|Academic Profile |
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Assoc Prof Lin Chun Ling Valerie
Associate Professor, School of Biological Sciences
|Name: Valerie LIN Chun Ling
DOB: March 29, 1960
School: Biological Sciences
Division: Chemical Biology and Biotechnology
Present Appointment: Associate Professor
BVM (Veterinary Medicine) - Laiyang Agricultural University, 1982
Diploma (Biological Statistics) - Si Chuan Agricultural University, 1984
PhD (Endocrinology & Biochemistry) - University of Reading, 1990
Summary of Work Experience:
1982 - 1984 Lecturer, Department of Veterinary Medicine, Lai Yang Agricultural University
1986 - 1989 Graduate Teaching Assistant, Department of Biochemistry & Physiology, University of Reading, UK.
1989 - 1991 Postdoctoral Fellow, School of Pharmacy & Pharmacology, University of Bath
1992 - 1995 Research Scientist, Dept of Physiology, National University of Singapore
1995 - 2002 Senior Scientist/Principal Investigator, Dept of Clinical Research, Singapore General Hospital
2002 - 2008 Assistant Professor, School of Biological Sciences, NTU
2008 – Present Associate Professor, School of Biological Sciences, NTU
|Estrogen and progesterone are essential for the development of normal mammary gland. They are also implicated in the development of breast cancer. The function of progesterone seems to come second after estrogen. Biologically, the expression of progesterone receptor (PR) in the target tissue is primarily dependent on the presence of estrogens so progesterone is only active in cells treated with estrogen. Evolutionarily, estrogen was the first steroid receptor to evolve and this was followed by a progesterone receptor. Our primary area of interest is to understand how PR modulate the activity of ER and what the significance of this modulation is in the context of breast cancer treatment. We are also characterizing the function of some novel progesterone-regulated genes in order to understand the down-stream pathways of PR. Tetratricopeptide repeat domain 9 (TTC9) codes for a 25 kD protein that was recently identified by our laboratory. It was also found an estrogen-inducible gene in mice. Our current research is to study the interacting proteins for TTC9 and to generate TTC9 knockout mice for functional studies. Tripartite motif-containing 22 (TRIM22) belongs to TRIM family of proteins that have a conserved domain structure consisting of a RING domain, followed by one or two B-boxes domains and a Coiled-coil domain (CC). TRIM22 was initially discovered as an interferon-inducible gene which was later found to inhibit clonogenic growth in leukemic cells, but it is better known for its anti-viral properties. We have found that TRIM22 protein form distinct nuclear bodies and the TRIM22 bodies undergo dynamic changes during cell cycle progression. Furthermore, it is immensely under-expressed in breast cancer cells compared to normal mammary epithelial cells. The current research effort for TRIM22 is directed to understand how it is inactivated in breast cancer cells and the molecular mechanism of action of TRIM22 in normal mammary epithelial cells.|
- Comprehensive mapping of methylation landscape of progesterone receptor
- Dynamic changes of TRIM22 nuclear bodies during cell cycle progrssion
- Elucidate novel roles of unliganded progesterone receptor in breast cancer
- Functional significance of progesterone receptor methylation in breast cancer
- Functional study of a novel protein tetratricopeptide repeat domain 9
- Pathobiology and mechanism of progesterone receptor signaling defect in endometrium
- Regulation of mammary adipogenesis during mammary involution and its implication in tumorigenesis
- The role of estrogen in mammary involution and malignant transformation
- Sijie Tan, Natasa Bajalovic, Esther S.P. Wong, Valerie C.L. Lin. (2019). Ligand-activated progesterone receptor B activates transcription factor EB to promote autophagy in human breast cancer cells. Experimental Cell Research, .
- Sun, Y., H. H. Chung, A. R. E. Woo and V. C. L. Lin. (2014). Protein arginine methyltransferase 6 enhances ligand-dependent and -independent activity of estrogen receptor α via distinct mechanisms. Biochimica et Biophysica Acta - Molecular Cell Research, 1843(9), 2067-2078.
- Shenglan Cao, J. K. Iyer, and Valerie CL. Lin. (2006). Identification of tetratricopeptide repeat domain 9, a hormonally regulated protein. Biochemical and Biophysical Research Communications, 345, 310-317.
- Maria Stepanova, Feng Lin and Valerie CL Lin. (2006). Establishing a statistic model for recognition of steroid hormone response elements. Computational Biology and Chemistry, 30, 339-47.
- Maria Stepanova, Feng Lin, and Valerie CL Lin. (2006). In Silico Modeling of Hormone Response Elements. BMC Bioinformatics, S4, 27.