Interspecies differences in membrane-associated protease activities of thyrocytes and their relevance for thyroid cancer studies
1 Department of Endocrinology, Metabolism, Nephrology and Clinical Chemistry, Internal Medicine, University of Tuebingen, Otfried-Muellerstrasse 10, 72076, Tuebingen, Germany
2 Institute of Anatomy, University of Tuebingen, Oesterbergstr 3, 72074, Tuebingen, Germany
3 Center for Medical Research, Medical University of Graz, Stiftingtalstr 24, Graz, 8010, Austria
Journal of Experimental & Clinical Cancer Research 2012, 31:45 doi:10.1186/1756-9966-31-45Published: 16 May 2012
To understand the role of proteases involved in human thyroid cancer progression and tissue invasion, thyrocytes from other species could potentially be used provided their characteristics are similar. It is not known whether dipeptidyl peptidase IV and aminopeptidase N activities, which are overexpressed in human thyroid cancer, are, as in human, also absent in normal thyrocytes of other species, making them suitable models for studies on the regulation of these proteases.
To assess the role of these proteases, activity was measured in thyroid tissue of human, mouse, rat, porcine, bovine and ovine origin. The lysosomal protease, dipeptidyl peptidase II, was used for comparison.
Murine, rat, ovine, bovine and human thyrocytes all lacked dipeptidyl peptidase IV and aminopeptidase N activity, but porcine thyrocytes were found to possess both. In contrast, lysosomal dipeptidyl peptidase II was strongly expressed in all species. These activity patterns were maintained in cultured cells. Cultured porcine thyrocytes formed follicles with typical morphology upon stimulation with TSH but differed from human thyrocytes in their response to thiamazole.
These species differences in the expression of dipeptidyl peptidase IV and aminopeptidase N, indicate that porcine thyrocytes cannot be considered appropriate for the study of proteases in human cancer development.