» Articles » PMID: 11242804

Expression of Tissue Inhibitors of Metalloproteinases (TIMPs) in Hepatocellular Carcinoma

Overview
Specialty General Medicine
Date 2001 Mar 13
PMID 11242804
Citations 3
Authors
Affiliations
Soon will be listed here.
Abstract

Background: Matrix metalloproteinases (MMPs) have been implicated in the remodelling of extracellular matrix (ECM), including basement membrane. ECM remodelling is associated with pathological processes, including hepatic fibrosis, tumor invasion and metastasis. Tissue inhibitors of metalloproteinase (TIMP)-1 and TIMP-2 were known to inhibit MMP-9 and MMP-2, respectively. In the present study, we examined the expression of TIMP-1 and TIMP-2 in surgical specimen pairs of hepatocellular carcinoma and nontumoral liver and the correlation between their expression and clinicopathological characteristics.

Methods: The localization of both transcripts and protein of TIMP-1 and TIMP-2 was studied by using in situ hybridization and immunohistochemistry.

Results: TIMP-1 and TIMP-2 mRNA transcripts were found in tumor cells, hepatocyte, sinusoidal cells, endothelial cells and stromal cells. Signal intensity of TIMP-1 was stronger than that of TIMP-2. The results of immunohistochemical stainings were concordant with those obtained by in situ hybridization. Expression of TIMP-1 and TIMP-2 was observed in tumorous tissue, in nontumorous tissue and in the portions of the tumors adjacent to the capsules. However, a clear difference in TIMP-1 and TIMP-2 mRNA expression was not observed among the three tissue types. The intensity of TIMP-2 expression was generally weaker than that of TIMP-1, and the intensity of TIMP-1 and TIMP-2 mRNA expression did not correlate with variable clinicopathological characteristics.

Conclusion: TIMPs was expressed in tumor cells and many cell types of the nontumoral liver. Further investigations for TIMPs' unknown functional role are needed.

Citing Articles

Liver Disease: Induction, Progression, Immunological Mechanisms, and Therapeutic Interventions.

Neshat S, Quiroz V, Wang Y, Tamayo S, Doloff J Int J Mol Sci. 2021; 22(13).

PMID: 34202537 PMC: 8267746. DOI: 10.3390/ijms22136777.


Radix Tetrastigma hemsleyani flavone inhibits proliferation, migration, and invasion of human lung carcinoma A549 cells.

Zhong L, Zheng J, Sun Q, Wei K, Hu Y Onco Targets Ther. 2016; 9:635-41.

PMID: 26893573 PMC: 4745953. DOI: 10.2147/OTT.S92707.


Usefulness of MMP-9/TIMP-1 in predicting tumor recurrence in patients undergoing curative surgical resection for gastric carcinoma.

Seo Y, Park J, Kim J, Kim J, Yeon J, Kim J Dig Dis Sci. 2007; 52(3):753-9.

PMID: 17237995 DOI: 10.1007/s10620-006-9535-0.

References
1.
BISSELL D, Friedman S, Maher J, Roll F . Connective tissue biology and hepatic fibrosis: report of a conference. Hepatology. 1990; 11(3):488-98. DOI: 10.1002/hep.1840110322. View

2.
DErrico A, Garbisa S, Liotta L, Castronovo V, Stetler-Stevenson W, Grigioni W . Augmentation of type IV collagenase, laminin receptor, and Ki67 proliferation antigen associated with human colon, gastric, and breast carcinoma progression. Mod Pathol. 1991; 4(2):239-46. View

3.
Gressner A, Bachem M . Cellular sources of noncollagenous matrix proteins: role of fat-storing cells in fibrogenesis. Semin Liver Dis. 1990; 10(1):30-46. DOI: 10.1055/s-2008-1040455. View

4.
Ries C, Petrides P . Cytokine regulation of matrix metalloproteinase activity and its regulatory dysfunction in disease. Biol Chem Hoppe Seyler. 1995; 376(6):345-55. View

5.
Murawaki Y, Yamada S, Koda M, Hirayama C . Collagenase and collagenolytic cathepsin in normal and fibrotic rat liver. J Biochem. 1990; 108(2):241-4. DOI: 10.1093/oxfordjournals.jbchem.a123187. View