- Title Research Assistant Professor, Pilch Laboratory
- Education PhD: Gunma University, Japan
Postdoctoral training: BU School of Medicine, Joslin Diabetes
- Office K6
- Email email@example.com
- Phone 617-638-4045
- Area of Interest Metabolism, diabetes, obesity, Insulin resistance, adipocyte, ribosome biogenesis, ribosomal transcription.
White adipose tissue (WAT) is a highly dynamic organ and can respond rapidly to alterations in nutrient excess and deprivation, thereby fulfilling its major role in whole body energy homeostasis. Dysfunctional WAT leads to the etiology of a large number of metabolic disorders including the metabolic syndrome and type II diabetes. As the major cell type in WAT, a healthy, highly metabolic responsible adipocyte itself is essential in maintaining adipose tissue functions. However, it has been known that the functions of adipocyte start to fail under many physiological (such as aging) and pathological (obesity, metabolic stress and lipodystrophy) conditions. We are trying to ask the questions about: what are the key factors and mechanisms that control adipocyte functional set limit beyond which WAT fails to function properly? One of our recent studies has shown the capacity of adipocyte ribosome biogenesis which is controlled by ribosomal transcription determines the maximal limit of functional homeostasis. Further studies for the components and mechanism details of this regulatory machinery will help us not only to understand the importance of the ribosome biogenesis for adipocyte physiology, but also to develop the potential biomarkers and drug targets for diagnosis, prognosis, and therapy in human obesity.
Libin Liu*, Paul Pilch*. (*Co-corresponding authors). PTRF/Cavin-1 Promotes Efficient Ribosomal RNA Transcription in Response to Metabolic Challenges. Elife. (Accepted). 2016.
Jedrychowski MP, Liu L, Laflamme CJ, Karastergiou K, Meshulam T, Ding SY, Wu Y, Lee MJ, Gygi SP, Fried SK, Pilch PF. Adiporedoxin, an upstream regulator of ER oxidative folding and protein secretion in adipocytes. Mol Metab. 2015 Nov; 4(11):758-70. PMID: 26629401.
Liu L, Hansen CG, Honeyman BJ, Nichols BJ, Pilch PF. Cavin-3 knockout mice show that cavin-3 is not essential for caveolae formation, for maintenance of body composition, or for glucose tolerance. PLoS One. 2014; 9(7):e102935. PMID: 25036884.
Ding SY, Lee MJ, Summer R, Liu L, Fried SK, Pilch PF. Pleiotropic effects of cavin-1 deficiency on lipid metabolism. J Biol Chem. 2014 Mar 21; 289(12):8473-83. PMID: 24509860.
Govender P, Romero F, Shah D, Paez J, Ding SY, Liu L, Gower A, Baez E, Aly SS, Pilch P, Summer R. Cavin1; a regulator of lung function and macrophage phenotype. PLoS One. 2013; 8(4):e62045. PMID: 23634221.
Meshulam T, Breen MR, Liu L, Parton RG, Pilch PF. Caveolins/caveolae protect adipocytes from fatty acid-mediated lipotoxicity. J Lipid Res. 2011 Aug; 52(8):1526-32. PMID: 21652731.
Pilch PF, Liu L. Fat caves: caveolae, lipid trafficking and lipid metabolism in adipocytes. Trends Endocrinol Metab. 2011 Aug; 22(8):318-24. PMID: 21592817.
Pilch PF, Meshulam T, Ding S, Liu L. Caveolae and lipid trafficking in adipocytes. Clin Lipidol. 2011; 6(1):49-58. PMID: 21625349.
Bastiani M, Liu L, Hill MM, Jedrychowski MP, Nixon SJ, Lo HP, Abankwa D, Luetterforst R, Fernandez-Rojo M, Breen MR, Gygi SP, Vinten J, Walser PJ, North KN, Hancock JF, Pilch PF, Parton RG. MURC/Cavin-4 and cavin family members form tissue-specific caveolar complexes. J Cell Biol. 2009 Jun 29; 185(7):1259-73. PMID: 19546242.
Liu L, Brown D, McKee M, Lebrasseur NK, Yang D, Albrecht KH, Ravid K, Pilch PF. Deletion of Cavin/PTRF causes global loss of caveolae, dyslipidemia, and glucose intolerance. Cell Metab. 2008 Oct; 8(4):310-7. PMID: 18840361.
Complete list can be found at BU Profiles