Improvements in optical mammography to advance breast cancer diagnostics

Researchers from Politecnico di Milano, Italy report improvements in the design of optical mammography used in diagnosis and monitoring of breast cancer.  They report increase sensitivity by a thousandfold.This research is presented at Biomedical Optics meeting 2018.

Schematic diagram of new and improved optical mammography device.
Credit: Edoardo Ferocino

Optical mammography uses infrared light and is used in conjunction with x-rays. It is optimal in cases needing repeated imaging to prevent high amounts of radiation associated with the regular procedure. Optical mammography can be used to measure blood volume, oxygenation, lipid, water and collagen content for a suspicious area identified through standard X-ray imaging. However, there are limitations to using optical mammography, which includes poor spatial resolution.

New improvements include using eight channel silicon photomultipliers (SiPMs) and multichannel time-to-digital converter instead of two photomultiplier tubes (PMTs) in existing optical mammography instruments. These changes eliminate the pre-scan step that was required to avoid damage to the photomultiplier tubes. In addition to increased sensitivity, the new instrument is both more robust and cheaper.

The investigators in Milan are working with a larger consortium on a project known as SOLUS, “Smart Optical and Ultrasound Diagnostics of Breast Cancer.” This project is funded by the European Union through the Horizon 2020 Research and Innovation Program and aims to combine optical imaging methods with ultrasound to improve specificity in the diagnosis of breast cancer.

Adapted from press release by the Optical Society.

Using ribosomal protein expression patterns as cancer biomarker

A research team at the University of Basel’s Biozentrum has investigated the expression of ribosomal proteins in a wide range of human tissues including tumors and discovered a cancer type specific signature. The study is reported in journal Genome Biology. Researchers think that these signature could be used for predicting progression and survival.

Gene expression level of individual ribosomal proteins (RP) in different types of cancer (blue: lower level; red: higher level compared to normal tissue). Credit: Mihaela Zavolan and Joao Guimaraes, University of Basel, Biozentrum

Prof. Mihaela Zavolan’s research group at the Biozentrum of the University of Basel has now discovered that about a quarter of the ribosomal proteins have tissue-specific expression and that different cancer types have their own individual expression pattern of ribosomal proteins. In the future, these patterns may serve as a prognostic marker for cancer and may point towards new therapeutic opportunities.

Mihaela Zavolan and her co-worker Joao Guimaraes have systematically analyzed ribosomal protein expression in thirty tissue types, three hundred different cell types and sixteen different types of tumors, such as lung and breast cancer. In contrast to previous assumptions, they found a wide variability in ribosomal protein gene expression. In particular, hematopoietic and tumor cells display the most complex expression pattern.

“For us, it was really impressive to see that consistent signatures emerged for the different cancer types after the analysis of distinct data sets including patient samples,” explains first author Guimaraes. “The pattern of the dysregulated proteins is very striking, whereby the expression of some ribosomal proteins is systematically reduced, and of others increased in cancer cells. This suggests that individual ribosomal proteins can either suppress or promote tumorogenesis.”

Furthermore, the scientists discovered a strong relationship between the “signature” in breast cancer and the relapse-free survival. “We were quite surprised to find that the expression level of just three ribosomal proteins allows a fairly accurate prognosis of disease progression, comparable to the best predictive markers that are currently known”, Zavolan points out.

“Our study demonstrates the potential of such expression signatures for the prognosis and perhaps a diagnosis of cancer. We are especially interested in studying the functions of individual ribosomal proteins and hopefully opening the door for new therapeutic options,” explains the scientist.
Citation: Guimaraes, Joao C., and Mihaela Zavolan. “Patterns of ribosomal protein expression specify normal and malignant human cells.” Genome Biology 2016 17:236.
DOI: 10.1186/s13059-016-1104-z
Adapted from press release by University of Basel.

