Abstract
Innovations in approaches for early detection and individual risk assessment of different cancers, including breast cancer (BC), are needed to reduce cancer morbidity and associated mortality. The assessment of potential cancer biomarkers in accessible bodily fluids provides a novel approach to identify the risk and/or onset of cancer. Biomarkers are biomolecules, such as proteins, that are indicative of an abnormality or a disease. Human milk is vastly underutilized biospecimen that offers the opportunity to investigate potential protein BC-biomarkers in young, reproductively active women. As a first step, we have examined the entire protein pattern in human milk samples from breastfeeding mothers with cancer, who were diagnosed either before or after milk donation, and from women without cancer, using mass spectrometry (MS)-based proteomics.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- 1D:
-
One-dimensional
- 2D:
-
Two-dimensional
- BC:
-
Breast cancer
- DDA:
-
Data dependent acquisition
- DDT:
-
Dithiothreitol
- IAA:
-
Iodoacetamide
- MS:
-
Mass spectrometry
- MS/MS:
-
Tandem mass spectrometry
- nanoLC-MS/MS:
-
Nano-liquid chromatography tandem mass spectrometry
- SDS-PAGE:
-
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
References
Torre, L. A., Islami, F., Siegel, R. L., Ward, E. M., & Jemal, A. (2017). Global Cancer in women: Burden and trends. Cancer Epidemiology, Biomarkers & Prevention, 26(4), 444–457.
National Cancer Institute. (2018). SEER cancer statistics factsheets: Breast cancer. Bethesda, MD: National Cancer Institute.
Nichols, H. B., Schoemaker, M. J., Cai, J., Xu, J., Wright, L. B., Brook, M. N., et al. (2018). Breast cancer risk after recent childbirth: A pooled analysis of 15 prospective studies. Annals of Internal Medicine.
Anderson, B. O., Petrek, J. A., Byrd, D. R., Senie, R. T., & Borgen, P. I. (1996). Pregnancy influences breast cancer stage at diagnosis in women 30 years of age and younger. Annals of Surgical Oncology, 3(2), 204–211.
Borges, V. F., & Schedin, P. J. (2012). Pregnancy-associated breast cancer: An entity needing refinement of the definition. Cancer, 118(13), 3226–3228.
Murphy, C. G., Mallam, D., Stein, S., Patil, S., Howard, J., Sklarin, N., et al. (2012). Current or recent pregnancy is associated with adverse pathologic features but not impaired survival in early breast cancer. Cancer, 118(13), 3254–3259.
Langer, A., Mohallem, M., Stevens, D., Rouzier, R., Lerebours, F., & Cherel, P. (2014). A single-institution study of 117 pregnancy-associated breast cancers (PABC): Presentation, imaging, clinicopathological data and outcome. Diagnostic and Interventional Imaging, 95(4), 435–441.
American Cancer Society. (2013). Breast cancer facts and figures 2013–2014. New York City, NY: American Cancer Society.
U.S. Preventive Services Task Force. (2010). Screening for breast cancer, topic page. Washington, DC: U.S. Preventive Services Task Force.
Beyer, I., Mutschler, N., Blum, K. S., & Mohrmann, S. (2015). Breast lesions during pregnancy - a diagnostic challenge: Case report. Breast Care (Basel), 10(3), 207–210.
Joshi, S., Dialani, V., Marotti, J., Mehta, T. S., & Slanetz, P. J. (2013). Breast disease in the pregnant and lactating patient: Radiological-pathological correlation. Insights Imaging, 4(5), 527–538.
Yang, H. P., Schneider, S. S., Chisholm, C. M., Browne, E. P., Mahmood, S., Gierach, G. L., et al. (2015). Association of TGF-β2 levels in breast milk with severity of breast biopsy diagnosis. Cancer Causes & Control, 26(3), 345–354.
Arcaro, K. F., Browne, E. P., Qin, W., Zhang, K., Anderton, D. L., & Sauter, E. R. (2012). Differential expression of cancer-related proteins in paired breast milk samples from women with breast cancer. Journal of Human Lactation, 28(4), 543–546.
