Laminin, long thought to be only a structural support protein in the microenvironment of breast and other epithelial tissues, is "famous" for its cross-like shape.
However, laminin is far more than just a support player with a "pretty face." Two studies led by one of the world's foremost breast cancer scientists have shown how laminin plays a central role in the development of breast cancer, the second most common cancer and second leading cause of cancer death among women in the United States. In one study it was shown how laminin influences the genetic information inside a cell's nucleus. In the other study it was shown how destruction of laminin can play a detrimental role in the early stages of tumor development.
Mina Bissell holds the title of "Distinguished Scientist" with the U.S. Department of Energy (DOE)'s Lawrence Berkeley National Laboratory (Berkeley Lab). She herself is famous for having discovered the critical role in breast cancer development played by the extracellular matrix (ECM), the network of fibrous and globular proteins surrounding a breast cell. Her "dynamic reciprocity" theory holds that the fate of cells whether they stay healthy or become cancerous hinges on the chemical signals exchanged between the ECM and a cell's nucleus. In these latest studies, Bissell and her collaborators focused on laminin and its connections with two other proteins actin, a cytoplasmic protein that has been linked to nuclear activities; and MMP9, an enzyme that is secreted outside the cells and is known to break down ECM constituents.
Laminin and Cell Quiescence
"Quiescence" is the process by which a biological cell stops growing or dividing. This is the opposite of a cancerous state, in which cell growth and division is often unchecked. Signals from laminin-111, an ECM protein that helps the cell and its ECM stick together, have been linked to cell quiescence but the mechanism was unknown. Bissell and postdocto
|Contact: Lynn Yarris|
DOE/Lawrence Berkeley National Laboratory