A motor protein that transports cargo within the cell, km23-1 is also involved in the movement or migration of cells. Migration is necessary for cancer to spread, so understanding this cell movement is important for development of better cancer treatments.
Kathleen Mulder, Ph.D., professor, biochemistry and molecular biology, looked for partner proteins that bind to and cooperate with km23-1 during cell movement, which turned out to include factors that can control proteins actin and RhoA.
"Cell migration is an important aspect of the process of a tumor spreading," Mulder said. "Changes in this process transform tumor cells from local, noninvasive, confined cells to the migrating, metastatic cancer cells."
Cells move through the body using the protein actin, which forms the structural frame of the cell, called the cytoskeleton. The actin creates a protrusion in the cell membrane by forming strands of thread-like fibers on the leading edge of the cell, pushing the cell forward. Several identified proteins regulate the reorganization of the cytoskeleton and are more active in several types of cancers.
Overexpression of km23-1 increases actin fiber formation, whereas when km23-1 is diminished, RhoA activity decreases. RhoA is known to be an important switch, activating processes in migration.
"By knowing that RhoA activity was decreased when km23-1 was reduced, we infer that km23-1 is needed for the regulation of these switches and has a role in cell movement," Mulder said.
To test this in the lab, km23-1 was reduced in a sample of human colon cancer cells. When km23-1 was diminished, cancer cells migrated less. More research needs to be done, but km23-1 may be a promising target for anti-metastatic drugs and cancer therapies to slow the spread of the disease.
"By inhibiting km23-1, you inhibit events that contribute to the cells spreading to other parts of the body," Mulder said.
Results were reported in Biochemical and Biophysical Research Communications.
Other researchers are Qunyan Jin, Nageswara R. Pulipati, Cory M. Staub, of the Department of Biochemistry and Molecular Biology, Penn State College of Medicine; and Weidong Zhou and Lance A. Liotta, Center for Applied Proteomics and Molecular Medicine, George Mason University.
Funding was provided by the National Institutes of Health.
Matthew Solovey | EurekAlert!
Scientists enlist engineered protein to battle the MERS virus
22.05.2017 | University of Toronto
Insight into enzyme's 3-D structure could cut biofuel costs
19.05.2017 | DOE/Los Alamos National Laboratory
Two-dimensional magnetic structures are regarded as a promising material for new types of data storage, since the magnetic properties of individual molecular building blocks can be investigated and modified. For the first time, researchers have now produced a wafer-thin ferrimagnet, in which molecules with different magnetic centers arrange themselves on a gold surface to form a checkerboard pattern. Scientists at the Swiss Nanoscience Institute at the University of Basel and the Paul Scherrer Institute published their findings in the journal Nature Communications.
Ferrimagnets are composed of two centers which are magnetized at different strengths and point in opposing directions. Two-dimensional, quasi-flat ferrimagnets...
An Australian-Chinese research team has created the world's thinnest hologram, paving the way towards the integration of 3D holography into everyday...
In the race to produce a quantum computer, a number of projects are seeking a way to create quantum bits -- or qubits -- that are stable, meaning they are not much affected by changes in their environment. This normally needs highly nonlinear non-dissipative elements capable of functioning at very low temperatures.
In pursuit of this goal, researchers at EPFL's Laboratory of Photonics and Quantum Measurements LPQM (STI/SB), have investigated a nonlinear graphene-based...
Dental plaque and the viscous brown slime in drainpipes are two familiar examples of bacterial biofilms. Removing such bacterial depositions from surfaces is...
For the first time, scientists have succeeded in studying the strength of hydrogen bonds in a single molecule using an atomic force microscope. Researchers from the University of Basel’s Swiss Nanoscience Institute network have reported the results in the journal Science Advances.
Hydrogen is the most common element in the universe and is an integral part of almost all organic compounds. Molecules and sections of macromolecules are...
22.05.2017 | Event News
17.05.2017 | Event News
16.05.2017 | Event News
22.05.2017 | Materials Sciences
22.05.2017 | Life Sciences
22.05.2017 | Physics and Astronomy