Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2004-12-1
pubmed:abstractText
Expression of matrilysin-2, matrix metalloproteinase (MMP)-26, has been implicated in the progression of several types of human cancer. Matrilysin-2 has been reported to be a physiological and pathological activator of pro-MMP-9. The aim of this study was to examine matrilysin-2 expression and determine whether it is correlated with progression of human esophageal squamous cell carcinoma (ESCC). Semi-quantitative reverse transcriptase-polymerase chain reaction, immunohistochemical analysis, zymography and an in vitro invasion assay were performed. Matrilysin-2 mRNA expression was undetectable or only faintly detected in non-tumor tissues, but its overexpression was detected in 24 of the 50 ESCC tissues. Matrilysin-2 overexpression was significantly correlated with depth of invasion, lymph node metastasis and an advance in pathological tumor node metastasis (pTNM) stage. Sections with immunostaining signals in >10% of carcinoma cells at the invasive front, which were observed in 46 of 100 cases, were judged to be positive for matrilysin-2 expression. Matrilysin-2 expression was significantly correlated with depth of invasion, lymph node and distant metastasis, advance in pTNM stage and recurrence. Expression of matrilysin-2 was significantly correlated with nuclear beta-catenin expression and MMP-9 expression. Patients with matrilysin-2-positive cancer had significantly shorter overall and disease-free survival periods than did those with matrilysin-2-negative cancer. Matrilysin-2 expression retained its significant predictive value for overall and disease-free survival in multivariate analysis. Moreover, patients with concomitant expression of matrilysin-2 and MMP-9 had the worst prognosis. Zymography revealed that matrilysin-2 expression was significantly correlated with expression of active MMP-9 in ESCC tissues. Matrilysin-2-transfected TE-1 ESCC cells showed active MMP-9 activity and were more invasive in vitro compared with mock-transfected TE-1 cells. The results of this study suggest that matrilysin-2, the expression of which is closely correlated with nuclear beta-catenin expression and active MMP-9 activity, plays a key role in the progression of ESCC.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0143-3334
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2353-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:15333466-Adenocarcinoma, pubmed-meshheading:15333466-Carcinoma, Squamous Cell, pubmed-meshheading:15333466-Cell Nucleus, pubmed-meshheading:15333466-Cytoskeletal Proteins, pubmed-meshheading:15333466-Disease Progression, pubmed-meshheading:15333466-Enzyme Activation, pubmed-meshheading:15333466-Esophageal Neoplasms, pubmed-meshheading:15333466-Female, pubmed-meshheading:15333466-Gene Expression Regulation, Neoplastic, pubmed-meshheading:15333466-Humans, pubmed-meshheading:15333466-Immunoenzyme Techniques, pubmed-meshheading:15333466-Lymphatic Metastasis, pubmed-meshheading:15333466-Male, pubmed-meshheading:15333466-Matrix Metalloproteinase 9, pubmed-meshheading:15333466-Matrix Metalloproteinases, pubmed-meshheading:15333466-Matrix Metalloproteinases, Secreted, pubmed-meshheading:15333466-Middle Aged, pubmed-meshheading:15333466-Neoplasm Invasiveness, pubmed-meshheading:15333466-Neoplasm Recurrence, Local, pubmed-meshheading:15333466-Prognosis, pubmed-meshheading:15333466-RNA, Messenger, pubmed-meshheading:15333466-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15333466-Survival Rate, pubmed-meshheading:15333466-Trans-Activators, pubmed-meshheading:15333466-Transfection, pubmed-meshheading:15333466-beta Catenin
pubmed:year
2004
pubmed:articleTitle
Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma.
pubmed:affiliation
First Department of Internal Medicine, Sapporo Medical University, South-1, West-16, Chuo-ku, Sapporo 060-8543, Japan. h-yama@sapmed.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't