Piperlongumine, chemical from Indian pepper plant inhibits enzyme in cancer cells

UT Southwestern Medical Center scientists have uncovered the chemical process behind anti-cancer properties of a spicy Indian pepper plant called the long pepper, whose suspected medicinal properties date back thousands of years. The study is published in the Journal of Biological Chemistry.

Dr. Westover’s lab used X-ray crystallography to create this molecular model of piperlongumine.
Credit: UT Southwestern

The secret lies in a chemical called Piperlongumine (PL), which has shown activity against many cancers including prostate, breast, lung, colon, lymphoma, leukemia, primary brain tumors, and gastric cancer.

Using x-ray crystallography, researchers were able to create molecular structures that show how the chemical is transformed after being ingested. Piperlongumine (PL) converts to hPiperlongumine (hPL), an active drug that silences a gene called GSTP1. The GSTP1 gene produces a detoxification enzyme Glutathione S-Transferase Pi 1 that is often overly abundant in tumors.

“We are hopeful that our structure will enable additional drug development efforts to improve the potency of PL for use in a wide range of cancer therapies,” said Dr. Kenneth Westover, Assistant Professor of Biochemistry and Radiation Oncology. “This research is a spectacular demonstration of the power of x-ray crystallography.”

Dr. Westover, a member of the Harold C. Simmons Comprehensive Cancer Center, used cutting edge technologies in UT Southwestern’s Structural Biology Core (SBC) – the University’s world-renowned facility for X-ray crystallography, to better understand the anticancer properties of Piperlongumine (PL). X-ray crystallography allows scientists to determine molecular structures that reveal how molecules interact with targets – in this case how Piperlongumine (PL) interacts with GSTP1. Viewing the structures helps in developing drugs for those targets.

Citation: Harshbarger, Wayne, Sudershan Gondi, Scott B. Ficarro, John Hunter, Durga Udayakumar, Deepak Gurbani, William Singer, Yan Liu, Lianbo Li, Jarrod A. Marto and Kenneth D. Westover. “Structural and Biochemical Analyses Reveal the Mechanism of Glutathione S-Transferase Pi 1 Inhibition by the Anti-cancer Compound Piperlongumine.” Journal of Biological Chemistry (2016): jbc-M116.
DOI: 10.1074/jbc.M116.750299
Research funding: V Foundation for Cancer Research, Welch Foundation, and Cancer Prevention and Research Institute of Texas.
Adapted from press release by UT Southwestern Medical Center.

Calcium channel blockers used for hypertension has potential to block cancer invasion

By screening already approved drugs, the team led by Postdoctoral Researcher Guillaume Jacquemet and Academy Professor Johanna Ivaska has discovered that calcium channel blockers can efficiently stop cancer cell invasion in vitro. Calcium channel blockers are currently used to treat hypertension, also known as high blood pressure, but their potential use in blocking cancer cell metastases has not been previously reported.

High-resolution microscope image of an invasive breast cancer cell (magenta) expressing
Myosin-10 induced “sticky-fingers” (green). Credit: Dr Guillaume Jacquemet, University of Turku.

Cancer kills because of its ability to spread throughout the body and form metastases. Therefore, developing drugs that block the ability of cancer cells to disseminate is a major anti-cancer therapeutic avenue. Developing new drugs, however, is a very lengthy and expensive process and many promising drugs fail clinical trials because of unanticipated toxicity and side effects. Thus, finding new targets for drugs already in use to treat other diseases, in other words, drug repurposing, is an emerging area in developing anti-cancer therapies.

Identification of anti-hypertension drugs as potential therapeutics against breast and pancreatic cancer metastasis was a big surprise. The targets of these drugs were not known to be present in cancer cells and therefore no one had considered the possibility that these drugs might be effective against aggressive cancer types, says Professor Ivaska.

For several years, the research team from the Turku Centre for Biotechnology lead by Professor Johanna Ivaska has focused their efforts on understanding how cancer cells move and invade surrounding tissue. The team has identified that aggressively spreading cancer cells express a protein called Myosin-10 which drives cancer cell motility.

