Certain types of cancers seem to show resistance to treatments that in earlier stages are very effective. An example of this is the breast cancer fighting drug known as Tamoxifan. In early stages, it is a standard drug to prescribe because of its effectiveness. But in later stages, it appears to have no effect whatsoever.

University of Rochester researchers believe they have isolated the difference between the two stages that causes this stymie. They have isolated a specific protein. that seems to make the difference. And with it, they may have discovered a way to extend the treatment of breast and other forms of cancer well beyond the early stages:

Led by doctoral student Hsing-Yu Chen and Mark Noble, Ph.D., professor of Biomedical Genetics at URMC, the team studied the molecular mechanism that allows basal-like breast cancer cells to escape the secondary effects of tamoxifen, and discovered that two proteins are critical in this escape. One protein, called c-Cbl, controls the levels of multiple receptors that are critical for cancer cell function. A second protein, Cdc42, can inhibit c-Cbl and is responsible for the tumor’s underlying resistance.

The team also discovered that targeting Cdc42 – and thus inhibiting the inhibitor – with an experimental drug compound known as ML141 restored c-Cbl’s normal function. Through additional work in animal models and in human cell cultures, the team demonstrated that when ML141 is paired with tamoxifen, it enhances the ability of tamoxifen to induce cancer cell death and suppress the growth of new cancer cells. Neither drug alone had the same effect on basal-like breast cells.

So in the future, a one / two punch of Tamoxifan and ML141 may be the program of choice when dealing with this difficult cancer.

The biggest concern with anti-bacterial soaps and the like is essentially the fast-forward nature of Darwinism in single-cell organisms. You kill all the bacteria that are susceptible to Anti-Bac A and the ones that are left get a wide-open ecosystem with none of their weaker brethren to hinder their reproduction. Before long, none of the bacteria that used to be weakened by Anti-Bac A are around, leaving you to find Anti-Bac B in a hurry. Because the new bacteria are wiping people out.

But researchers at the University of Rochester are aiming at another, more effective way to deal with bacteria. One that doesn’t allow them to evolve around the latest defense, because it goes to the core of how cells – any cells, really – operate. The new theory is that we may someday be able to interrupt the processing of two key proteins used in ribosomes. Ribosomes are the protein-creating organelle in the cell. Without properly-functioning ribosomes, no cell can live. Interrupt these two key proteins and you kill the cell:

They discovered that two proteins already present in E. coli cells—RbfA and KsgA—need to be in balance with each other in order for ribosomes to function. If those proteins are present in the wrong concentrations, the ribosomes will not mature properly and will be unable to produce proteins, leading to the death of the cells. Their findings are being published this week in the journal Molecular Microbiology.

Researching, cataloging and analyzing proteins is one of the major biological research competencies of the Rochester area. Another research project at RIT discovered the protein required to allow photosynthesis in algae. Once again, finding a path to disrupt the use of this particular protein would create an organism-specific means to control an undesirable population.

In this case, researchers are again focusing on a specific species – E. Coli – but identifying similar proteins in other species would work as well.

The goal of soon stopping the aging process entirely is something Ray Kurzweil swears by, and for this he gets a lot of criticism. But U of R scientists have recently discovered that a protein named SIRT6 extends the lifespans of mice, and this is a step towards its application in our own bodies. Although this may seem like a menial leap, the team plans on using their research to eventually extend a person’s life and treat cancer.

This makes me wonder what societal changes will be made about the collective perception of an average lifespan. In my lifetime, will it be normal for me to live out 120 years before passing away? Will that be the norm? I’m not sure what to expect, but with great jumps in medicine and the exponential growth of technology, I’m wondering if I really will see these breakthroughs in my life.

Enhancing the way cells repair DNA increases lifespan, U of R scientists found. By overexpressing the SIRT6 protein, DNA repair by cells can take place for an extended amount of time. Old cells are 38 times less efficient at repairing critically broken DNA than younger ones, and SIRT6 lowers this number. Vera Gorbunova, one of the U of R scientists, sums the idea up well:

“Our research looked at DNA repair and found a reason for the longevity, and that is SIRT6’s role in promoting more efficient DNA repair.”

With a recent poll showing that nearly half of Americans either feel they look their age or older than their age, it’s clear U of R scientists are headed in the right direction. Medicine is evolving into a practice that caters to the needs of the masses and to the wants of the masses as well. Whether fiddling with our lifespan is ethical or not is beyond my capacity for a philosophical discussion, but I’m excitedly waiting for the day I can enhance the way my cells repair DNA, entirely avoid any terminal illnesses like cancer, and maybe even live well past 120.

There are a few very particular races happening in the world of medical science that are probably at least as important to our current era as the Space Race was to the Nuclear Age, but they receive very little press, indeed.

The first is the race to map and contextualize the genomes of the various species on the planet. The sequencing and understanding of the various blocks of data found within the genome – basically, the framework of DNA upon which every individual of a species is built – is yielding unprecedented discoveries about the way biotic systems go together.

But that isn’t the only one. Another hugely-important race is the race to identify all the various forms of protein that exist in life on the planet. Proteins perform a wide variety of functions in the body; we generally accept that you need to eat protein so your body can build muscle and bone. But these are not the only functions of proteins.

For example, DFE recently reported on Professor Andre Hudson’s research on the protein involved in allowing algae to photosynthesize. In this case, the protein is an enzyme that allows the photosythetic process to happen. Once identified, researchers can find ways to arrest photosynthesis in a single species of algae, thus controlling it while leaving the rest of the ecosystem intact.

RIT just recently published a presser on colleagues of Professor Hudson’s and the project to map out all known forms of proteins. The idea of this project is geared at the second phase of Dr Hudson’s research and others: by creating a single database with all the protein information you need, technologists and companies can use the data to create their own solutions to biological problems.

At the same time, in addition to knowing what the protein is, knowing how it is formed is equally important. Researchers elsewhere in the community are finding that gamers are doing some of the best work figuring out how the “game theory” of protein shapes work best.

The pace of this research is breath-taking. The consequences of mapping the genomes of every species on Earth and knowing every protein out there is pretty staggering. Honestly, its also a little bit scary. Which is why the lack of proper coverage in mainstream circles is more than a little upsetting.

It is ironic that the mainstream media is focused on the trial of a celebrity doctor who proscribed drugs to a willing patient while the whole of our understanding of biology – to say nothing of the relatively narrow field of medicine – passes them by.