scholarly journals Heparan Sulfate Proteoglycans and Human Breast Cancer Epithelial Cell Tumorigenicity

2014 ◽  
Vol 115 (5) ◽  
pp. 967-976 ◽  
Author(s):  
Rachel K. Okolicsanyi ◽  
Andre J. van Wijnen ◽  
Simon M. Cool ◽  
Gary S. Stein ◽  
Lyn R. Griffiths ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Epithelial Cell ◽  
Heparan Sulfate ◽  
Human Breast Cancer ◽  
Heparan Sulfate Proteoglycans ◽  
Human Breast ◽  
Breast Cancer Epithelial Cell

scholarly journals Direct Visualization of the Human Estrogen Receptor α Reveals a Role for Ligand in the Nuclear Distribution of the Receptor

1999 ◽  
Vol 10 (2) ◽  
pp. 471-486 ◽  
Author(s):  
Han Htun ◽  
Laurel T. Holth ◽  
Dawn Walker ◽  
James R. Davie ◽  
Gordon L. Hager
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Epithelial Cell ◽  
Cell Lines ◽  
Human Breast Cancer ◽  
Estrogen Receptor Α ◽  
Human Breast ◽  
Epithelial Cell Lines ◽  
Human Estrogen Receptor ◽  
Breast Cancer Epithelial Cell

The human estrogen receptor α (ER α) has been tagged at its amino terminus with the S65T variant of the green fluorescent protein (GFP), allowing subcellular trafficking and localization to be observed in living cells by fluorescence microscopy. The tagged receptor, GFP-ER, is functional as a ligand-dependent transcription factor, responds to both agonist and antagonist ligands, and can associate with the nuclear matrix. Its cellular localization was analyzed in four human breast cancer epithelial cell lines, two ER+ (MCF7 and T47D) and two ER− (MDA-MB-231 and MDA-MB-435A), under a variety of ligand conditions. In all cell lines, GFP-ER is observed only in the nucleus in the absence of ligand. Upon the addition of agonist or antagonist ligand, a dramatic redistribution of GFP-ER from a reticular to punctate pattern occurs within the nucleus. In addition, the full antagonist ICI 182780 alters the nucleocytoplasmic compartmentalization of the receptor and causes partial accumulation in the cytoplasm in a process requiring continued protein synthesis. GFP-ER localization varies between cells, despite being cultured and treated in a similar manner. Analysis of the nuclear fluorescence intensity for variation in its frequency distribution helped establish localization patterns characteristic of cell line and ligand. During the course of this study, localization of GFP-ER to the nucleolar region is observed for ER− but not ER+ human breast cancer epithelial cell lines. Finally, our work provides a visual description of the “unoccupied” and ligand-bound receptor and is discussed in the context of the role of ligand in modulating receptor activity.

scholarly journals Interactions of the 67 kDa laminin receptor and its precursor with laminin

2009 ◽  
Vol 30 (2) ◽  
pp. 73-79 ◽  
Author(s):  
Aliya Fatehullah ◽  
Caroline Doherty ◽  
Géraldine Pivato ◽  
George Allen ◽  
Lynda Devine ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Escherichia Coli ◽  
Heparan Sulfate ◽  
Human Breast Cancer ◽  
Biological Activities ◽  
Laminin Receptor ◽  
Human Breast ◽  
Surface Plasmon Resonance Experiment ◽  
Kinetics Of ◽  
Precise Molecular Mechanism

The 67LR (67 kDa laminin receptor) enables cells to interact with components of the extracellular matrix. The molecule is derived from the 37LRP (37 kDa laminin receptor precursor); however, the precise molecular mechanism of this conversion is unknown. Recombinant 37LRP, expressed in and purified from Escherichia coli, bound to human laminin in a SPR (surface plasmon resonance) experiment. 67LR isolated from human breast-cancer-derived cells in culture was also shown to bind to laminin by SPR. However, the kinetics of association are qualitatively different. 37LRP, but not 67LR, binds to heparan sulfate. The binding of 37LRP to heparan sulfate did not affect the interaction of 37LRP with laminin. In contrast, heparan sulfate reduces the extent of binding of laminin to 67LR. Taken together, these results show that 37LRP has some of the biological activities of 67LR, even prior to the conversion event. However, the conversion affects the sites of interaction with both laminin and heparan sulfate.

scholarly journals Oligosaccharide Sequence of Human Breast Cancer Cell Heparan Sulfate with High Affinity for Laminin

1998 ◽  
Vol 273 (33) ◽  
pp. 21111-21114 ◽  
Author(s):  
Narayanan Parthasarathy ◽  
Lisa F. Gotow ◽  
James D. Bottoms ◽  
Timothy E. Kute ◽  
William D. Wagner ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Heparan Sulfate ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Human Breast Cancer ◽  
Human Breast Cancer Cell ◽  
Human Breast ◽  
High Affinity

scholarly journals Differential Expression of Nicotine Acetylcholine Receptors Associates with Human Breast Cancer and Mediates Antitumor Activity of αO-Conotoxin GeXIVA