Wong, C. M., Anderton, D. L., Smith-Schneider, S., Wing, M. A., Greven, M. C., & Arcaro, K. F. (2010). Quantitative analysis of promoter methylation in exfoliated epithelial cells isolated from breast milk of healthy women. Epigenetics, 5(7), 645–655.
Qin, W., Zhang, K., Kliethermes, B., Ruhlen, R. L., Browne, E. P., Arcaro, K. F., et al. (2012). Differential expression of cancer associated proteins in breast milk based on age at first full term pregnancy. BMC Cancer, 12(1), 100.
Browne, E. P., Punska, E. C., Lenington, S., Otis, C. N., Anderton, D. L., & Arcaro, K. F. (2011). Increased promoter methylation in exfoliated breast epithelial cells in women with a previous breast biopsy. Epigenetics, 6(12), 1425–1435.
Murphy, J., Sherman, M. E., Browne, E. P., Caballero, A. I., Punska, E. C., Pfeiffer, R. M., et al. (2016). Potential of breastmilk analysis to inform early events in breast carcinogenesis: Rationale and considerations. Breast Cancer Research and Treatment, 157(1), 13–22.
Faupel-Badger, J. M., Arcaro, K. F., Balkam, J. J., Eliassen, A. H., Hassiotou, F., Lebrilla, C. B., et al. (2012). Postpartum remodeling, lactation, and breast cancer risk: Summary of a National Cancer Institute–sponsored workshop. Journal of the National Cancer Institute, 105(3), 166–174.
Schneider, S. S., Aslebagh, R., Wetie, A. G., Sturgeon, S. R., Darie, C. C., & Arcaro, K. F. (2014). Using breast milk to assess breast cancer risk: The role of mass spectrometry-based proteomics. Advances in Experimental Medicine and Biology, 806, 399–408.
Thompson, P., Kadlubar, F., Vena, S., Hill, H., McClure, G., McDaniel, L., et al. (1998). Exfoliated ductal epithelial cells in human breast milk: A source of target tissue DNA for molecular epidemiologic studies of breast cancer. Cancer Epidemiology and Prevention Biomarkers, 7(1), 37–42.
Gu, Y.-Q., Gong, G., Xu, Z.-L., Wang, L.-Y., Fang, M.-L., Zhou, H., et al. (2014). miRNA profiling reveals a potential role of milk stasis in breast carcinogenesis. International Journal of Molecular Medicine, 33(5), 1243–1249.
Aslebagh, R., Channaveerappa, D., Arcaro, K. F., & Darie, C. C. (2018). Proteomics analysis of human breast milk to assess breast cancer risk. Electrophoresis, 39(4), 653–665.
Aslebagh, R., Channaveerappa, D., Arcaro, K. F., & Darie, C. C. (2018). Comparative two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) of human milk to identify dysregulated proteins in breast cancer. Electrophoresis, 39(14), 1723–1734.
Monte, L., & Ellis, R. (2014). Fertility of Women in the United States: 2012. Suitland, MD: U.S. Census Bureau.
Linder, N., Lundin, J., Isola, J., Lundin, M., Raivio, K. O., & Joensuu, H. (2005). Down-regulated xanthine oxidoreductase is a feature of aggressive breast cancer. Clinical Cancer Research, 11(12), 4372–4381.
Fini, M. A., Monks, J., Farabaugh, S. M., & Wright, R. M. (2011). Contribution of xanthine oxidoreductase to mammary epithelial and breast cancer cell differentiation in part modulates inhibitor of differentiation-1. Molecular Cancer Research, 9, 1242.
Schramm, G., Surmann, E.-M., Wiesberg, S., Oswald, M., Reinelt, G., Eils, R., et al. (2010). Analyzing the regulation of metabolic pathways in human breast cancer. BMC Medical Genomics, 3(1), 39.
