» Articles » PMID: 18454879

Nuclear Localization and Intensity of Staining of Nm23 Protein is Useful Marker for Breast Cancer Progression

Overview
Journal Cancer Cell Int
Publisher Biomed Central
Date 2008 May 6
PMID 18454879
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

Background: Breast cancer is the most common cause of cancer death in the western world. The expression differences of many proteins are associated with breast cancer progression or suppression. The purpose of the study was to determine the expression of nm23 protein in the invasion status and metastatic potential of breast cancer by using tissue microarray and to determine its role in breast cancer based on the expression of nm23 gene product.

Method: nm23 protein expression was examined by immunohistochemistry (IHC) using commercially available tissue microarray containing malignant and normal breast tissues from 216 patients.

Results: a similar percentage of cases showed positive cytoplasmic/nuclear staining for nm23 in normal breast tissue (85.7%), primary breast carcinoma node negative (97.5%) and carcinoma with lymph node metastasis (92.1%). Nuclear localization of staining for nm23 protein was higher in infiltrating ductal carcinoma (IDC) node positive (24.3%) and in matched lymph mode metastasis (18.9%) compared to IDC node negative (4.9%). Strong intensity of cytoplasmic/nucleus staining was observed in IDC node negative (42.6%), in IDC node positive (57.1%), and Infiltrating lobular carcinoma (ILC) node negative (44%) compared to normal breast tissue (16.7%).

Conclusion: nm23 protein expression appears widely expressed in normal breast, early and advanced breast cancer stages. Interestingly our study found that strong staining intensity and nuclear localization of nm23 protein may prove to be a useful marker of breast cancer progression.

Citing Articles

Nuclear enhances the malignant behavior of A549 cells and impacts lung adenocarcinoma patient prognosis.

Xu M, Liu Y, Kuang X, Pu Y, Jiang Y, Zhao X iScience. 2024; 27(7):110286.

PMID: 39055952 PMC: 11269300. DOI: 10.1016/j.isci.2024.110286.


Nuclear functions of NME proteins.

Puts G, Leonard M, Pamidimukkala N, Snyder D, Kaetzel D Lab Invest. 2017; 98(2):211-218.

PMID: 29058704 PMC: 6136249. DOI: 10.1038/labinvest.2017.109.


Extracellular NM23 Protein as a Therapeutic Target for Hematologic Malignancies.

Okabe-Kado J, Kasukabe T, Kaneko Y Adv Hematol. 2011; 2012:879368.

PMID: 21941554 PMC: 3175692. DOI: 10.1155/2012/879368.


Mass spectrometry detection of histidine phosphorylation on NM23-H1.

Lapek Jr J, Tombline G, Friedman A J Proteome Res. 2010; 10(2):751-5.

PMID: 21121676 PMC: 3033978. DOI: 10.1021/pr100905m.


Antimetastatic role of Smad4 signaling in colorectal cancer.

Zhang B, Halder S, Kashikar N, Cho Y, Datta A, Gorden D Gastroenterology. 2009; 138(3):969-80.e1-3.

PMID: 19909744 PMC: 2831103. DOI: 10.1053/j.gastro.2009.11.004.


References
1.
Bertheau P, Steinberg S, Merino M . C-erbB-2, p53, and nm23 gene product expression in breast cancer in young women: immunohistochemical analysis and clinicopathologic correlation. Hum Pathol. 1998; 29(4):323-9. DOI: 10.1016/s0046-8177(98)90111-3. View

2.
Chen S, Wu Y, Shieh H, Yen C, Shen J, Lin K . P53 is a regulator of the metastasis suppressor gene Nm23-H1. Mol Carcinog. 2003; 36(4):204-14. DOI: 10.1002/mc.10110. View

3.
Kamby C . The pattern of metastases in human breast cancer: methodological aspects and influence of prognostic factors. Cancer Treat Rev. 1990; 17(1):37-61. DOI: 10.1016/0305-7372(90)90075-q. View

4.
Hennessy C, Henry J, May F, Westley B, Angus B, Lennard T . Expression of the antimetastatic gene nm23 in human breast cancer: an association with good prognosis. J Natl Cancer Inst. 1991; 83(4):281-5. DOI: 10.1093/jnci/83.4.281. View

5.
Yamaguchi A, Urano T, Goi T, Takeuchi K, Niimoto S, Nakagawara G . Expression of human nm23-H1 and nm23-H2 proteins in hepatocellular carcinoma. Cancer. 1994; 73(9):2280-4. DOI: 10.1002/1097-0142(19940501)73:9<2280::aid-cncr2820730908>3.0.co;2-3. View