On the surface of every living cell, there’s a protein-embedded membrane covered with polysaccharide chains. Cancer cells have an especially thick and pronounced version of this “sugar-coating.”
The thick, slimy coating that would feel like a slug’s skin is a crucial determinant of a cancer cell’s survival. Consisting of long, sugar-decorated molecules called glycoproteins, the coating causes physical changes in the cell membrane that make the cell better able to thrive—leading to a more lethal cancer.
Matthew Paszek, assistant professor of chemical and biomolecular engineering at Cornell University, led the study on glycoprotein-induced cancer cell survival, published online in Nature.
The researchers found that long glycoprotein chains on a cancer cell’s surface cause the cell membrane to push away from its environment and bend inward. This physical change causes adhesion receptors on the cell surface called integrins to clump together.
Integrins bind to protein scaffolds in their environment and regulate pretty much everything a cell does—movement, change, and growth.
This clustering mechanism causes the integrins to alter the cell’s normal signaling, leading to unchecked growth and survival.
The mechanics of this sugar-coating and its subsequent chemical signaling is likely dictated by basic factors like nutrient availability and metabolism—things with implications for diet and genetic makeup, for example, Paszek says.
“Changes to the sugar composition on the cell surface could alter physically how receptors are organized,” he explains. “That’s really the big thing: coupling the regulation of the sugar-coating to these biochemical signaling molecules.”
The Kavli Institute at Cornell for Nanoscale Science supported the Paszek’s work.
Source: Cornell University