Bártková, J., Burchell, J., Bártek, J., Vojtěšek, B., Taylor-Papadimitriou, J., Rejthar, A., et al. (1987). Lack of β-casein production by human breast tumours revealed by monoclonal antibodies. European Journal of Cancer and Clinical Oncology, 23(10), 1557–1563.
Flavin, R., Peluso, S., Nguyen, P. L., & Loda, M. (2010). Fatty acid synthase as a potential therapeutic target in cancer. Future Oncology, 6(4), 551–562.
Wang, Y. Y., Kuhajda, F. P., Li, J., Finch, T. T., Cheng, P., Koh, C., et al. (2004). Fatty acid synthase as a tumor marker: Its extracellular expression in human breast cancer. Journal of Experimental Therapeutics & Oncology, 4(2).
Wang, Y. Y., Kuhajda, F. P., Li, J. N., Pizer, E. S., Han, W. F., Sokoll, L. J., et al. (2001). Fatty acid synthase (FAS) expression in human breast cancer cell culture supernatants and in breast cancer patients. Cancer Letters, 167(1), 99–104.
Yamamura, J., Miyoshi, Y., Tamaki, Y., Taguchi, T., Iwao, K., Monden, M., et al. (2004). mRNA expression level of estrogen-inducible gene, α1-antichymotrypsin, is a predictor of early tumor recurrence in patients with invasive breast cancers. Cancer Science, 95(11), 887–892.
Higashiyama, M., Doi, O., Yokouchi, H., Kodama, K., Nakamori, S., & Tateishi, R. (1995). Alpha-1-antichymotrypsin expression in lung adenocarcinoma and its possible association with tumor progression. Cancer, 76(8), 1368–1376.
Cho, N. H., Park, C., & Park, D. S. (1997). Expression of alpha-1-antichymotrypsin in prostate carcinoma. Journal of Korean Medical Science, 12(3), 228–233.
Channaveerappa, D., Lux, J. C., Wormwood, K. L., Heintz, T. A., McLerie, M., Treat, J. A., et al. (2017). Atrial electrophysiological and molecular remodelling induced by obstructive sleep apnoea. Journal of Cellular and Molecular Medicine, 21(9), 2223–2235.
Cole, L. A. (2009). New discoveries on the biology and detection of human chorionic gonadotropin. Reproductive Biology and Endocrinology, 7(1), 8.
Gregory, J. J., & Finlay, J. L. (1999). α-Fetoprotein and β-human chorionic gonadotropin. Drugs, 57(4), 463–467.
Hall, R. E., Aspinall, J., Horsfall, D., Birrell, S., Bentel, J., Sutherland, R., et al. (1996). Expression of the androgen receptor and an androgen-responsive protein, apolipoprotein D, in human breast cancer. British Journal of Cancer, 74(8), 1175.
Diez-Itza, I., Vizoso, F., Merino, A. M., Sánchez, L. M., Tolivia, J., Fernandez, J., et al. (1994). Expression and prognostic significance of apolipoprotein D in breast cancer. The American Journal of Pathology, 144(2), 310.
Sturge, J., Todd, S. K., Kogianni, G., McCarthy, A., & Isacke, C. M. (2007). Mannose receptor regulation of macrophage cell migration. Journal of Leukocyte Biology, 82(3), 585–593.
Brown, N. J., Higham, S. E., Perunovic, B., Arafa, M., Balasubramanian, S., & Rehman, I. (2013). Lactate dehydrogenase-B is silenced by promoter methylation in a high frequency of human breast cancers. PLoS One, 8(2), e57697.
Zhao, L., Wei, Y., Song, A., & Li, Y. (2016). Association study between genome-wide significant variants of vitamin B12 metabolism and gastric cancer in a han Chinese population. IUBMB Life, 68(4), 303–310.
Castillo-Tong, D. C., Pils, D., Heinze, G., Braicu, I., Sehouli, J., Reinthaller, A., et al. (2014). Association of myeloperoxidase with ovarian cancer. Tumor Biology, 35(1), 141–148.
Spencer, V. A. (2011). Actin—Towards a deeper understanding of the relationship between tissue context, cellular function and tumorigenesis. Cancers, 3(4), 4269–4280.
