Slow moving proteinase

Samloff, I. Michael; Taggart, R T; Shiraishi, Taizo; Branch, Tabriz; Reid, William A.; Heath, RH; Lewis, Ronald W.; Valler, Martin J.; Kay, John

doi:10.1016/0016-5085(87)90317-9

Cited by 94 publications

(15 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the previous studies [2,3], we purified this enzyme to apparent homogeneity and investigated its several properties. Similar studies were also performed by Samloff et al [4]. Further, the complete amino acid sequence of human procathepsin E has been deduced recently by Azuma et al [5] from the analysis of its cDNA clones.…”

Section: Introductionsupporting

confidence: 63%

See 1 more Smart Citation

Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin

1991

FEBS Letters

View full text Add to dashboard Cite

Proteolytic activity and cleavage specificity of cathcpsin E were investigated in a wide range of pHs from 3.0 to 10.5 using the B chain of oxidized insulin as substrate. Contrary to the previous notion that cathepsin E is virtually inactive above pH 6, significant proteolytic activity yeas observed at pH 7.4 and above. Further. cleavage specificity appeared to change significantly with pH and rather specific cleavage occurred at pH 7.4 and above as compared to pH 5.5 and 3.0. These results suggest that cathepsin E may function in vivo at the physiological pH with a rather restricted specificity.Cathepsin E: Gastric mucosal aspartic proteinase" Proteolytic activity; Cleavage specificity; B chain of oxidized insulin

show abstract

Section: Introductionsupporting

confidence: 63%

“…However, its physiological function and the process of activation remain obscure. Due to its intracellular localization in lymphoid-associated tissues and cells, it has been suggested to have a role in immune function [4,10]. It has also been suggested to be involved in the processing of big endothelin-I [11].…”

Section: Introductionmentioning

confidence: 99%

Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin

1991

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…Proteolytic activity was measured against haemoglobin as substrate [14] in 0.17 M sodium citrate buffer, pH 3.1, when crude preparations needed to be evaluated; or utilising peptide substrates containing p-nitrophenylalanine (Nph) in the P~ position as a chromogenic reporter group [17] when purer enzyme samples were available. Kinetic analyses with two of these peptide substrates (generously provided by Dr. Ben M. Dunn, University of Florida, USA) were performed as described previously [4] except that the pH used was pH 3.1 at a final ionic strength of 0.1 M. Initial velocities were measured with at least six concentrations of each peptide substrate within an appropriate range in order to derive the kinetic constants, K, I1 and Vm~x.…”

Section: Methodsmentioning

confidence: 99%

“…inhibitor from the parasitic worm, Ascaris lumbricoides [4,7,14,18]. Consequently, an inhibition constant (Ki) was determined for the interaction of this protein with the recombinant enzyme.…”

Section: -mentioning

confidence: 99%

“…Production (of the precursors) of the secretory enzymes, pepsin and renin, and the membrane-encapsulated lysosomal cathepsin D in recombinant form [8][9][10] has greatly facilitated investigations into structure/function relationships in addition to providing sufficient material for 3-dimensional structural analysis by X-ray crystallography [11][12][13]. Cathepsin E is neither a secretory nor a lysosomal enzyme [7,14]; thus this intracellular aspartic proteinase is difficult to isolate in reasonable amounts. With its potential involvement in the processing reactions itemised above, it was considered of interest to produce cathepsin E in recombinant form to facilitate its molecular characterisation.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Human cathepsin E produced in E. coli

1993

View full text Add to dashboard Cite

A cDNA for procathepsin E was generated from human gastric adenocarcinoma (AGS) cells, amplified by PCR and inserted into the T7 dependent vector pET 22b for expression in E. coll. Purification of the resultant product was accomplished simply, without the need to resort to column chromatography. The recombinant protein displayed comparable properties to those of its naturally occurring counterpart. The yield of homogeneous active enzyme obtained was -3 mg per 40 g of cells. This is sufficient to permit crystallisation and structural analysis to begin and a mutagenesis programme to examine structure/activity relationships now to be undertaken.

show abstract

Expression of cathepsin E in pancreas: A possible tumor marker for pancreas, a preliminary report

et al. 1996

View full text Add to dashboard Cite

Ductal cancers of the pancreas frequently express markers of gastrointestinal epithelial cells. Cathepsin E (CTSE) is a nonsecretory, intracellular, but non-lysosomal proteinase found in the highest concentration in the superficial epithelial cells of the stomach. The aims of our study were to examine the expression of CTSE in the pancreas, to establish an assay system of CTSE and to evaluate the diagnostic usefulness of CTSE in the pancreatic juice. Eleven patients with pancreatic ductal adenocarcinoma, 10 with mucin-producing adenoma, 3 with intraductal papillary hyperplasia and 43 with chronic pancreatitis were examined. Surgically resected pancreatic tissues were subjected to irnmunohistochemistry for CTSE. Pancreatic juice was collected from the patients and subjected to sandwich ELISA and Western analysis for detecting CTSE. Positive staining for CTSE was observed in pancreatic ductal adenocarcinoma by immunohistochemistry. CTSE was also expressed in mucin-producing adenoma, intraductal papillary hyperplasia and mucinous hyperplasia. CTSE in the pancreatic juice was present in 8 of I I patients with pancreatic ductal adenocarcinoma. 5 of 10 patients with mucin-producing tumor, I of 3 patients with intraductal papillary hyperplasia and 4 of 43 patients with chronic pancreatitis. The detection frequency of CTSE in the pancreatic juice was significantly higher in the patients with pancreatic ductal adenocarcinoma than in the patients with chronic pancreatitis. Our findings suggest that the expression of CTSE is associated with the pathogenesis of pancreatic ductal adenocarcinoma, that CTSE in the pancreatic juice seems to be a useful marker for a definitive diagnosis and that CTSE may be expressed at a relatively early stage of multistep carcinogenesis in pancreatic lesions.o 1996 Wiley-Liss, Inc.The incidence of pancreatic cancer continues to increase in industrialized Western countries (Silverberg and Lubera, 1989). Pancreatic carcinoma has the lowest 5-year survival rate. Late diagnosis, high recurrence rates and a characteristic tumor biology with regard to growth behavior are responsible for the fact that most tumors of the pancreas, when diagnosed, have spread beyond the reach of surgical cure. Only 10-20% of the patients have a resectable tumor at the time of diagnosis and a chance of being cured by surgery (Gudjonsson, 1987;. Early diagnosis of pancreatic cancer is presently the only means to increase the proportion of patients detected at resectable and curable tumor stages . During the past few years, great efforts have been made to render the pancreas visible with new or improved imaging techniques. It can still be difficult to distinguish between pancreatic cancer and chronic pancreatitis, since the two diseases may share many clinical and radiologic characteristics (Kawai et al., 1987). A wide variety of tumor markers have been proposed for use in the diagnosis of pancreatic cancer. These include the serum levels of tumorassociated antigens, enzymes and hormones (Steinberg et al.. 1986; Friess e...

show abstract

Slow moving proteinase

Cited by 94 publications

References 29 publications

Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin

Proteolytic activity and cleavage specificity of cathepsin E at the physiological pH as examined towards the B chain of oxidized insulin

Human cathepsin E produced in E. coli

Expression of cathepsin E in pancreas: A possible tumor marker for pancreas, a preliminary report

Contact Info

Product

Resources

About