Pancreatic Stone Protein and Lactoferrin in Human Pancreatic Juice in Chronic Pancreatitis

Hayakawa, Tetsuo; Naruse, Satoru; Kitagawa, Motoji; Nakae, Yasuyuki; Harada, Hideo; Ochi, Koji; Kuno, Nobuyoshi; Karasawa, Kumiko; Hayakawa, Shinobu

doi:10.1097/00006676-199503000-00005

Cited by 17 publications

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“…16 Elevations of lactoferrin have previously been reported in the pancreatic juice of patients with chronic calcifying pancreatitis and/or autoimmunerelated pancreatitis. [17][18][19][20] Interestingly, in experimental studies, lactoferrin has been shown to inhibit the growth of some solid tumors such as colon, esophagus, and lung tumors. 21,22 Interestingly, stool lactoferrin has been shown to be a sensitive marker of intestinal inflammation in patients with intestinal tract symptoms and is being used in clinical practice to identify patients with intestinal tract inflammation.…”

Section: Discussionmentioning

confidence: 99%

Gene expression alterations in the non-neoplastic parenchyma adjacent to infiltrating pancreatic ductal adenocarcinoma

et al. 2005

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The non-neoplastic pancreatic parenchyma adjacent to infiltrating ductal adenocarcinoma demonstrates inflammation, fibrosis, acinar cell loss and small duct-like metaplasia of acinar cells. Similar morphologic changes are also observed in the setting of chronic pancreatitis. In addition, peritumoral acini have been shown to have alterations in gene expression even in the absence of morphological changes. To better understand the pancreatic acinar responses to infiltrating pancreatic ductal adenocarcinoma, we characterized gene expression patterns of pancreatic acinar tissue adjacent to infiltrating pancreatic ductal adenocarcinomas and compared them to gene expression patterns of acinar tissue affected by chronic pancreatitis as well as to those of normal pancreatic acini. Fresh-frozen pancreatic acinar tissue was microdissected from nine patients (three with pancreatic cancer, three with chronic pancreatitis, three with normal pancreata) using laser capture microdissection, and extracted RNA from each microdissection was subjected to two rounds of linear amplification and hybridized to oligonucleotide microarrays. Gene expression patterns were confirmed using quantitative RT-PCR and/or immunohistochemistry. A total of 20 genes was found to be overexpressed in peritumoral acinar tissue compared to normal acinar tissue and to acini affected by chronic pancreatitis. These 20 genes included pancreatitis-associated protein (HIP/PAP), a gene known to be overexpressed in acini adjacent to infiltrating pancreatic cancer, and the gene cartilage glycoprotein-39 (HC gp-39 or TKL-40). Serum HC gp-39 protein levels were significantly higher in patients with pancreatic cancer and in those with chronic pancreatitis than in controls without pancreatic disease. There was no significant difference in the levels of serum HC gp-39 in patients with pancreatic cancer and those with chronic pancreatitis. Our results demonstrate some of the molecular alterations in acinar cells that occur in response to adjacent infiltrating pancreatic ductal adenocarcinoma and reveal that such alterations can provide a rich source of markers of pancreatic cancer.

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Section: Discussionmentioning

confidence: 99%

Gene expression alterations in the non-neoplastic parenchyma adjacent to infiltrating pancreatic ductal adenocarcinoma

et al. 2005

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“…First, the findings concerning altered lithostatin biosynthesis and function in chronic pancreatitis have not been universally confirmed. [64][65][66] Second, the hypothesis only recognizes chronic pancreatitis as an alcohol-induced disease and neglects the fact that acute pancreatitis may also be caused by alcohol. [67][68][69][70] Third, alcoholic acute and chronic pancreatitis have many features in common, such as clinical symptoms and the presence of pseudocysts.…”

Section: Pathogenesismentioning

confidence: 99%

Chronic pancreatitis, pseudotumors and other tumor-like lesions

2007

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“…Trypsin causes conversion of a 16-kDa PSP, by Arg11-Ile12 specific cleavage, into a 14-kDa soluble isoform or pancreatic thread protein, which rapidly polymerizes into insoluble sedimenting fibrils (13)(14)(15). Katsuzaki et al confirmed experimentally that adding bovine trypsin to the pancreatic juice makes 50 to 85% of PSP precipitate into pancreatic thread protein (16).…”

Section: Discussionmentioning

confidence: 99%

“…PSP concentrations were measured by enzyme immunoassay (EIA) using a monoclonal antibody with reactivity to both soluble and insoluble forms of PSP (Taico Co., Kasugai, Japan) (14). Samples were first diluted 1:100 with 0.1 M sodium acetate buffer, pH 4.0, then further diluted to an appropriate concentration with 10 mM sodium acetate buffer, pH 7.0, containing 0.1% bovine serum albumin, 0.125% gelatin, and 0.15 M NaCl.…”

Section: Methodsmentioning

confidence: 99%

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Activated Pancreatic Enzyme and Pancreatic Stone Protein (PSP/reg) in Bile of Patients with Pancreaticobiliary Maljunction/Choledochal Cysts

et al. 2004

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Symptoms of pancreaticobiliary maljunction/choledochal cysts are caused by the obstruction of bile and pancreatic ducts due to protein plugs compacted in the common channel. However, the mechanism of protein plug formation remains unknown. Pancreatic stone protein (PSP) is reported to be a key protein to form protein plugs in chronic pancreatitis. Bile from 13 patients with pancreaticobiliary maljunction and bile from two normal controls were analyzed. Activity of pancreatic enzymes and the concentration of PSP were measured. The mean concentrations of PSP were 76.9+/-30.9 ng/mL in the bile-duct bile, and 76.9+/-29.8 ng/mL in the gallbladder bile. PSP was not detected in the controls (P < 0.05). In the bile-duct bile of the patients, trypsin(ogen) was detectable in nine patients, of which seven patients had activated trypsin. In the gallbladder bile, trypsin(ogen) was detectable in 12 patients, of which 9 patients had activated trypsin. Neither activated trypsin nor trypsinogen was detected in the controls. Bile in pancreaticobiliary maljunction patients contained both activated trypsin and PSP. Activated trypsin cleaves soluble PSP and creates insoluble PSP. Protein plugs in pancreaticobiliary maljunction may be formed by assembled insoluble PSP.

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Pancreatic Stone Protein and Lactoferrin in Human Pancreatic Juice in Chronic Pancreatitis

Cited by 17 publications

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Gene expression alterations in the non-neoplastic parenchyma adjacent to infiltrating pancreatic ductal adenocarcinoma

Gene expression alterations in the non-neoplastic parenchyma adjacent to infiltrating pancreatic ductal adenocarcinoma

Chronic pancreatitis, pseudotumors and other tumor-like lesions

Activated Pancreatic Enzyme and Pancreatic Stone Protein (PSP/reg) in Bile of Patients with Pancreaticobiliary Maljunction/Choledochal Cysts

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