Stetler-Stevenson, W. G. (1990). Type IV collagenases in tumor invasion and metastasis. Cancer and Metastasis Reviews, 9(4), 289–303.
Kao, R. T., & Stern, R. (1986). Collagenases in human breast carcinoma cell lines. Cancer Research, 46(3), 1349–1354.
Liu, X.-H., & Rose, D. P. (1994). Stimulation of type IV collagenase expression by linoleic acid in a metastatic human breast cancer cell line. Cancer Letters, 76(1), 71–77.
Benbow, U., Schoenermark, M. P., Orndorff, K. A., Givan, A. L., & Brinckerhoff, C. E. (1999). Human breast cancer cells activate procollagenase-1 and invade type I collagen: Invasion is inhibited by all-trans retinoic acid. Clinical & Experimental Metastasis, 17(3), 231–238.
Simpson-Haidaris, P., & Rybarczyk, B. (2001). Tumors and fibrinogen. Annals of the New York Academy of Sciences, 936(1), 406–425.
Wang, L., Bi, J., Yao, C., Xu, X., Li, X., Wang, S., et al. (2010). Annexin A1 expression and its prognostic significance in human breast cancer. Neoplasma, 57(3), 253–259.
Kloth, L., Belge, G., Burchardt, K., Loeschke, S., Wosniok, W., Fu, X., et al. (2011). Decrease in thyroid adenoma associated (THADA) expression is a marker of dedifferentiation of thyroid tissue. BMC Clinical Pathology, 11(1), 13.
Ostler, D. A., Prieto, V. G., Reed, J. A., Deavers, M. T., Lazar, A. J., & Ivan, D. (2010). Adipophilin expression in sebaceous tumors and other cutaneous lesions with clear cell histology: An immunohistochemical study of 117 cases. Modern Pathology, 23(4), 567.
Straub, B. K., Herpel, E., Singer, S., Zimbelmann, R., Breuhahn, K., Macher-Goeppinger, S., et al. (2010). Lipid droplet-associated PAT-proteins show frequent and differential expression in neoplastic steatogenesis. Modern Pathology, 23(3), 480.
Divyya, S., Naushad, S. M., Addlagatta, A., Murthy, P., Reddy, C. R., Digumarti, R. R., et al. (2013). Association of glutamate carboxypeptidase II (GCPII) haplotypes with breast and prostate cancer risk. Gene, 516(1), 76–81.
Wang, X., Yin, L., Rao, P., Stein, R., Harsch, K. M., Lee, Z., et al. (2007). Targeted treatment of prostate cancer. Journal of Cellular Biochemistry, 102(3), 571–579.
Xiao, S., Liu, L., Lu, X., Long, J., Zhou, X., & Fang, M. (2015). The prognostic significance of bromodomain PHD-finger transcription factor in colorectal carcinoma and association with vimentin and E-cadherin. Journal of Cancer Research and Clinical Oncology, 141(8), 1465–1474.
Sun, F., Ding, W., He, J.-H., Wang, X.-J., Ma, Z.-B., & Li, Y.-F. (2015). Stomatin-like protein 2 is overexpressed in epithelial ovarian cancer and predicts poor patient survival. BMC Cancer, 15(1), 1.
Kwon, Y.-J., Lee, S. J., Koh, J. S., Kim, S. H., Lee, H. W., Kang, M. C., et al. (2012). Genome-wide analysis of DNA methylation and the gene expression change in lung cancer. Journal of Thoracic Oncology, 7(1), 20–33.
Gibbs, G. M., Roelants, K., & O’bryan, M. K. (2008). The CAP superfamily: Cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins—Roles in reproduction, cancer, and immune defense. Endocrine Reviews, 29(7), 865–897.
Orend, G., & Chiquet-Ehrismann, R. (2006). Tenascin-C induced signaling in cancer. Cancer Letters, 244(2), 143–163.