Myosin-10 expressing cancers have a large number of structures called filopodia. They are sticky finger-like structures the cancer cells extend to sense their environment and to navigate – imagine a walking blind spider, explains Dr. Jacquemet.

The team found that calcium channel blockers target specifically these sticky fingers rendering them inactive, thus efficiently blocking cancer cell movement. This suggests that they might be effective drugs against cancer metastasis. However, at this stage, much more work is required to assess if these drugs would be efficient against cancer progression.

The team and their collaborators are currently assessing the efficiency of calcium channel blockers to stop the spreading of breast and pancreatic cancer using pre-clinical models and analyzing patient data. The findings were published in Nature Communications journal.

Citation: Jacquemet, Guillaume, Habib Baghirov, Maria Georgiadou, Harri Sihto, Emilia Peuhu, Pierre Cettour-Janet, Tao He, Merja Perälä, Pauliina Kronqvist, Heikki Joensuu & Johanna Ivaska. “L-type calcium channels regulate filopodia stability and cancer cell invasion downstream of integrin signalling.” Nature Communications 7 (2016): 13297.
DOI:10.1038/ncomms13297
Adapted from press release by the University of Turku.

Trastuzumab biosimilar (MYL-14010) shown effective in breast cancer clinical trial

Among women with metastatic breast cancer, treatment with a drug that is biosimilar to the breast cancer drug trastuzumab resulted in an equivalent overall response rate at 24 weeks compared with trastuzumab, according to a study published online by JAMA.

Trstuzumab Biosimilars
Biological agents, including monoclonal antibodies, have increased the treatment options and greatly improved outcomes for a number of cancers. However, patient access to these biologics is limited in many countries. With impending patent expiration of some biological agents, development of biosimilars has become a high priority for drug developers and health authorities throughout the world to provide access to high-quality alternatives. A biosimilar drug is a biological product that is highly similar to a licensed biological product, with no clinically meaningful differences in terms of safety or potency.

Treatment with the anti-ERBB2 humanized monoclonal antibody trastuzumab and chemotherapy significantly improves progression-free and overall survival in patients with ERBB2 (HER2)-positive metastatic breast cancer. In this multicenter, phase 3 study, Hope S. Rugo, M.D., of the University of California San Francisco Helen Diller Family Comprehensive Cancer Center, and colleagues randomly assigned patients with ERBB2-positive metastatic breast cancer to receive a proposed trastuzumab biosimilar (MYL-14010) (n = 230) or trastuzumab (n = 228) with a taxane (a chemotherapy agent) to compare the overall response rate and safety after 24 weeks. Chemotherapy was administered for at least 24 weeks followed by antibody alone until unacceptable toxic effects or disease progression occurred. Tumor was assessed every 6 weeks. The primary outcome was week 24 overall response rate defined as complete or partial response.

The overall response rate was 70 percent for the proposed biosimilar vs 64 percent for trastuzumab. At week 48, there was no statistically significant difference with the proposed biosimilar vs trastuzumab for time to tumor progression (41 percent vs 43 percent), progression-free survival (44 percent vs 45 percent), or overall survival (89 percent vs 85 percent). In the proposed biosimilar and trastuzumab groups, 99 percent and 95 percent of patients had at least 1 adverse event.

“Trastuzumab is not widely available around the world,” the authors write. “A biosimilar treatment option may increase global access to biologic cancer therapies, provided, among other issues, that the price of the biosimilar is sufficiently inexpensive to enable women in non-high-income countries to access this therapy.”

The researchers note that further study is needed to assess safety as well as long-term clinical outcome.

Additional Comments
With trastuzumab coming towards end of its patent life we should expect arrival of new biosimilar drugs that will mimic transtuzumab in action and potency. It is a good news to see some of them in action such as above. There is a new hope with arrival of these biosimilar drugs that it will be widely available around the world at reasonable price level.

