Format

Send to

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 1999 Apr 13;257(2):494-9.

Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells.

Author information

1
Laboratory of Cellular Carcinogenesis and Tumor Promotion, National Cancer Institute, Bethesda, Maryland, 20892, USA.

Abstract

To study cellular and subcellular localization of TIMP-1, we constructed a cDNA which would express a chimeric protein, TIMP-1-EGFP, having the enhanced green fluorescent protein of the jelly fish Aequorea victoria fused to the carboxyl-terminus of TIMP-1. Chinese Hamster Ovary (CHO) cells were stably transfected with the TIMP-1-EGFP expressing plasmid. The secreted chimera was processed through the endoplasmic reticulum and Golgi, as was shown by fluorescent confocal microscopy after incubations at temperatures which block processing at the intermediate compartment and the trans-Golgi network. In a co-culture system, secreted TIMP-1-EGFP could be visualized binding to the surface of MCF-7 breast carcinoma cells but not non-neoplastic HBL-100 breast epithelial cells. TIMP-1-EGFP localized to the nucleus of MCF-7 cells after 72 hrs in co-culture. These findings suggest that TIMP-1 may preferentially bind to and be taken up by malignant breast epithelial cells and that TIMP-1 may play a yet unidentified role in nuclear functions.

PMID:
10198240
DOI:
10.1006/bbrc.1999.0408
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Support Center