Jahkola, T., Toivonen, T., Virtanen, I., von Smitten, K., Nordling, S., von Boguslawski, K., et al. (1998). Tenascin-C expression in invasion border of early breast cancer: A predictor of local and distant recurrence. British Journal of Cancer, 78(11), 1507.
Dandachi, N., Hauser-Kronberger, C., More, E., Wiesener, B., Hacker, G., Dietze, O., et al. (2001). Co-expression of tenascin-C and vimentin in human breast cancer cells indicates phenotypic transdifferentiation during tumour progression: Correlation with histopathological parameters, hormone receptors, and oncoproteins. The Journal of Pathology, 193(2), 181–189.
Adams, M., Jones, J. L., Walker, R. A., Pringle, J. H., & Bell, S. C. (2002). Changes in tenascin-C isoform expression in invasive and preinvasive breast disease. Cancer Research, 62(11), 3289–3297.
Scherberich, A., Tucker, R. P., Degen, M., Brown-Luedi, M., Andres, A.-C., & Chiquet-Ehrismann, R. (2005). Tenascin-W is found in malignant mammary tumors, promotes alpha8 integrin-dependent motility and requires p38MAPK activity for BMP-2 and TNF-alpha induced expression in vitro. Oncogene, 24(9), 1525–1532.
Kawakita, T., Sasaki, H., Hoshiba, T., Asamoto, A., & Williamson, E. (2012). Amylase-producing ovarian carcinoma: A case report and a retrospective study. Gynecologic Oncology Case Reports, 2(3), 112–114.
Tomita, N., Matsuura, N., Horii, A., Emi, M., Nishide, T., Ogawa, M., et al. (1988). Expression of α-amylase in human lung cancers. Cancer Research, 48(11), 3288–3291.
Lenler-Petersen, P., Grove, A., Brock, A., & Jelnes, R. (1994). Alpha-amylase in resectable lung cancer. European Respiratory Journal, 7(5), 941–945.
Hassan, M. I., Waheed, A., Yadav, S., Singh, T. P., & Ahmad, F. (2008). Zinc α2-glycoprotein: A multidisciplinary protein. Molecular Cancer Research, 6(6), 892–906.
Dubois, V., Delort, L., Mishellany, F., Jarde, T., Billard, H., Lequeux, C., et al. (2010). Zinc-α2-glycoprotein: A new biomarker of breast Cancer? Anticancer Research, 30(7), 2919–2925.
DÃez-Itza, I., Sánchez, L. M., Allende, M. T., Vizoso, F., Ruibal, A., & López-OtÃn, C. (1993). Zn-α2-glycoprotein levels in breast cancer cytosols and correlation with clinical, histological and biochemical parameters. European Journal of Cancer, 29(9), 1256–1260.
Freije, J. P., Fueyo, A., UrÃa, J., & López-Otin, C. (1991). Human Zn-α2-glycoprotein cDNA cloning and expression analysis in benign and malignant breast tissues. FEBS Letters, 290(1–2), 247–249.
Millan, A., & Huerta, S. (2009). Apoptosis-inducing factor and colon cancer. Journal of Surgical Research, 151(1), 163–170.
Lewis, E. M., Wilkinson, A. S., Jackson, J. S., Mehra, R., Varambally, S., Chinnaiyan, A. M., et al. (2012). The enzymatic activity of apoptosis-inducing factor supports energy metabolism benefiting the growth and invasiveness of advanced prostate cancer cells. Journal of Biological Chemistry, 287(52), 43862–43875.
Lee, J. W., Jeong, E. G., Soung, Y. H., Kim, S. Y., Nam, S. W., Kim, S. H., et al. (2006). Immunohistochemical analysis of apoptosis-inducing factor (AIF) expression in gastric carcinomas. Pathology-Research and Practice, 202(7), 497–501.
Aaboe, M., Offersen, B. V., Christensen, A., & Andreasen, P. A. (2003). Vitronectin in human breast carcinomas. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1638(1), 72–82.
