UA Life Science Research - BioGate


Anne E Cress PhD


Anne Cress Contact Information

Address: Arizona Cancer Center Room 4963
PO 245024
1515 N. Campbell Avenue
Tucson, AZ 85724-5024
Phone: (520) 626-7553
E-Mail: acress@azcc.arizona.edu

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Department Affiliations
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Research Areas

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Research Interests

My research interest is to understand the regulation of normal and cancer cell responses to environmental signals. The response of cells to extracellular signals is one determinant of epithelial cancer progression and is a major avenue to exploit for new therapeutic and diagnostic purposes. The following major areas of research are investigated in my laboratory.

1) The response of cells to adhesive signals via integrin cell surface molecules. The integrins are major cell surface molecules that are responsible for the signaling of environmental changes to cells within a tissue environment. One specific integrin, a6b1, is a laminin receptor and is persistently expressed in progressing epithelial cancers and in metastatic lesions. Our current work is to understand the contribution of variant forms of the alpha 6 integrin to cancer progression and to develop ligand mimetics. During the course of this work, we have discovered a novel form of the a6b1 integrin expressed on tumor cells and have identified lead peptides that may prove useful in modifying tumor cell progression. Alternatively, these agents may be useful for specific targeting of tumor cells for diagnostic and therapeutic purposes.

2) The response of human cells to the extracellular matrix protein, laminin. We recently purified two forms of laminin called laminin 5 and laminin 10. These proteins are the ligands for the integrins a6b4 and a6b1, respectively, and act as powerful signaling molecules to direct cellular responses. Our current working hypothesis is that these ligands and their fragments promote cell migration and distinct cellular transcription responses. We currently are using DNA microarray technology to determine whether specific laminin forms and fragments will trigger specific patterns of gene activation. These ligands also are being tested for their ability to promote attachment and spreading characteristics of human microvessel endothelial cells for use in human graft material.

3) The response of cells to damaging agents. In particular, we have studied the signaling responses of normal and tumor cells to ionizing radiation and chemotherapeutic agents. During the course of this work, we have discovered a novel form of drug resistance that is dependent upon the cytoskeleton and cellular adhesion.

Selected Publications
Davis TL, Rabinovitz I, Futscher BW, Cress AE . Identification of a novel structural variant of the a6 integrin. J. Biol. Chem .,276:(28)26099-26106, 2001.

DeRoock IB, Pennington ME, Sroka TC, Lam KS, Bowden GT, Bair El, Cress AE. Synthetic peptides inhibit adhesion of human tumor cells to extracellular matrix proteins. Cancer Research ,61:3308-3318, 2001.

Schmelz M, Cress AE , Scott KM, Burger F, Cui H, Sallam S, McDaniel K, Dalkin BL, Nagle RB. Different phenotypes in human prostate cancer: ?6 or ?3 integrin in cell-extracellular adhesion sites. Neoplasia , 4(2): 243-254 , 2002.

Whitacre DC, Chahuan S, Davis TD, Cress AE , Miesfeld RL. Androgen-induction of in vitro prostate cell differentiation, Cell Growth and Differentiation, 13(1):1-11, 2002

Davis TL, Buerger F and Cress AE . Differential regulation o

Selected Publications

abstract Pawar SC, Dougherty S, Pennington ME, Demetriou MC, Stea BD, Dorr RT, Cress AE. Nov 2007. alpha6 Integrin Cleavage: Sensitizing human prostate cancer to ionizing radiation. Int J Radiat Biol, 83:761-7

abstract King T, Vardanyan A, Majuta L, Melemedjian O, Nagle R, Cress AE, Vanderah TW, Lai J, Porreca F. Nov 2007. Morphine treatment accelerates sarcoma-induced bone pain, bone loss, and spontaneous fracture in a murine model of bone cancer. Pain, 132:154-68

abstract Pawar SC, Demetriou MC, Nagle RB, Bowden GT, Cress AE. Apr 2007. Integrin alpha6 cleavage: a novel modification to modulate cell migration. Exp Cell Res, 313:1080-9

abstract Sroka TC, Pennington ME, Cress AE. Mar 2006. Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5. Carcinogenesis,2006 Mar 14;


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