z-logo
open-access-imgOpen Access
Arylsulfatase, β-galactosidase and lysozyme in gastric cancer cells and its relationship to invasion
Author(s) -
Yongxiang Yi
Publication year - 1998
Publication title -
world journal of gastroenterology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.427
H-Index - 155
eISSN - 2219-2840
pISSN - 1007-9327
DOI - 10.3748/wjg.v4.i1.52
Subject(s) - arylsulfatase , cancer cell , adenocarcinoma , cancer , lysozyme , immunohistochemistry , arylsulfatase a , pathology , biology , metastasis , perineural invasion , cellular differentiation , chemistry , cancer research , enzyme , biochemistry , medicine , gene , genetics
AIM:To study the distribution of arylsulfatase,beta-galactosidase and lysozyme in gastric cancer cells, and its relationship to differentiation and invasion of gastric cancer cells.METHODS: Histochemical, immunohistochemical and ruthenium red (RR) electrocytochemical technique for three types of hydrolases and proteoglycans in pericancerous matrix in 33 cases of gastric cancer were observed under light and electron microscopy.RESULTS:The expression intensities of arylsulfatase,beta-glactosidase and lysozyme in mucinous cell carcinomas were more intensive than those in well-differentiated and poorly-differentiated adenocar-cinomas (P < 0.05-0.01). The fibrous tissues smooth muscle and proteoglycans close to the cancer cells were degraded. They were found in the region far from the cancer cells. Expression of three enzymes mentioned above was low in adenocarcinoma cells, and fibrous tissues and RR granules were present and intact near the well-differentiated and poorly differentiated adenocarcinoma cells.CONCLUSION: Mucinous cell carcinoma may release various hydrolases into extra-cellular matrix, inducing degradation of pericancerous matrix and facilitating cancer cell invasion and metastasis.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here