Seve, P., Ray-Coquard, I., Trillet-Lenoir, V., Sawyer, M., Hanson, J., Broussolle, C., et al. (2006). Low serum albumin levels and liver metastasis are powerful prognostic markers for survival in patients with carcinomas of unknown primary site. Cancer, 107(11), 2698–2705.
Gopal, S. H., & Das, S. K. (2016). Role of Lactoferrin in the carcinogenesis of triple-negative breast Cancer. Journal of Cancer Clinical Trials, 1(3).
Benaïssa, M., Peyrat, J. P., Hornez, L., Mariller, C., Mazurier, J., & Pierce, A. (2005). Expression and prognostic value of lactoferrin mRNA isoforms in human breast cancer. International Journal of Cancer, 114(2), 299–306.
Penco, S., Caligo, M. A., Cipollini, G., Bevilacqua, G., & Garre, C. (1999). Lactoferrin expression in human breast cancer. Cancer Biochemistry Biophysics, 17(1–2), 163–178.
Naleskina, L., Lukianova, N. Y., Sobchenko, S., Storchai, D., & Chekhun, V. (2016). Lactoferrin expression in breast cancer in relation to biologic properties of tumors and clinical features of disease. Experimental Oncology, 38(3), 181–186.
Lehner, A., Magdolen, V., Schuster, T., Kotzsch, M., Kiechle, M., Meindl, A., et al. (2013). Downregulation of serine protease HTRA1 is associated with poor survival in breast cancer. PLoS One, 8(4), e60359.
Tufail, R., Jorda, M., Zhao, W., Reis, I., & Nawaz, Z. (2012). Loss of yes-associated protein (YAP) expression is associated with estrogen and progesterone receptors negativity in invasive breast carcinomas. Breast Cancer Research and Treatment, 131(3), 743–750.
Yuan, M., Tomlinson, V., Lara, R., Holliday, D., Chelala, C., Harada, T., et al. (2008). Yes-associated protein (YAP) functions as a tumor suppressor in breast. Cell Death and Differentiation, 15(11), 1752.
Lehn, S., Tobin, N. P., Sims, A. H., Stål, O., Jirström, K., Axelson, H., et al. (2014). Decreased expression of Yes-associated protein is associated with outcome in the luminal a breast cancer subgroup and with an impaired tamoxifen response. BMC Cancer, 14(1), 119.
Lei, B., Lionetti, V., Young, M. E., Chandler, M. P., d’Agostino, C., Kang, E., et al. (2004). Paradoxical downregulation of the glucose oxidation pathway despite enhanced flux in severe heart failure. Journal of Molecular and Cellular Cardiology, 36(4), 567–576.
Légaré, S., Cavallone, L., Mamo, A., Chabot, C., Sirois, I., Magliocco, A., et al. (2015). The estrogen receptor cofactor SPEN functions as a tumor suppressor and candidate biomarker of drug responsiveness in hormone-dependent breast cancers. Cancer Research, 75(20), 4351–4363.
Marnef, A., & Standart, N. (2010). Pat1 proteins: A life in translation, translation repression and mRNA decay. London: Portland Press Limited.
Oberley, T., & Oberley, L. (1997). Antioxidant enzyme levels in cancer. Histology and Histopathology, 12(2), 525–535.
Tsai, S.-M., Hou, M.-F., Wu, S.-H., Hu, B.-W., Yang, S.-F., Chen, W.-T., et al. (2011). Expression of manganese superoxide dismutase in patients with breast cancer. The Kaohsiung Journal of Medical Sciences, 27(5), 167–172.
Hitchler, M. J., Oberley, L. W., & Domann, F. E. (2008). Epigenetic silencing of SOD2 by histone modifications in human breast cancer cells. Free Radical Biology and Medicine, 45(11), 1573–1580.
Srour, N., Reymond, M. A., & Steinert, R. (2008). Lost in translation? A systematic database of gene expression in breast cancer. Pathobiology, 75(2), 112–118.
DeRoo, E. P., Wrobleski, S. K., Shea, E. M., Al-Khalil, R. K., Hawley, A. E., Henke, P. K., et al. (2015). The role of galectin-3 and galectin-3–binding protein in venous thrombosis. Blood, 125(11), 1813–1821.