Citations
1.“Effect of a Proposed Trastuzumab Biosimilar Compared With Trastuzumab on Overall Response Rate in Patients With ERBB2 (HER2)–Positive Metastatic Breast Cancer: A Randomized Clinical Trial”. Hope S. Rugo, Abhijit Barve, Cornelius F. Waller, Miguel Hernandez-Bronchud, Jay Herson, Jinyu Yuan, Rajiv Sharma, Mark Baczkowski, Mudgal Kothekar, Subramanian Loganathan, Alexey Manikhas, Igor Bondarenko, Guzel Mukhametshina, Gia Nemsadze, Joseph D. Parra, Maria Luisa T. Abesamis-Tiambeng, Kakhaber Baramidze, Charuwan Akewanlop, Ihor Vynnychenko, Virote Sriuranpong, Gopichand Mamillapalli, Sirshendu Ray, Eduardo P. Yanez Ruiz, Eduardo Pennella. JAMA vol: 56 (4) pp: 226-243.
DOI: 10.1001/jama.2016.18305
Research funding: Mylan Inc., Biocon Research Limited.
Adapted from press release by The JAMA Network.

Over expression of protein BRD4 associated with breast cancer metastasis

Researchers have identified a new pathway and with it a protein, BRD4, necessary for breast cancer cells to spread. The findings, which appear in the journal Cancer Research, may provide a new target to suppress breast cancer metastasis.

Triple-negative breast cancer is considered the worst subgroup of breast cancer. It is highly aggressive and responds poorly to the current therapeutic tools resulting in a dismal prognosis for patients. Furthermore, the lack of identified targets has limited the development of new drug strategies.

Researchers from Boston University School of Medicine (BUSM) used breast cancer cell lines that present the clinical characteristics of an aggressive breast cancer subtype (clinically described as a triple-negative breast cancer). They then used an experimental design to model cancer cell metastasis. By suppressing the expression of the protein BRD4 in these cell lines, they observed that their dissemination capabilities were blocked, indicating that BRD4 drives breast cancer dissemination. In addition, they conducted a screening analysis of human breast tumors and found that tumors with a high expression of BRD4 were more likely to metastasize.

“The current treatment options for a triple-negative cancer are unacceptably limited. It is crucial to identify new therapeutic targets to tackle challenging cancer types, including triple negative breast cancer. BDR4 targeting represents an innovative strategy to ablate breast cancer metastasis,” explained lead investigator Guillaume Andrieu, PhD, a post-doctoral research associate at Boston University School of Medicine.

Although obesity per se is not thought of as a carcinogen, the abnormal, inflamed microenvironments found in obesity are critical for progression, invasion and metastasis of triple negative breast cancer. “Bromodomain and ExtraTerminal domain (BET) proteins, which include BRD2, BRD3 and BRD4, are known to regulate production of inflammatory mediators. Our study proposes that BRD4 couples inflammation to breast cancer dissemination. Thus, small molecules that block BET proteins possess anti-inflammatory properties that can be useful for therapy,” he added.

Although these findings primarily focus on breast cancer and metastasis, the researchers plan to expand their results to the treatment of prostate cancer, which they believe has similar pathways involved in its metastasis.

Citation: Andrieu, Guillaume, Anna H. Tran, Katherine J. Strissel, and Gerald V. Denis. “BRD4 regulates breast cancer dissemination through Jagged1/Notch1 signaling.” Cancer Research (2016): canres-0559.
DOI: http://dx.doi.org/10.1158/0008-5472.CAN-16-0559
Research funding: NIH/National Cancer Institute
Adapted from press release by Boston Univsersity School of Medicine

Vitamin D and Breast Cancer survival

Women with higher vitamin D levels in their blood following a breast cancer diagnosis had significantly better long-term outcomes, according to new research from Kaiser Permanente and Roswell Park Cancer Institute. The study was published in JAMA Oncology.

