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Morphological and Biochemical Changes in the Pancreas of the Copper-Deficient Female Rat^{1,2,3, 3}

Michael A. Dubick^*,+, Gloria S. M. Yu and Adhip P. N. Majumdar^,¶

^* Division of Military Trauma Research, Letterman Army Institute of Research, Presidio of San Francisco, CA 94129 ⁺ Department of Nutrition, University of California, Davis, CA 95616 Department of Pathology, Veterans Administration Medical Center, Martinez, CA 94553 Research Service, Veterans Administration Medical Center, Allen Park, MI 48101 ^¶ Departments of Medicine and Nutrition and Food Science, Wayne State University, Detroit, MI 48201

Earlier histological studies have demonstrated that copper deficiency results in a selective and progressive atrophy of pancreatic acinar tissue. The present study examines both biochemical and morphological changes of the exocrine pancreas in nutritional copper deficiency. Groups of mature female rats were fed a purified diet either deficient (< 0.5 µg/g) or sufficient (6.2 µg/g) in copper for 6 wk. Copper deficiency resulted in distinct ultrastructural changes in acinar cells, including marked variability in zymogen granule content, autophagic vacuoles and dilation of acinar lumen. Pancreatic weight and total DNA, RNA and protein content of the pancreas were similar in both groups of rats, whereas pancreatic amylase, trypsin and chymotrypsin activity was significantly lower in the copper-deficient group. In addition, secretagogue-induced release of these enzymes from dispersed acini isolated from copper-deficient rats was significantly reduced in comparison to enzyme secretion from normal controls. Pancreatic Cu-Zn and Mn superoxide dismutase activity was also found to be significantly lower in the copper-deficient rats than in normal controls. We conclude that nutritional copper deficiency in adult female rats reduces the responsiveness of the pancreas to secretagogues and may increase the susceptibility of the pancreas to oxidative damage.

KEY WORDS: • copper deficiency • pancreas • pancreatic acini • amylase • trypsinogen • superoxide dismutase • rat

¹ Supported by the Medical Research Service of the Veterans Administration and a Grant-in-Aid from the American Heart Association, California Affiliate, and with funds contributed by the American Heart Association, Central Mission Trails Chapter.

² The opinions and assertions contained herein are the private views of the authors and are not to be construed as official or as reflecting the views of the Department of the Army or the Department of Defense (AR 360-5).

³ In conducting the research described in this report, the investigators adhered to the Guide for the Care and Use of Laboratory Animals, as promulgated by the Committee on Revision of the Guide for Laboratory Animal Facilities and Care, Institute of Laboratory Animal Resources, National Research Council.

Manuscript received 13 December 1988. Revision accepted 13 April 1989.