Most new cancer cases are treated with chemotherapy, but humans naturally express proteins that indiscriminately remove chemotherapy drugs from many cells—including tumor cells, which reduces treatment efficacy.
New research out of St. Jude, along with Australian and English collaborators, has discovered how one of these cellular-cleaning proteins, ABCG2, removes many kinds of chemotherapeutics from a cell and how to prevent it, which could improve future anti-cancer therapies. The findings were published August 18 inChemotherapy involves a course of one or several drugs that usually take the form of small molecules.
"ABCG2 plays a role in clearing toxins and protecting healthy stem cells from chemotherapy and toxic chemotherapeutic agents," said John Schuetz, Ph.D., St. Jude Department of Pharmacy and Pharmaceutical Sciences."We showed a few years ago that ABCG2 levels were quite high in certain subtypes of medulloblastoma, which impacted how much of the drug could get in to kill the
"We were completely puzzled by ABCG2's promiscuity until we did these studies," Schuetz said."We found that unlike some of its genetic family members, which have a very hydrophobic binding pocket, the ABCG2 pocket is dotted with hydrophilic residues as well as hydrophobic ones." The researchers set out to find the exact residues giving ABCG2 the capability to bind and remove hydrophilic molecules. Twostand out within the substrate binding site of ABCG2—a threonine and an asparagine. The distinguishing feature of these amino acids is that they are polar and therefore hydrophilic.
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