We found that women with the highest levels of vitamin D levels had about a 30 percent better likelihood of survival than women with the lowest levels of vitamin D,” said Lawrence H. Kushi, ScD, research scientist with the Kaiser Permanente Northern California Division of Research and principal investigator of Kaiser Permanente’s Pathways study of breast cancer survivorship. The current study included 1,666 Pathways study members who provided samples between 2006 and 2013.

With funding from the National Cancer Institute, the Pathways study began enrolling Kaiser Permanente members in Northern California who had a diagnosis of invasive breast cancer in 2006. Participants provided blood samples within two months of diagnosis and answered questions about diet, lifestyle and other risk factors, with follow-ups at six months and at two, four, six and eight years.

“With the extremely rich data sources from a large sample size, we were able to prospectively analyze three major breast cancer outcomes — recurrence, second primary cancer and death,” said Song Yao, PhD, associate professor of oncology at Roswell Park Cancer Institute and the study’s lead author. The institute, located in Buffalo, NY, is a partner in the Pathways study.

“We were also able to adjust for multiple possible contributing factors that could influence vitamin D levels,” Yao said, “such as age, obesity, race and ethnicity, socioeconomic status, and several tumor characteristics that are known to influence breast cancer outcomes — to ensure that the effects we observed were independent of these factors.”

In addition to lower overall mortality among all breast cancer survivors studied, the researchers found even stronger associations among premenopausal women in the highest third of vitamin D levels for breast-cancer-specific (63 percent better), recurrence-free (48 percent better) and invasive-disease-free survival (42 percent better), during a median follow up of seven years.

Although the study did not examine the effects of vitamin D intake from foods versus supplements, Kushi noted that it supports the recommended daily levels of vitamin D (600 IU for those 1 to 70 years old and pregnant or breastfeeding women, and 800 IU for those over 71 years old).

“The more we know about vitamin D, the more we understand that it may play a key role in cancer prevention and prognosis,” Kushi said. “This study adds to the evidence that vitamin D is an important nutrient.”

Citation: Association of Serum Level of Vitamin D at Diagnosis With Breast Cancer Survival. A Case-Cohort Analysis in the Pathways Study. Song Yao, Marilyn L. Kwan, Isaac J. Ergas, Janise M. Roh, Ting-Yuan David Cheng, Chi-Chen Hong, Susan E. McCann, Li Tang, Warren Davis, Song Liu, Charles P. Quesenberry Jr, Marion M. Lee, Christine B. Ambrosone, Lawrence H. Kushi. JAMA Oncology 2016 vol: 7 (9) pp: 684-700
DOI: http://dx.doi.org/10.1001/jamaoncol.2016.4188
Research funding: National Cancer Institute
Adapted from press release by Kaiser Permanente.

Synthetic binding protein called “NS1 Monobody” found to inhibit common cancer causing (RAS) mutation

Monobody NS1 binds to H-RAS or K-RAS protein and blocks
RAS function by disrupting the protein’s ability to form active
 molecular pairs. Credit: John P. O’Bryan, et al. 

Researchers at the University of Illinois at Chicago have identified a new way to block the action of genetic mutations found in nearly 30 percent of all cancers. Mutations in genes for the RAS family of proteins are present in nearly 90 percent of pancreatic cancers and are also highly prevalent in colon cancer, lung cancer and melanoma, the most dangerous kind of skin cancer. The group of proteins include three members, K-RAS, H-RAS and N-RAS.

The prevalence of RAS mutations in human cancers and the dependence of tumors on RAS for survival has made a RAS a prime target for cancer research and drug discovery. Scientists and drug developers have long studied RAS oncogenes hoping to find a new treatment for cancer, but they have not yet been able to identify drugs that safely inhibit the oncogene’s activity.

John O’Bryan, associate professor of pharmacology in the UIC College of Medicine, led a team of researchers that took a different approach to studying RAS, and discovered that a synthetic binding protein they call “NS1 monobody,” which they created in the lab, can block the activity of the RAS proteins.

