract:Background: Recent genetic investigations into cationic trypsinogen and pancreatic secretory trypsin inhibitor (PstI) led to the conclusion that mutations in either gene can contrib
Naohiro Tomita - One of the best experts on this subject based on the ideXlab platform.
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Elevation of circulating monitor peptide/pancreatic secretory trypsin inhibitor-I (PstI-61) after turpentine-induced inflammation in rats: hepatocytes produce it as an acute phase reactant.
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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elevation of circulating monitor peptide pancreatic secretory trypsin inhibitor i PstI 61 after turpentine induced inflammation in rats hepatocytes produce it as an acute phase reactant
Journal of Surgical Research, 1994Co-Authors: Atsuo Murata, Naohiro Tomita, Michio Ogawa, Junichi Nishijima, Takesada MoriAbstract:Monitor peptide (MP) is a trypsin-sensitive cholecystokinin (CCK)-releasing peptide purified from rat pancreatic juice on the basis of its stimulatory activity toward pancreatic enzyme secretion and has been reported to exhibit cell growth-stimulating activity. Pancreatic secretory trypsin inhibitor (PstI) prevents premature activation of trypsinogen in the pancreatic duct. There are two PstIs (PstI-61 and -56) purified from rat pancreatic juice on the basis of trypsin inhibitory activity as reported previously. Fushiki et al. (1989, FASEB J. 3, 121) showed that MP is structually the same peptide as PstI-61. We measured the serial changes of circulating MP/PstI-61 in rat and those in the level of PstI-61 mRNA in the rat liver to investigate another novel role of this peptide in the turpentine-induced acute inflammation model. The elevation of serum MP/PstI-61 as well as the α2-globulin fraction, which is known to include several acute phase reactants such as α2-macroglobulin and haptoglobin, was observed after induction of the turpentine inflammation. The serum α2-globulin fraction had increased approximately 3-fold over the initial level at 48 hr after the injection. In contrast, serum MP/PstI-61 had increased approximately 17-fold over the initial level at 48 hr after the injection. The elevation of circulating MP/PstI-61 was significantly related with that of the α2-globulin fraction (r = 0.91, P < 0.01). Immunoreactive MP/PstI-61 was detected in the liver after induction of the inflammation (152.5 ± 16.5 ng/g wet weight), but in the normal rat liver there was no immunoreactive MP/PstI-61. Furthermore, the elevated expression of PstI-61 mRNA was only detected in the liver, using a synthetic oligonucleotide probe specific for PstI-61. These results demonstrate that rat MP/ PstI-61 is produced as an acute phase reactant in the liver in response to inflammatory stimuli, as well as other known acute phase reactants such as α2-macroglobulin and haptoglobin.
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expression of pancreatic secretory trypsin inhibitor PstI in colorectal cancer
British Journal of Cancer, 1990Co-Authors: Masahiko Higashiyama, Takushi Monden, Naohiro Tomita, M Murotani, Yasuhito Kawasaki, Hideki Morimoto, Atsuo Murata, Takashi Shimano, Michio Ogawa, Takesada MoriAbstract:We examined the expression of pancreatic secretory trypsin inhibitor (PstI) in colorectal cancer by immunohistochemical staining using an anti-PstI antiserum, an in situ hybridisation technique utilising sulphonated PstI cDNA probe, and a Northern blot hybridisation method, using a 32P-labelled PstI cDNA probe. Immunohistochemically, PstI was detected in 80 of 95 (84%) colorectal cancer cases. Analyses with in situ hybridisation as well as Northern blot hybridisation demonstrated PstI mRNAs in immunohistochemically positive cases, showing PstI could be produced in colorectal cancerous cells. Histologically well or moderately differentiated adenocarcinoma showed higher incidence of PstI immunoreactivity than the other types. Furthermore, the intensity of the immunohistochemical staining for PstI increased the more cases advanced, particularly in regard to depth of invasion and tumour size. Thus, PstI expression is widespread in colorectal cancer, and occurs more commonly in advanced cases. Considering the suggestion that PstI is a growth-stimulating factor as an well as inhibitor to proteolytic proteinase, the present findings may indicate that PstI expressed in colorectal cancerous cells may play a role possibly closely associated with tumour development.
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immunohistochemical study on pancreatic secretory trypsin inhibitor PstI in gastric carcinomas
American Journal of Clinical Pathology, 1990Co-Authors: Masahiko Higashiyama, Takushi Monden, Naohiro Tomita, M Murotani, Yasuhito Kawasaki, Atsuo Murata, Takashi Shimano, Michio Ogawa, Nariaki Matsuura, Takesada MoriAbstract:: The expression of pancreatic secretory trypsin inhibitor (PstI) was studied immunohistochemically in 106 cases of gastric carcinoma. Of the 45 intestinal-type carcinomas, 34 cases (76%) expressed PstI: 15 (63%) of 24 early carcinomas and 19 (90%) of 21 advanced carcinomas, the incidence being significantly different (P less than 0.05). Furthermore, in the intestinal-type carcinomas, a significant correlation was observed between PstI expression and clinical stage or nodal involvement. On the other hand, of the 61 diffuse-type carcinomas, including 27 early and 34 advanced carcinomas, 54 cases (89%) were positive for PstI; a high incidence of the PstI expression was observed in both early and advanced carcinomas, being 93% and 85%, respectively. Moreover, PstI-positive cells were localized in more than half of the early diffuse-type gastric carcinomas at the invading zone of the surrounding tissues. The incidence of PstI expression in advanced scirrhous-type carcinomas (100%) was significantly higher than that (76%) in medullary-type ones (P less than 0.05). Thus, the present findings, together with the previous reports that PstI stimulates 3H-thymidine incorporation into DNA in human fibroblasts, suggest that the PstI expressed in gastric carcinomas may possibly possess a biologic function responsible for the tumor growth and progression and for the stromal proliferation of fibrous tissues.
