Jean Jiang, PhD photo
Jean Jiang, PhD

Jean Jiang, PhD, Ashbel Smith Professor

Room:208.4-STRF Building
Phone:562-4094
Email:jiangj@uthscsa.edu
Web Page(s):http://biochem.uthscsa.edu/~jiang
Education:Ph.D. State University of New York at Stony Brook
Post Doctoral:Harvard Medical School
Other Faculty Positions:Associate Director, Joint Biomedical Engineering Graduate Program of UTSA/UTHSCSA

Research Interest:

Gap junction and hemichannel research
Cells connect and communicate via an information superhighway named gap junctions. Gap junctions are clusters of transmembrane channels that connect the cytoplasms of adjacent cells. These channels are formed by a family of proteins called connexins. Gap junction channels permit small metabolites, ions, and second messengers to pass from cell to cell. For cells like bone osteocytes, signals generated by mechanical loading can be transmitted extensively at high speed through gap junction channels. Therefore, gap junctions provide the critical means for cell survival and for physiological regulation of cellular functions. Cells like lens fibers within the interior of the vertebrate eye lens have neither a blood supply nor organelles. Thus, lens survival and homeostasis are uniquely dependent upon intercellular communication via gap junctions with the cells localized at the lens surface. In addition to forming gap junctions, connexins are recently shown to form hemichannels, un-apposed halves of gap junction channels. Hemichannels mediate the passage of biological molecules, especially for cells under stress conditions. Moreover, the activation of hemichannels exerts intrinsic defensive system of the bone tissue against tumor invasion. Our current research interests are focusing on three research areas: 1) To investigate the mechanistic role of osteocytic connexin hemichannels in suppression of breast cancer bone metastasis; 2) To explore the functional significance of gap junctions and hemichannels in transmitting the signals generated by mechanical stress for bone formation and remodeling; 3) To determine the gap junction or hemichannel-dependent and independent roles of connexins in cell differentiation and lens development.

Amino acid transporter research:
Cellular metabolic needs are fulfilled by import of amino acids across the plasma membrane via specialized transporter proteins. We have identified a new family of amino acid transporters. Our current research interests are: 1). To characterize the functions and the structure-function relationship of identified transporters. 2). To investigate the biological roles of the amino acid transporters in vivo using gene knockout mouse model.

Selected publications:

  • Osteocytic connexin 43 hemichannels suppress breast cancer growth and bone metastasis.
    Zhou, J.Z., Riquelme, M.A., Gu, S., Kar, R., Gao, X., Sun, L and Jiang, J. X.
    Oncogene: 2016-10-27; 35(43); 5597-5607     Epub: 2016-04-04.
    PMID:    LINK:
  • Connexin controls cell cycle exit and cell differentiation by directly promoting cytosolic localization and degradation of E3 ligase Skp2.
    Shi, Q., Gu, S., Yu, X.S., White, T.A., Banks, E.A., and Jiang, J.X.
    Dev. Cell.: 2015-11-23; 35(4); 483-496     Epub: 2015-11-12.
    PMID:    LINK:
  • Differential impact of adenosine nucleotides released by osteocytes on breast cancer growth and bone metastasis
    Zhou, J.Z., Riquelme, M.A., Ellies, L.G., Sun, L-Z., Jiang, J.X.
    Oncogene: 2015-04-02; 34(14); 1831-42     Epub: 2014-05-19.
    PMID:    LINK:
  • Mechanical stress-activated integrin α5β1 induces opening of connexin 43 hemichannels.
    Batra, N, Burra, S., Siller-Jackson, A.J, Gu, S., Xia, X., Weber, G.F., DeSimone, D., Bonewald L.F., Lafer E.M., Sprague, E., Schwartz, M.A., and Jiang, J.X.
    Proc. Natl. Acad. Sci. USA.: 2012-02-28; 109(9); 3359-3364     Epub: 2012-02-13.
    PMID:    LINK:
  • Dendritic process of osteocytes is a mechanotransducer that induces the opening of hemichannels
    Burra, S., Nicolella. D.P., Francis, W.L., Freitas, C.J., Mueschke, N.J., Poole, C., and Jiang, J.X.
    Proc. Natl. Acad. Sci., USA: 2010-08-03; 107(31); 13648-13653     Epub: 2010-07-19.
    PMID:    LINK:

Complete Publication Listing

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