“We did not look for a drug or specifically for an inhibitor,” said O’Bryan, who is also a member of the University of Illinois Cancer Center and holds an appointment at the Jesse Brown VA Medical Center in Chicago. “We used monobody technology, a type of protein-engineering technology, to identify regions of RAS that are critical for its function.” Unlike conventional antibodies, monobodies are not dependent on their environment and can be readily used as genetically encoded inhibitors, O’Bryan said. “The beauty of the technology is that when a monobody binds a protein, it usually works as an inhibitor of that protein,” he said.

Monobodies were developed by Shohei Koide, a co-author on the study who is professor of biochemistry and molecular pharmacology at New York University. They have been used to target a diverse array of proteins that include enzymes and receptors.

The researchers found that the NS1 monobody binds to an area of the RAS protein molecule that was not previously known to be important for its oncogenic activity. NS1 strongly inhibits oncogenic K-RAS and H-RAS function by blocking the ability of the protein to interact with an identical one to form a molecular pair. NS1 does not affect N-RAS.

O’Bryan says the findings, published in the journal Nature Chemical Biology, provide important insight into long-standing questions about how RAS proteins function in cells. These insights may help guide the development of new therapeutic approaches to treating cancer by interfering with mutant RAS function in cancer cells.

“Development of effective RAS inhibitors represents a ‘holy grail’ in cancer biology,” O’Bryan said. “We now have a powerful tool we can use to further probe RAS function. While future studies and trials are needed before these findings can be leveraged outside the lab, this study provides new insight into how we can potentially inhibit RAS to slow tumor growth.”

Citation: Russell Spencer-Smith, Akiko Koide, Yong Zhou, Raphael R Eguchi, Fern Sha, Priyanka Gajwani, Dianicha Santana, Ankit Gupta, Miranda Jacobs, Erika Herrero-Garcia, Jacqueline Cobbert, Hugo Lavoie, Matthew Smith, Thanashan Rajakulendran, Evan Dowdell, Mustafa Nazir Okur, Irina Dementieva, Frank Sicheri, Marc Therrien, John F Hancock, Mitsuhiko Ikura, Shohei Koide & John P O’Bryan. “Inhibition of RAS function through targeting an allosteric regulatory site” Nature Chemical Biology 2016
DOI: http://dx.doi.org/10.1038/nchembio.2231
Research funding: Chicago Biomedical Consortium, Searle Funds at the Chicago Community Trust, Department of Veterans Affairs, National Institutes of Health
Adapted from press release by University of Illinois at Chicago

Synthetic binding protein called "NS1 Monobody" found to inhibit common cancer causing (RAS) mutation

Monobody NS1 binds to H-RAS or K-RAS protein and blocks
RAS function by disrupting the protein’s ability to form active
 molecular pairs. Credit: John P. O’Bryan, et al. 

Researchers at the University of Illinois at Chicago have identified a new way to block the action of genetic mutations found in nearly 30 percent of all cancers. Mutations in genes for the RAS family of proteins are present in nearly 90 percent of pancreatic cancers and are also highly prevalent in colon cancer, lung cancer and melanoma, the most dangerous kind of skin cancer. The group of proteins include three members, K-RAS, H-RAS and N-RAS.

The prevalence of RAS mutations in human cancers and the dependence of tumors on RAS for survival has made a RAS a prime target for cancer research and drug discovery. Scientists and drug developers have long studied RAS oncogenes hoping to find a new treatment for cancer, but they have not yet been able to identify drugs that safely inhibit the oncogene’s activity.

John O’Bryan, associate professor of pharmacology in the UIC College of Medicine, led a team of researchers that took a different approach to studying RAS, and discovered that a synthetic binding protein they call “NS1 monobody,” which they created in the lab, can block the activity of the RAS proteins.

