Literature DB >> 11641616

The expression of thymidine phosphorylase suppresses spontaneous apoptosis of cancer cells in esophageal squamous cell carcinoma.

M Ikeguchi1, T Sakatani, T Ueta, K Fukuda, K Yamaguchi, S Tsujitani, N Kaibara.   

Abstract

OBJECTIVE: Thymidine phosphorylase (TP) is an enzyme which converts thymidine to thymine. TP is expressed in a variety of human carcinomas and is known to be a potent angiogenic factor. A recent in vitro study indicated that TP is involved in the intracellular apoptotic signal transduction pathway. The aim of this study was to investigate the correlations between the expression of TP, microvessel density (MVD) and the occurrence of spontaneous apoptosis in esophageal squamous cell carcinoma (ESCC).
METHODS: The expression of TP, intratumoral MVDs and percentages of apoptotic cancer cells, expressed by the apoptotic index (AI), of 155 tumors from 155 patients with ESCC were analyzed by immunohistochemistry and compared.
RESULTS: Positive TP expression in cancer and stromal cells was detected in 89 (57.4%) and 104 (67.1%) cases, respectively. The mean MVD and mean AI of the 155 tumors were 288/mm(2) (range: 36-668/mm(2)) and 2.1% (range: 0-20.4%). The mean MVD of 104 tumors with TP-positive stromal cells (336/mm(2)) was higher than that of 51 tumors with TP-negative stromal cells (188/mm(2), p < 0.001). However, the mean MVD of 89 tumors with TP-positive cancer cells (293/mm(2)) did not differ from that of 66 tumors with TP-negative cancer cells (280/mm(2), p = 0.509). On the other hand, the mean AI of 89 tumors with TP-positive cancer cells (1.2%) was lower than that of 66 tumors with TP-negative cancer cells (3.4%, p < 0.001). However, the mean AI of 104 tumors with TP-positive stromal cells (1.9%) did not differ from that of 51 tumors with TP-negative stromal cells (2.6%, p = 0.058). No significant correlation between the MVDs and the AIs was observed (rho = -0.067, p = 0.409).
CONCLUSION: In ESCC, TP may play an important role in tumor progression by increasing microvessels and suppressing apoptosis of cancer cells. Copyright 2001 S. Karger AG, Basel

Entities:  

Mesh:

Substances:

Year:  2001        PMID: 11641616     DOI: 10.1159/000048756

Source DB:  PubMed          Journal:  Pathobiology        ISSN: 1015-2008            Impact factor:   4.342


  3 in total

Review 1.  Thymidine phosphorylase: A potential new target for treating cardiovascular disease.

Authors:  Wei Li; Hong Yue
Journal:  Trends Cardiovasc Med       Date:  2017-10-20       Impact factor: 6.677

2.  Expression of thymidine phosphorylase in lymph nodes involved with mycosis fungoides and sézary syndrome.

Authors:  Xingcao Nie; Rekha Bhat; Essel Dulaimi Al-Saleem; Eric C Vonderheid; J Steve Hou
Journal:  Adv Hematol       Date:  2011-11-14

Review 3.  The dual role of thymidine phosphorylase in cancer development and chemotherapy.

Authors:  Annelies Bronckaers; Federico Gago; Jan Balzarini; Sandra Liekens
Journal:  Med Res Rev       Date:  2009-11       Impact factor: 12.944

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.