Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 2 de 2
Filter
Add filters








Year range
1.
KMJ-Kuwait Medical Journal. 2015; 47 (1): 17-23
in English | IMEMR | ID: emr-161680

ABSTRACT

To investigate the clinical significance of aberrant hypoxia inducible factor-la [HIF-la], matrix metalloproteinase-2 [MMP-2], and E-cadherin expression in rectal adenocarcinoma. Prospective study.Chongqing Medical University, Chinese Ministry of Education Key Laboratory of Child Development and Disorders, Chongqing Provincial Key Laboratory of Pediatrics, Chongqing, China A total of 88 rectal adenocarcinoma tissues and 12 normal mucosa specimens were included in the study. The expression of HIF-la, MMP-2 and E-cadherin protein were detected by using immunohistochemistry. Clinico-pathological factors associated with expression of HIF-la, MMP-2, and E-cadherin were analyzed using the x[2] test. Survival curves were plotted according to the Kaplan-Meier method. HIF-la, MMP-2, and E-cadherin protein expression Results: HIF-la, MMP-2, and E-cadherin proteins were expressed in 65.9%, 71.6%, and 28.4% of rectal cancer tissues, respectively. However, HIF-la and MMP-2 proteins were not expressed, but E-cadherin protein was strongly expressed in 12 normal tissue samples. Altered HIF-la and MMP-2 protein expression was associated with lymph node and distant metastases and Duke's classification, while loss of E-cadherin protein expression was associated with tumor de-differentiation and lymph node and distant metastases. Combining these three markers together, the association was even more significant. Kaplan-Meier curve analysis showed that HIF-la and MMP-2 protein expression but loss of E-cadherin protein expression significantly contributed to poor overall patient survival. Altered HIF-la, MMP-2, and E-cadherin protein expression significantly contributed to the progression of rectal carcinoma and poorer patient survival

2.
Chinese Journal of Otorhinolaryngology Head and Neck Surgery ; (12): 934-938, 2007.
Article in Chinese | WPRIM | ID: wpr-309387

ABSTRACT

<p><b>OBJECTIVE</b>To establish two-dimensional electrophoresis profiles from human laryngeal squamous cell carcinoma tissue and paired normal tumor-adjacent mucosa epithelia tissue, and to identify differential expression proteins.</p><p><b>METHODS</b>The total proteins of human laryngeal squamous carcinoma tissue and paired normal tumor-adjacent mucosa epithelia tissue were separated by immobilized pH gradient-based two-dimensional gel electrophoresis (2-DE). The differential expression proteins were analyzed using image analysis software, then identified using mass spectrometry and database searching.</p><p><b>RESULTS</b>Well-resolved, reproducible 2-DE patterns of laryngeal squamous cell carcinoma and adjacent normal mucosa epithelial were obtained. Differential protein spots were defined as spots in 2-DE gels. Thirteen proteins were preliminarily identified, naming which 10 proteins were upregulated in laryngeal cancer tissue. Such as cofilin-1, nuclear body protein SP140, GRP94, HSP 90, GSTP1-1, superoxide dismutase [Mn], cyclophilin A, proteasome activator complex subunit 2, apolipoprotein A-I precursor, CaM-like protein and so on. There were 3 proteins downregulated in laryngeal cancer tissue, which were fatty acid-binding protein, calgranulin A and calgranulin B.</p><p><b>CONCLUSIONS</b>Thirteen proteins which are associated with the tumorigenesis of the laryngeal squamous cell carcinoma were characterized. These extensive protein variations indicate that multiple protein molecules should be simultaneously targeted as an effective strategy to counter the disease. It is better for understanding of the oncogenesis and pathogenesis in a global way, which in turn is a basis-for the rational designs of diagnostic and therapeutic methods.</p>


Subject(s)
Aged , Humans , Male , Middle Aged , Carcinoma, Squamous Cell , Metabolism , Laryngeal Neoplasms , Metabolism , Neoplasm Proteins , Metabolism , Proteomics , Methods
SELECTION OF CITATIONS
SEARCH DETAIL