Education:
B.S., Bihar University, 1959
M.S., Ranchi University, 1962
Ph.D., University of Vermont, 1969
Training:
1969-1972 , Post Doctoral Research Associate, Oakland University,
Rochester, MI, Major Professor - Dr. C.V. Harding
1973-1975, Special fellow (N.I.H.) at Wayne State University School of Medicine, Kresge Eye Institute
Professional and Faculty Appointments:
1975-1981, Assistant Professor, Department of Anatomy/Cell Biology,
Wayne State University School of Medicine
1981-present, Associate Professor, Department of Anatomy/Cell Biology, Wayne State University School of Medicine
Major Research Interests:
Role of ocular lens proteins in the maintenance of lens transparency.
Current Research
The maintenance of lens clarity is essential for normal vision.
a-crystallins are involved in the maintenance of lens clarity
by their chaperone like activities and supramolecular organization.
Sustained a-crystallin synthesis is necessary for its functional
role. a-crystallin genes and their regulatory regions have been
characterized. However, most of these investigations are performed
in cell free systems and the in vivo regulatory mechanisms of
a-crystallin gene expression are not known. The three dimensional
organization within the nucleus of a cell anchors chromatin at
its proper space, and facilities interactions between genes and
their regulatory proteins. The a-crystallins are small heat shock
proteins and like all other heat shock protein, synthesis of a-crystallins
are presumably regulated by heat shock transcription factors.
We have identified two nuclear matrix proteins, and one of them
by its significant sequence homology, is identified as a member
of the heat shock factor protein family, and another as a aA-crystallin
gene regulatory protein, by its sequence specific binding activity.
The proposed study will further characterize and examine the functional
role of those two nuclear matrix proteins in the regulation of
a-crystallin synthesis.
The data obtained from these studies should reveal the roles of
these two regulatory proteins in the activation of a-crystallin
synthesis, and thereby contribute to our understanding of the
maintenance of lens clarity.
Recent papers:
| 1. | M. Bagchi, A. VanWijnen, M. Katar, H. Merriman, J. Lian, J. Stein, G. Stein, and H. Maisel. Sequence-specific DNA binding activities of nuclear matrix proteins of mammalian lens epithelial cells. J. Cell Biochem. 58, 1-5, 1995. Medline |
| 2. | M. Bagchi, A. Roher, A. Banerjee, Barrett, R., Hazlett, L., Kusunic, T. and Maisel, H. Identification of a ubiquitin like protein in the mammalian vitreous humor. J. Cell Biochem. 61, 26-31, 1996. Medline |
| 3. | M. Bagchi, S. Ansari, M. Katar and H. Maisel. Non-chromatin nuclear proteins of mammalian lens epithelial cells. J. Cell Biochem. 64, 644-65, 1997. Medline |
| 4. | M. Bagchi, S. Ansari, D.M. Lindemuth, A. VanWijmen, J. Lian, J. Stein and G. Stein. Nuclear matrix associated DNA binding proteins of ocular lens epithelial cells. Molecular Biology Reports 25, 13-19, 1998. Medline |
| 5. | M. Bagchi, M. Katar and H. Maisel. A heat shock transcription factor like protein in the nuclear matrix compartment of the tissue cultured mammalian lens epithelial cell. J Cell Biochem. 2001;80(3):382-7.Medline |
About the Department /Graduate Studies /ResearchFaculty /Body Bequest /Vision Core Grant /Medical School Home Page /WayneStateHomePage