Marine Drugs ◽  
2020 ◽  
Vol 18 (1) ◽  
pp. 61 ◽  
Author(s):  
Zhihua Sun ◽  
Manqi Zhangsun ◽  
Shuai Dong ◽  
Yiqiao Liu ◽  
Jiang Qian ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Epithelial Cell ◽  
Cell Lines ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Human Breast Cancer ◽  
Acetylcholine Receptors ◽  
Cancer Cell Lines ◽  
Breast Cancer Cell Lines ◽  
Human Breast

Nicotinic acetylcholine receptors (nAChRs) are membrane receptors and play a major role in tumorigenesis and cancer progression. Here, we have investigated the differential expression of nAChR subunits in human breast cancer cell lines and breast epithelial cell lines at mRNA and protein levels and the effects of the αO-conotoxin GeXIVA, antagonist of α9α10 nAChR, on human breast cancer cells. Reverse transcription polymerase chain reaction (PCR) demonstrated that all nAChR subunits, except α6, were expressed in the 20 tested cell lines. Real time quantitative PCR (QRT-PCR) suggested that the mRNA of α5, α7, α9 and β4 nAChR subunits were overexpressed in all the breast cancer cell lines compared with the normal epithelial cell line HS578BST. α9 nAChR was highly expressed in almost all the breast cancer cell lines in comparison to normal cells. The different expression is prominent (p < 0.001) as determined by flow cytometry and Western blotting, except for MDA-MB-453 and HCC1395 cell lines. αO-conotoxin GeXIVA that targeted α9α10 nAChR were able to significantly inhibit breast cancer cell proliferation in vitro and merits further investigation as potential agents for targeted therapy.

scholarly journals A Novel Pathway for Mammary Epithelial Cell Invasion Induced by the Helix-Loop-Helix Protein Id-1

1998 ◽  
Vol 18 (8) ◽  
pp. 4577-4588 ◽  
Author(s):  
Pierre-Yves Desprez ◽  
Claudia Qiao Lin ◽  
Nicole Thomasset ◽  
Carolyn J. Sympson ◽  
Mina J. Bissell ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Mammary Gland ◽  
Epithelial Cell ◽  
Basement Membrane ◽  
Human Breast Cancer ◽  
Mammary Epithelial Cell ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Human Breast ◽  
Helix Loop Helix

ABSTRACT Mammary epithelial cells undergo changes in growth, invasion, and differentiation throughout much of adulthood, and most strikingly during pregnancy, lactation, and involution. Although the pathways of milk protein expression are being elucidated, little is known, at a molecular level, about control of mammary epithelial cell phenotypes during normal tissue morphogenesis and evolution of aggressive breast cancer. We developed a murine mammary epithelial cell line, SCp2, that arrests growth and functionally differentiates in response to a basement membrane and lactogenic hormones. In these cells, expression of Id-1, an inhibitor of basic helix-loop-helix transcription factors, declines prior to differentiation, and constitutive Id-1 expression blocks differentiation. Here, we show that SCp2 cells that constitutively express Id-1 slowly invade the basement membrane but remain anchorage dependent for growth and do not form tumors in nude mice. Cells expressing Id-1 secreted a ∼120-kDa gelatinase. From inhibitor studies, this gelatinase appeared to be a metalloproteinase, and it was the only metalloproteinase detectable in conditioned medium from these cells. A nontoxic inhibitor diminished the activity of this metalloproteinase in vitro and repressed the invasive phenotype of Id-1-expressing cells in culture. The implications of these findings for normal mammary-gland development and human breast cancer were investigated. A gelatinase of ∼120 kDa was expressed by the mammary gland during involution, a time when Id-1 expression is high and there is extensive tissue remodeling. Moreover, high levels of Id-1 expression and the activity of a ∼120-kDa gelatinase correlated with a less-differentiated and more-aggressive phenotype in human breast cancer cells. We suggest that Id-1 controls invasion by normal and neoplastic mammary epithelial cells, primarily through induction of a ∼120-kDa gelatinase. This Id-1-regulated invasive phenotype could contribute to involution of the mammary gland and possibly to the development of invasive breast cancer.

Virus-Like Particles in a Human Breast Cancer: Structural Similarity to Previously Reported Particles

1973 ◽  
Vol 31 ◽  
pp. 378-379
Author(s):  
G. Kasnic ◽  
S. E. Stewart ◽  
C. Urbanski
Keyword(s):  
Breast Cancer ◽  
Biological Activity ◽  
Human Breast Cancer ◽  
Osteogenic Sarcoma ◽  
Human Tumor ◽  
Structural Similarity ◽  
Cell Tumor ◽  
Human Breast ◽  
Human Tumor Cell ◽  
Type Particle

We have reported the maturation of an intracisternal A-type particle in murine plasma cell tumor cultures and three human tumor cell cultures (rhabdomyosarcoma, lung adenocarcinoma, and osteogenic sarcoma) after IUDR-DMSO activation. In all of these studies the A-type particle seems to develop into a form with an electron dense nucleoid, presumably mature, which is also intracisternal. A similar intracisternal A-type particle has been described in leukemic guinea pigs. Although no biological activity has yet been demonstrated for these particles, on morphologic grounds, and by the manner in which they develop within the cell, they may represent members of the same family of viruses.

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