» Articles » PMID: 16495931

Expression of a Disintegrin and Metalloprotease (ADAM and ADAMTS) Enzymes in Human Non-small-cell Lung Carcinomas (NSCLC)

Overview
Journal Br J Cancer
Specialty Oncology
Date 2006 Feb 24
PMID 16495931
Citations 39
Authors
Affiliations
Soon will be listed here.
Abstract

A Disintegrin and Metalloprotease (ADAM) are transmembrane proteases displaying multiple functions. ADAM with ThromboSpondin-like motifs (ADAMTS) are secreted proteases characterised by thrombospondin (TS) motifs in their C-terminal domain. The aim of this work was to evaluate the expression pattern of ADAMs and ADAMTS in non small cell lung carcinomas (NSCLC) and to investigate the possible correlation between their expression and cancer progression. Reverse transcriptase-polymerase chain reaction (RT-PCR), Western blot and immunohistochemical analyses were performed on NSCLC samples and corresponding nondiseased tissue fragments. Among the ADAMs evaluated (ADAM-8, -9, -10, -12, -15, -17, ADAMTS-1, TS-2 and TS-12), a modulation of ADAM-12 and ADAMTS-1 mRNA expression was observed. Amounts of ADAM-12 mRNA transcripts were increased in tumour tissues as compared to the corresponding controls. In sharp contrast, ADAMTS-1 mRNA levels were significantly lower in tumour tissues when compared to corresponding nondiseased lung. These results were corroborated at the protein level by Western blot and immunohistochemistry. A positive correlation was observed between the mRNA levels of ADAM-12 and those of two vascular endothelial growth factor (VEGF)-A isoforms (VEGF-A(165) and VEGF-A(121)). Taken together, these results providing evidence for an overexpression of ADAM-12 and a lower expression of ADAMTS-1 in non-small-cell lung cancer suggest that these proteases play different functions in cancer progression.

Citing Articles

Decoding tumor heterogeneity in uveal melanoma: basement membrane genes as novel biomarkers and therapeutic targets revealed by multi-omics approaches for cancer immunotherapy.

Li Y, Cai H, Yang J, Xie X, Pei S, Wu Y Front Pharmacol. 2023; 14:1264345.

PMID: 37822877 PMC: 10562578. DOI: 10.3389/fphar.2023.1264345.


The emerging roles of lysine-specific demethylase 4A in cancer: Implications in tumorigenesis and therapeutic opportunities.

Yang G, Li C, Tao F, Liu Y, Zhu M, Du Y Genes Dis. 2023; 11(2):645-663.

PMID: 37692513 PMC: 10491877. DOI: 10.1016/j.gendis.2022.12.020.


Transcriptome and methylome sequencing reveals altered long non-coding RNA genes expression and their aberrant DNA methylation in equine sarcoids.

Semik-Gurgul E, Gurgul A, Szmatola T Funct Integr Genomics. 2023; 23(3):268.

PMID: 37552338 PMC: 10409845. DOI: 10.1007/s10142-023-01200-2.


ADAMTS-1 inhibits angiogenesis via the PI3K/Akt-eNOS-VEGF pathway in lung cancer cells.

Wang B, Chen S, Zhao J, Xiang B, Gu X, Zou F Transl Cancer Res. 2022; 8(8):2725-2735.

PMID: 35117030 PMC: 8798392. DOI: 10.21037/tcr.2019.10.34.


In Silico Identification of Contradictory Role of ADAMTS5 in Hepatocellular Carcinoma.

Zhu Z, Xu J, Wu X, Lin S, Li L, Ye W Technol Cancer Res Treat. 2021; 20:1533033820986826.

PMID: 33522433 PMC: 7871357. DOI: 10.1177/1533033820986826.


References
1.
Luque A, Carpizo D, Iruela-Arispe M . ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J Biol Chem. 2003; 278(26):23656-65. DOI: 10.1074/jbc.M212964200. View

2.
Wu E, Croucher P, McKie N . Expression of members of the novel membrane linked metalloproteinase family ADAM in cells derived from a range of haematological malignancies. Biochem Biophys Res Commun. 1997; 235(2):437-42. DOI: 10.1006/bbrc.1997.6714. View

3.
Asakura M, Kitakaze M, Takashima S, Liao Y, Ishikura F, Yoshinaka T . Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat Med. 2002; 8(1):35-40. DOI: 10.1038/nm0102-35. View

4.
Sounni N, Roghi C, Chabottaux V, Janssen M, Munaut C, Maquoi E . Up-regulation of vascular endothelial growth factor-A by active membrane-type 1 matrix metalloproteinase through activation of Src-tyrosine kinases. J Biol Chem. 2004; 279(14):13564-74. DOI: 10.1074/jbc.M307688200. View

5.
Werb Z, Vu T, Rinkenberger J, Coussens L . Matrix-degrading proteases and angiogenesis during development and tumor formation. APMIS. 1999; 107(1):11-8. DOI: 10.1111/j.1699-0463.1999.tb01521.x. View