Leukemia is known as a type of cancer that attacks the blood. A recent discovered protein is believed to provide insights into the details of the interaction between sperm and egg. Its structure is believed to hold the key to new treatments for the earlier mentioned condition, leukemia. This protein structure was discovered by C.D. Stout at the Scripps Research Institute in La Jolla, California.



Their research has proved the connection between a protein in the eggs of a marine mollusk and the protein on the outside of human white blood cells.

The egg protein was from the California sea snail named Aplysia californica, an animal that is frequently used by biologists in the process of fertilization. As we know, events occur at the molecular level when a sperm cell joins with an egg but these events are similar to those that are seen among the animals and humans too. The premier event that occurs is that a flood of calcium ions is released as a signal for the egg to begin to divide. The flood of the calcium ions is known to be controlled by a regulatory molecule, some kind of molecular switch, termed as a secondary messenger.

The mentioned secondary messenger is synthesized inside the egg from the building blocks of DNA. It is known that the reaction requires a specialized protein known as ADP ribosyl cyclase. This is the protein that we were talking about in the beginning of our article. ADP ribosyl cyclase is the protein that was studied by the researchers at the Scripps. A three dimensional image was reconstructed after preparing the crystals of the protein and after scattering x-rays off them. The image reveals that two of the molecules combine together to create a hole or a molecular cavity between the proteins. In these holes or cavities, the protein traps the DNA building blocks and rearranges their pattern of chemical bonds to synthesize the messenger.

In leukemia patients the white blood cells have a signaling protein called CD38 that for normal cells is present only in the early stages of the condition. It was noticed that molecule CD38 is similar to the cyclase protein that we discussed about earlier and that is why researchers think that CD38 molecules also pair up to create an internal cavity. The main difference between the cyclase and CD38 protein is that CD38 has a tail reaching across the cell membrane providing a means for it to transmit signals to inside the white cells.

Researchers do hope that drugs targeted toward the cavity in CD#* could be useful in allowing the immune system to eliminate leukemia cells.