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Gordon, Marion K.


Marion K. Gordon
Associate Professor
Rutgers University
Department of Pharmacology and Toxicology
Piscataway, NJ 08854-8020
(848) 445-3751
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Cell-matrix interactions; cel,. developmental and molecular biology of extracellular matrix molecules

The laboratory of Dr. Marion Gordon is investigating cell-matrix interaction,. as well as the cell, developmental and molecular biology of extracellular matrix molecules. One project studies epithelial cancers: EMMPRIN is a transmembrane molecule on the surface of epithelial-derived tumor cells that directs the neighboring fibroblasts to synthesize matrix metalloproteinases, allowing the tumors to alter the matrix and metastasize. In addition to examining how tumor cells regulate this molecule, the laboratory is attempting to determine the function of EMMPRIN in normal cells. Based on EMMPRIN's function in tumors, the transmembrane molecule is suspected to play a major role in normal matrix remodeling during development.

Another major project examines how extracellular matrix molecules establish the architecture of our tissues and organs during development and in pathology. A subset of collagens, the fibril-associated collagens (FACITs), modulate the properties of collagen fibrils, altering how the fibrils interact with adjacent fibrils. One of the lab's major goals is to understand the role of these bridging molecules in proper tissue architecture. In the developing eye, the cornea is at first opaque, and undergoes a compaction event that results in a transparent cornea. Dr. Gordon's work suggests that the FACIT molecule collagen XIV facilitates the compaction event by preventing the fusion of collagen fibrils. This would maintain fibrils in a lattice that can transmit light.

Misregulation of EMMPRIN and/or FACIT collagens is hypothesized to be important in disease states involving inappropriate synthesis and degradation of extracellular matrix. The laboratory is also investigating the involvement of collagens and EMMPRIN in the premature rupture of fetal membranes, in pulmonary hypertension, as well as in pulmonary and hepatic fibrosis. In each of these pathologies, FACIT collagen XII appears to temporarily stabilize new fibril structures until a permanent stabilization occurs, and a concomitant decrease in FACIT collagen XIV appears to allow type I collagen fibril fusions. Such fusions impair the resiliency of the tissues. Future work will examine the FACIT collagens in cystic fibrosis.


Contact Us

Division of Life Sciences Graduate Program Office
Rutgers, The State University of New Jersey
Nelson Lab-604 Allison Rd
Piscataway, NJ 08854
Phone: 848.445.9517