The brain is the command center of the body, processing multitudes of sensory information and controlling many behaviors. The basic information-processing unit in the brain is called a synapse, where two brain cells connect and communicate each other. Increasing evidence indicates that subtle changes in synapse formation can increase risk of developing autism and schizophrenia.
Dr. Peng Zhang’s research interest is to find out how synapses form and affect the communications among different neurons in the brain, and eventually to develop therapeutic strategies for human psychiatric diseases. Working in the lab of Dr. Ann Marie Craig, Dr. Zhang and colleagues have found that a group of membrane glycoproteins, heparan sulfate proteoglycans (HSPGs), are involved in synapse formation.
Dr. Zhang’s research continues to study the mechanism by which HSPGs regulate synapse formation. It will combine biochemical and cell biological methods to study the mechanisms both in primary neuron culture and in a genetic model organism where HSPGs are deficient. This research will help us understand the role of HSPGs in synapse formation, potentially leading to novel ways to treat neuropsychiatric diseases.
Zhang P, Yang Y, Candiello J, Thorn TL, Gray N, Halfter WM, Hu H. Biochemical and biophysical changes underlie the mechanisms of basement membrane disruptions in a mouse model of dystroglycanopathy. Matrix Biol. 2013 Apr 24;32(3-4):196-207. doi: 10.1016/j.matbio.2013.02.002. Epub 2013 Feb 27. (PubMed abstract)
Yu M, He Y, Wang K, Zhang P, Zhang S, Hu H. Adeno-associated viral-mediated LARGE gene therapy rescues the muscular dystrophic phenotype in mouse models of dystroglycanopathy. Hum Gene Ther. 2013 Mar;24(3):317-30. doi: 10.1089/hum.2012.084. (PubMed abstract)
Zhang P, Hu H. Differential glycosylation of α-dystroglycan and proteins other than α-dystroglycan by like-glycosyltransferase. Glycobiology. 2012 Feb;22(2):235-47. doi: 10.1093/glycob/cwr131. Epub 2011 Sep 19. (PubMed abstract)
Zhang Z, Zhang P, Hu H. LARGE expression augments the glycosylation of glycoproteins in addition to α-dystroglycan conferring laminin binding. PLoS One. 2011 Apr 20;6(4):e19080. doi: 10.1371/journal.pone.0019080. (PubMed abstract)
Stalnaker SH, Aoki K, Lim JM, Porterfield M, Liu M, Satz JS, Buskirk S, Xiong Y, Zhang P, Campbell KP, Hu H, Live D, Tiemeyer M, Wells L. Glycomic analyses of mouse models of congenital muscular dystrophy. J Biol Chem. 2011 Jun 17;286(24):21180-90. doi: 10.1074/jbc.M110.203281. Epub 2011 Apr 1. (PubMed abstract)