“We did not look for a drug or specifically for an inhibitor,” said O’Bryan, who is also a member of the University of Illinois Cancer Center and holds an appointment at the Jesse Brown VA Medical Center in Chicago. “We used monobody technology, a type of protein-engineering technology, to identify regions of RAS that are critical for its function.” Unlike conventional antibodies, monobodies are not dependent on their environment and can be readily used as genetically encoded inhibitors, O’Bryan said. “The beauty of the technology is that when a monobody binds a protein, it usually works as an inhibitor of that protein,” he said.

Monobodies were developed by Shohei Koide, a co-author on the study who is professor of biochemistry and molecular pharmacology at New York University. They have been used to target a diverse array of proteins that include enzymes and receptors.

The researchers found that the NS1 monobody binds to an area of the RAS protein molecule that was not previously known to be important for its oncogenic activity. NS1 strongly inhibits oncogenic K-RAS and H-RAS function by blocking the ability of the protein to interact with an identical one to form a molecular pair. NS1 does not affect N-RAS.

O’Bryan says the findings, published in the journal Nature Chemical Biology, provide important insight into long-standing questions about how RAS proteins function in cells. These insights may help guide the development of new therapeutic approaches to treating cancer by interfering with mutant RAS function in cancer cells.

“Development of effective RAS inhibitors represents a ‘holy grail’ in cancer biology,” O’Bryan said. “We now have a powerful tool we can use to further probe RAS function. While future studies and trials are needed before these findings can be leveraged outside the lab, this study provides new insight into how we can potentially inhibit RAS to slow tumor growth.”

Citation: Russell Spencer-Smith, Akiko Koide, Yong Zhou, Raphael R Eguchi, Fern Sha, Priyanka Gajwani, Dianicha Santana, Ankit Gupta, Miranda Jacobs, Erika Herrero-Garcia, Jacqueline Cobbert, Hugo Lavoie, Matthew Smith, Thanashan Rajakulendran, Evan Dowdell, Mustafa Nazir Okur, Irina Dementieva, Frank Sicheri, Marc Therrien, John F Hancock, Mitsuhiko Ikura, Shohei Koide & John P O’Bryan. “Inhibition of RAS function through targeting an allosteric regulatory site” Nature Chemical Biology 2016
DOI: http://dx.doi.org/10.1038/nchembio.2231
Research funding: Chicago Biomedical Consortium, Searle Funds at the Chicago Community Trust, Department of Veterans Affairs, National Institutes of Health
Adapted from press release by University of Illinois at Chicago

Role of Prolactin Inducible Protein in Breast Cancer

Researchers describe the first evidence linking prolactin inducible protein (PIP) to the immune system’s ability to recognize and destroy foreign cells, such as tumor cells. New research in prolactin inducible protein deficient mice that demonstrates the role of prolactin inducible protein  in cell-mediated immunity and suggests that this immune regulatory function may be protective against breast cancer is presented in DNA and Cell Biology, a peer-reviewed journal.

Coauthors Olivia Ihedioha, Robert Shiu, Jude Uzonna, and Yvonne Myal, University of Manitoba, Winnipeg, Canada, describe the potential clinical implications of these findings, in which prolactin inducible protein could represent an effective new target for the development of novel immunotherapeutic agents.

“Breast cancers are among the most common tumors. prolactin inducible protein was observed to be selectively expressed by these cells,” says Carol Shoshkes Reiss, PhD, Editor-in-Chief of DNA and Cell Biology and Professor, Departments of Biology and Neural Science, and Global Public Health at New York University, NY. “The work from the Myal lab in this paper is exciting because of the immunoregulatory activity they describe. I hope it will lead to novel therapeutic approaches to this devastating disease.”

Citation: Prolactin-Inducible Protein: From Breast Cancer Biomarker to Immune Modulator—Novel Insights from Knockout Mice. Authors: Olivia C. Ihedioha, Robert P.C. Shiu,  Jude E. Uzonna, and Yvonne Myal.
DOI: http://dx.doi.org/10.1089/dna.2016.3472
Journal: DNA and Cell Biology
Adapted from press release by Mary Ann Liebert, Inc., publishers