Johns Hopkins Kimmel Cancer Center researchers have designed a blood test to detect ovarian cancer using three proteins found in common in the blood of women with the disease. Their preliminary studies with the new test suggest a molecular signature exclusive to this deadly cancer, known for its ability to remain undetected and spread quickly.
The Hopkins test, described in the August 15 issue of Cancer Research, identifies the proteins as a truncated form of transthyretin, a fragment of ITIH4 and apolipoprotein A1, teased out with a rigorous evaluation of protein patterns present in blood samples from ovarian cancer patients at several U.S. and international hospitals. Other research groups are evaluating ovarian cancer blood tests that use protein profiles consisting of tens of thousands of unidentified molecules.
"By identifying a select group of biomarkers specific to ovarian cancer, we not only know the proteins we are dealing with, but we can trace them back to alterations in the genetic code of ovarian cancer cells," says Daniel W. Chan, Ph.D., professor and director of the Biomarker Discovery Center at Johns Hopkins. "We are focusing on the markers for which we have good biological reasoning behind their selection, and hope to expand the panel of markers to catch as many variations in ovarian cancer proteins as possible."
Vanessa Wasta | EurekAlert!
Climate Impact Research in Hannover: Small Plants against Large Waves
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First transcription atlas of all wheat genes expands prospects for research and cultivation
17.08.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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