Ilmer, M., Mazurek, N., Gilcrease, M. Z., Byrd, J. C., Woodward, W. A., Buchholz, T. A., et al. (2016). Low expression of galectin-3 is associated with poor survival in node-positive breast cancers and mesenchymal phenotype in breast cancer stem cells. Breast Cancer Research, 18(1), 97.
Escara-Wilke, J., Yeung, K., & Keller, E. T. (2012). Raf kinase inhibitor protein (RKIP) in cancer. Cancer and Metastasis Reviews, 31(3–4), 615–620.
Keller, E. T., Fu, Z., & Brennan, M. (2004). The role of Raf kinase inhibitor protein (RKIP) in health and disease. Biochemical Pharmacology, 68(6), 1049–1053.
Hagan, S., Al-Mulla, F., Mallon, E., Oien, K., Ferrier, R., Gusterson, B., et al. (2005). Reduction of Raf-1 kinase inhibitor protein expression correlates with breast cancer metastasis. Clinical Cancer Research, 11(20), 7392–7397.
Fu, Z., Kitagawa, Y., Shen, R., Shah, R., Mehra, R., Rhodes, D., et al. (2006). Metastasis suppressor gene Raf kinase inhibitor protein (RKIP) is a novel prognostic marker in prostate cancer. The Prostate, 66(3), 248–256.
Luce, L. N., Abbate, M., Cotignola, J., & Giliberto, F. (2017). Non-myogenic tumors display altered expression of dystrophin (DMD) and a high frequency of genetic alterations. Oncotarget, 8(1), 145.
Sgambato, A., Migaldi, M., Montanari, M., Camerini, A., Brancaccio, A., Rossi, G., et al. (2003). Dystroglycan expression is frequently reduced in human breast and colon cancers and is associated with tumor progression. The American Journal of Pathology, 162(3), 849–860.
Henry, M. D., Cohen, M. B., & Campbell, K. P. (2001). Reduced expression of dystroglycan in breast and prostate cancer. Human Pathology, 32(8), 791–795.
Vizoso, F., Plaza, E., Vázquez, J., Serra, C., Lamelas, M. L., González, L. O., et al. (2001). Lysozyme expression by breast carcinomas, correlation with clinicopathologic parameters, and prognostic significance. Annals of Surgical Oncology, 8(8), 667–674.
Bresnick, A. R., Weber, D. J., & Zimmer, D. B. (2015). S100 proteins in cancer. Nature Reviews Cancer, 15(2), 96–109.
Ghavami, S., Rashedi, I., Dattilo, B. M., Eshraghi, M., Chazin, W. J., Hashemi, M., et al. (2008). S100A8/A9 at low concentration promotes tumor cell growth via RAGE ligation and MAP kinase-dependent pathway. Journal of Leukocyte Biology, 83(6), 1484–1492.
Eatemadi, A., Aiyelabegan, H. T., Negahdari, B., Mazlomi, M. A., Daraee, H., Daraee, N., et al. (2017). Role of protease and protease inhibitors in cancer pathogenesis and treatment. Biomedicine & Pharmacotherapy, 86, 221–231.
Acknowledgements
We thank the members of our labs for the pleasant working environment.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Switzerland AG
About this chapter
Cite this chapter
Aslebagh, R., Channaveerappa, D., Pentecost, B.T., Arcaro, K.F., Darie, C.C. (2019). Combinatorial Electrophoresis and Mass Spectrometry-Based Proteomics in Breast Milk for Breast Cancer Biomarker Discovery. In: Woods, A., Darie, C. (eds) Advancements of Mass Spectrometry in Biomedical Research. Advances in Experimental Medicine and Biology, vol 1140. Springer, Cham. https://doi.org/10.1007/978-3-030-15950-4_26
Download citation
DOI: https://doi.org/10.1007/978-3-030-15950-4_26
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-030-15949-8
Online ISBN: 978-3-030-15950-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)