The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here:

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Blocks aquaporins, thereby inhibiting cancer growth

aquaporin. photo.
The picture shows how a drug (orange) attaches to the aquaporin (purple), resulting in the aquaporin no longer being able to transport molecules across the cell membrane. Photo: Raminta Venskutonyte.

Aquaporins are proteins that regulate the flow of water in and out of cells. These proteins have been found to play a role in both cancer and type 2 diabetes. Now, a research group at Lund University has succeeded in finding a drug candidate that binds to the protein, something that has been shown to affect the growth capability of leukemia cells. The study is published in PNAS.

Aquaporins are water channels found in the cell membranes. Their role is to facilitate the transport of water and other smaller molecules to and from cells. In this way, they regulate the flow and pressure within the cell. Aquaporins are central to many mechanisms in our cells, and also play a crucial role in several health conditions such as cancer and type 2 diabetes.

– It seems that cancer cells may increase the number of aquaporins to enhance their own survival and increase their spreading ability, says Karin Lindkvist, professor of cell biology at Lund University and structural biology researcher.

Therefore, it’s interesting to try to develop new drugs that block the activity of aquaporins. But to create new drug candidates, researchers must first gain knowledge of how they bind to aquaporins. Using cryo-electron microscopy, a technology with extremely high resolution, researchers have now, for the first time, managed to produce an image of an aquaporin with a drug candidate bound to the protein. They have also shown that the drug affects the growth capability of leukemia cells by inactivating aquaporins.

– By understanding the structure of the protein, and how drugs attach to it, we are trying to comprehend how cancer cells respond to new drug candidates. This means that we can now begin to develop new and better drug candidates that selectively target certain groups of aquaporins and then proceed to investigate the drug's effectiveness for different types of cancer, concludes Karin Lindkvist.


"Molecular basis for human aquaporin inhibition"
PNAS, 6 Februari 2024.

The study is financed by the Swedish Research Council, Diabetesfonden, Swedish Cancer Society and Chinese Scholarship Council


portrait karin lindkvist. photo

Karin Lindkvist, professor of cell biology at Lund University and structural biology researcher+46 46 734-222786,  karin [dot] lindkvist [at] med [dot] lu [dot] se
Profile in Lund University Research portal

Previously published about Karin Lindkvist's research on aquaporins:
Mapping aquaporins, water channels in cell membranes