Joyce Taylor-Papadimitriou FMedSci | |
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Born | 1932 (age 91–92) Burnley, Lancashire, England |
Education | University of Cambridge, University of Toronto (PhD) |
Known for | Interferon type 1 requires the synthesis of effector proteins |
Scientific career | |
Fields | Molecular biology and genetics |
Doctoral advisor | Louis Siminovitch |
Joyce Taylor-Papadimitriou FMedSci (born 1932) is a British molecular biologist and geneticist. She is Senior Fellow and Visiting Professor at King's College London specialising in the area of cellular, genetic and proteomic studies on patient breast tumour samples, and works within the Breast Cancer Biology Group. [1] She was the first to identify that the action of interferon type 1 requires the synthesis of effector proteins.
Joyce Taylor-Papadimitriou was born in 1932 in Burnley, Lancashire. [2] [3] She read biochemistry at the University of Cambridge, graduating in 1954. Further study led to a PhD at the University of Toronto, supervised by Louis Siminovitch.
As an early career researcher, Taylor-Papadimitriou worked at the National Institute for Medical Research (NIMR), London with Alick Isaacs. Here she found that the action of type 1 interferons requires effector protein synthesis. She worked in Greece for eight years following NIMR, returning to England after to set up her own lab at the Imperial Cancer Research Fund (ICRF).
Her work has included identifying and characterising the MUC1 membrane mucin, a breast and ovarian tumour associated antigen which is over expressed and aberrantly glycosylated in these tissues. Immunogens based on the MUC1 mucin are in various clinical trials.
Her most highly cited paper, Sandra J. GendlerS, Carole A. Lancaster, Joyce Taylor-Papadimitriou, Trevor Duhig, Nigel Peat, Joy Burchell, Lucy Pemherton, El-Nasir Lalani, and David Wilson " Molecular Cloning and Expression of Human Tumor-associated Polymorphic Epithelial Mucin*" Journal of Biological Chemistry 265:15286-93 (1990) has been cited 1039 times. The most cited paper of which she is first author, Joyce Taylor-Papadimitriou1, J. A. Peterson2, J. Arklie1, Joy Burchell1, R. L. Ceriani2 and W. F. Bodmer1 "Monoclonal antibodies to epithelium‐specific components of the human milk fat globule membrane: Production and reaction with cells in culture" International Journal of Cancer Volume 28, Issue 1, pages 17–21, 15 July 1981 has been cited 698 times. [4]
Taylor-Papadimitriou was elected a Fellow of the Academy of Medical Sciences in 2001. [5]
Mucin-16(MUC-16) also known as Ovarian cancer-related tumor marker CA125 is a protein that in humans is encoded by the MUC16 gene. MUC-16 is a member of the mucin family glycoproteins. MUC-16 has found application as a tumor marker or biomarker that may be elevated in the blood of some patients with specific types of cancers, most notably ovarian cancer, or other conditions that are benign.
Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most animals. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. They often take an inhibitory role. Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms and bone formation in vertebrates. They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer.
The National Institute for Medical Research (NIMR), was a medical research institute based in Mill Hill, on the outskirts of north London, England. It was funded by the Medical Research Council (MRC);
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Karen Heather Vousden is a British medical researcher. She is known for her work on the tumour suppressor protein, p53, and in particular her discovery of the important regulatory role of Mdm2, an attractive target for anti-cancer agents. From 2003 to 2016, she was the director of the Cancer Research UK Beatson Institute in Glasgow, UK, moving back to London in 2016 to take up the role of Chief Scientist at CRUK and Group Leader at the Francis Crick Institute.
Mucin short variant S1, also called polymorphic epithelial mucin (PEM) or epithelial membrane antigen (EMA), is a mucin encoded by the MUC1 gene in humans. Mucin short variant S1 is a glycoprotein with extensive O-linked glycosylation of its extracellular domain. Mucins line the apical surface of epithelial cells in the lungs, stomach, intestines, eyes and several other organs. Mucins protect the body from infection by pathogen binding to oligosaccharides in the extracellular domain, preventing the pathogen from reaching the cell surface. Overexpression of MUC1 is often associated with colon, breast, ovarian, lung and pancreatic cancers. Joyce Taylor-Papadimitriou identified and characterised the antigen during her work with breast and ovarian tumors.
Mucin-4 (MUC-4) is a mucin protein that in humans is encoded by the MUC4 gene. Like other mucins, MUC-4 is a high-molecular weight glycoprotein.
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Mucin-1(MUC-1) is a heterodimer transmembrane protein of the mucin family encoded in humans by the MUC1 gene. It is cleaved into two chains: mucin-1 subunit alpha and mucin-1 subunit beta. These subunits differ in size due to proteolytic cleavage of the translated precursor protein in the endoplasmic reticulum. The larger subunit of MUC-1 is characterized by numerous O-glycosylated bonds and a terminal sialic acid, creating a net negative charge on MUC-1. The smaller subunit contains a juxtamembrane region of the extracellular area, a transmembrane domain, and the cytoplasmic tail. The extracellular domain of MUC-1 is composed of 20 identical amino acid tandem repeats (TR). Each tandem repeat contains two serine and three threonine amino acid residues, providing five sites for potential O-glycosylation. MUC-1 protein is estimated to weigh 120 to 225 kDA.
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