Dr. Lucinda Jack

Jack Email

LUCINDA J. W. JACK
UNIVERSITY LECTURER
Education
B.S. (Microbiology) University College, University of London, 1982
Ph.D. (Molecular Biology) University of London, 1986.
email ljwjack@comcast.net
(301) 854-3413

COURSES TAUGHT
BSCI 222 Principles of Genetics
LCLFS 609A Food Safety and Genetically Modified Foods

PROFESSIONAL EXPERIENCE
1/02 - present Editing, Journal of Biological Chemistry , American Society of Biochemistry and Molecular Biology

7/99 - present University Lecturer, College of Chemical and Life Sciences, University of Maryland, College
Park, MD 20742.

7/97 - 6/99 Director of Science Outreach & Special Programs, College of Life Sciences,
University of Maryland, College Park, MD 20742.
6/95 – 6/97 Assistant to the Dean, Science Outreach, College of Life Sciences,
University of Maryland, College Park, MD 20742.

11/93 – 5/95 Manager of the Protein Sequencing Lab, Medical Biotechnology Center,
University of Maryland at Baltimore.

6/90 – 9/93 Research Biologist, Agricultural Research Service, USDA, Beltsville, MD 20705.

10/86 – 6/90 Faculty Research Associate, Department of Animal Sciences, University of Maryland, College Park, MD 20742.

9/82 – 9/86 Medical Laboratory Scientific Officer, Courtauld Institute of Biochemistry, UCL and Middlesex Hospital School of Medicine, University of London, England.SCIENTIFIC

INTERESTS

1. Genetics & biochemistry: Cloning and characterizing genes encoding proteins expressed in milk; regulation and expression of transfected genes; ontogeny of expression of mammary gland development genes; the role of butyrophilin in milk-fat secretion; characterization of bacteriocidal and bacteriostatic bovine proteins; purification (HPLC) and characterization (sequencing) of proteins.
2. Food Safety: Transmissible spongiform encephalopathies, in vitro genetically-modified foods.

SELECTED PEER REVIEWED PUBLICATIONS

Laird, J.E., Jack L.J.W., Hall, L., Boulton, A.P., Parker, D. and Craig, R.K. (1988). Structure and expression of the guinea-pig _-lactalbumin gene. Biochem. J. 254, 85 – 94.

Jack, L.J.W., and Mather, I.H. (1990). Molecular cloning and analysis of cDNA encoding bovine butyrophilin, an apical membrane glycoprotein expressed in lactating mammary tissue and secreted in association with the milk-fat globule membrane during lactation, J. Biol. Chem. 265, 14481 – 14486.

Madara, P.J., Banghart, L.R., Jack, L.J.W. and Mather, I.H. (1990). Affinity purification of polyclonal antibodies from antigen immobilized in situ in sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem. 187, 246 – 250.

Mather, I.H. and Jack, L.J.W. (1993). A review of the molecular and cellular biology of butyrophilin, the major protein of bovine milk-fat globule membrane. J. Dairy Sci. 76,
3832 – 3850.

Vernet, C., Boretto, J., Mattei, M-G., Takahashi, M., Jack, L.J.W., Mather, I.H., Rouquier, S., and Pontarotti, P. (1993). Evolutionary study of multigene families mapping close to the human MHC class I region. J. Mol. Evol. 37, 600 - 612.

Capuco A.V., Mein, G.A., Nickerson, S.C., Jack, L.J.W., Wood, D.L., Bright, S.A., Aschenbrenner, R.A., Miller, R.H., and Bitman, J. (1994). Influence of pulsationless milking on teat canal keratin and mastitis. J. Dairy Sci. 77, 64 – 74.

Jack, L.J.W., Kahl, S., St. Germain, D., and Capuco, A.V. (1994). Tissue distribution and regulation of 5’-deiodinase processes in lactating rats. J. Endocrinol. 142, 205 – 215.
Molenaar, A.J., Davis S.R., Jack L.J.W., and Wilkins, J. (1995). Expression of the butyrophilin gene, a milk–fat globule membrane protein, is associated with the expression of _-S1-casein gene. Histochem. J. 27, 388 – 394.

Banghart, L.R., Chamberlain, C.W., Velarde, J., Korobko, I.V., Ogg, S.L., Jack, L.J., Vakharia, V.N., and Mather. I.H. (1998). Butyrophilin is expressed in mammary epithelial cells from a single-sized messenger RNA as a type I membrane glycoprotein. J. Biol. Chem. 273, 4171 – 4179.

Mather I.H., Jack, L.J.W., Madara, P.J., and Johnson, V.G. (2001). The distribution of MUC1, an apical glycoprotein, in mammary epithelial cells at the resolution of the electron microscope: Implications for the mechanism of milk secretion. Cell Tiss. Res. 304, 91 – 101.