scholarly journals Pepsinogen C Measurement

2020 ◽  
Author(s):  
Keyword(s):  
Gut ◽  
1993 ◽  
Vol 34 (10) ◽  
pp. 1315-1318 ◽  
Author(s):  
I Biemond ◽  
J Kreuning ◽  
J B Jansen ◽  
C B Lamers

2000 ◽  
Vol 15 (2) ◽  
pp. 165-170 ◽  
Author(s):  
A.M. Merino ◽  
J. Vázquez ◽  
J.C. Rodríguez ◽  
R. Fernández ◽  
I. Quintela ◽  
...  

We have examined by immunohistochemistry the ability of human carcinomas of various origin to produce pepsinogen C, an aspartyl proteinase mainly involved in the digestion of proteins in the stomach and recently found to be associated with breast carcinomas. Of the 268 tumors analyzed 80 (29.8%) showed positive staining for pepsinogen C. These positive tumors included 12 gastric (38.7% of the 31 examined cases), nine pancreatic (42.8%), two renal (20%), 12 prostatic (40%), three bladder (27.3%), 14 endometrial (29.7%) and 18 ovarian (40%) carcinomas. We also detected 10 melanomas (50%) that were positive for pepsinogen C. By contrast, immunohistochemical staining for the proteinase was not detected in colorectal, cervical, lung and basal cell skin carcinomas. These results demonstrate that pepsinogen C, a proteolytic enzyme of highly restricted expression in human tissues, can also be expressed by a wide variety of human carcinomas. In addition, and similar to pepsinogen C expression in breast carcinomas, the production of this enzyme by different human tumors might be related to putative hormonal alterations associated with the development and progression of these tumors.


2003 ◽  
Vol 13 (5) ◽  
pp. 301-308 ◽  
Author(s):  
Michelle Wells ◽  
Brian Brown ◽  
Judith Hall
Keyword(s):  

2009 ◽  
Vol 181 (2) ◽  
pp. 594-600 ◽  
Author(s):  
Alberto A. Antunes ◽  
Kátia R. Leite ◽  
Juliana M. Sousa-Canavez ◽  
Luiz H. Camara-Lopes ◽  
Miguel Srougi

1989 ◽  
Vol 52 (1-2) ◽  
pp. 100-101 ◽  
Author(s):  
K. Takahara ◽  
S. Fukushige ◽  
T. Murotsu ◽  
Y. Ichihara ◽  
T. Hayano ◽  
...  
Keyword(s):  

2001 ◽  
Vol 16 (1) ◽  
pp. 31-36 ◽  
Author(s):  
N. Truan ◽  
F. Vizoso ◽  
M.F. Fresno ◽  
R. Fernández ◽  
I. Quintela ◽  
...  

Pepsinogen C is an aspartyl-proteinase usually involved in the digestion of proteins in the stomach, and an androgen- inducible protein in breast cancer cells. In this study we evaluated its expression and clinical significance in patients with resectable pancreatic cancer. Pepsinogen C expression was examined by immunohistochemical methods in a series of 73 pancreatic carcinomas. The prognostic value of pepsinogen C was retrospectively evaluated by multivariate analysis. A total of 21 (28.8%) pancreatic carcinomas stained positively for pepsinogen C. The percentage of pepsinogen C-positive tumors was significantly higher in well-differentiated tumors (38.3%) than in moderately differentiated (15.8%) and poorly differentiated (0%) tumors (p<0.05). In addition, statistical analysis revealed that pepsinogen C expression was associated with clinical outcome. Thus, patients with pepsinogen C-negative tumors have a poorer overall survival than those with pepsinogen C-positive tumors. Our results led us to consider that the expression of pepsinogen C may represent a useful biological marker in pancreatic cancer. Expression of this protein may be a marker of gastric-type differentiation of the tumors and it might also reflect the existence of a complete hormone receptor pathway in a subset of pancreatic carcinomas.


1995 ◽  
Vol 49 (6) ◽  
pp. 998-1003
Author(s):  
Zentaro YAMAGATA ◽  
Sumio IIJIMA ◽  
Akio ASAKA ◽  
Kazuhisa KOBAYASHI

1995 ◽  
Vol 13 (1) ◽  
pp. 54-61 ◽  
Author(s):  
F Vizoso ◽  
L M Sánchez ◽  
I Díez-Itza ◽  
A M Merino ◽  
C López-Otín

PURPOSE Here we evaluate in breast cancer patients the prognostic value of pepsinogen C, a proteolytic enzyme involved in the digestion of proteins in the stomach that is also synthesized by a significant percentage of breast carcinomas. PATIENTS AND METHODS Pepsinogen C expression was examined by immunoperoxidase staining in a series of 243 breast cancer tissue sections, and results obtained were quantified using the HSCORE system, which considers both the intensity and the percentage of cells staining at each intensity. Evaluation of the prognostic value of pepsinogen C was performed retrospectively in corresponding patients by multivariate analysis that took into account conventional prognostic factors. The mean follow-up period was 48.5 months. RESULTS A total of 113 carcinomas (46.5%) stained positively for this proteinase, but there were clear differences among them with regard to the intensity and percentage of stained cells. Pepsinogen C values were significantly higher in well differentiated (grade I, 89.1) and moderately differentiated (grade II, 88.5) tumors than in poorly differentiated (grade III, 27.7) tumors (P < .001). Similarly, significant differences in pepsinogen C content were found between estrogen receptor (ER)-positive tumors and ER-negative tumors (85.9 v 41.2, respectively; P < .05). Moreover, results indicated that low pepsinogen C content predicted shorter relapse-free survival duration and overall survival duration (P < .0001). Separate Cox multivariate analysis for relapse-free survival and overall survival in subgroups of patients as defined by node status showed that pepsinogen C expression was the strongest factor to predict both relapse-free survival and overall survival in node-positive patients (P < .0001 for both) and node-negative patients (P < .005 and P < .01, respectively). CONCLUSION Pepsinogen C is a new prognostic factor for early recurrence and death in both node-positive and node-negative breast cancer. In addition, and in contrast to most studies that concern the prognostic significance of proteolytic enzymes in cancer, pepsinogen C production by breast cancer cells is associated with lesions of favorable evolution.


1987 ◽  
Vol 21 (2) ◽  
pp. 204
Author(s):  
R. Waalewijn ◽  
S.G.M. Meuwissen ◽  
E.C.M. Hoefsmit

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