The Histochemical Journal

, Volume 14, Issue 3, pp 507–515 | Cite as

Immunohistochemical distribution of aldose reductase

  • Timothy S. Kern
  • Ronald L. Engerman


Aldose reductase (AR) has been purified from canine kidneys., and a monospecific antibody against the enzyme prepared. These antibodies were used in an immunohistochemical test to detect tissue sites of aldose reductase in the dog, a species known to develop diabetic lesions morphologically identical to those seen in diabetic patients. Using this method, the enzyme has been demonstrated in numerous cell types, including lens, epithelium, aortic endothelium and smooth muscle, Schwann cells of peripheral nerves, and, in the kidney, interstitial cells and cells of Henlés loop and the collecting tubules. Many other cells and tissues, including capillaries throughout the body, lack immunoreactive aldose reductase. The distribution of the immunoreactive enzyme is compatible with a potential role of the enzyme in the aetiology of some complications of diabetes, namely cataract, neuropathy, macroangiopathy and renal papillary necrosis, but not the microvascular complications.


Neuropathy Diabetic Patient Cataract Peripheral Nerve Schwann Cell 
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  1. Beaumont, P., Hollows, F. C., Schofield, P. J., Williams, J. F. &Steinbeck, A. W. (1971) Growth hormone, sorbitol, and diabetic capillary disease.Lancet 1, 579–81.Google Scholar
  2. Bloodworth, J. M. B., Jr, Engerman, R. L. &Anderson, P. J. (1973) Microangiopathy in the experimentally diabetic animal.Adv. Metab. Dis. Suppl.2, 245–50.Google Scholar
  3. Dons, R. F. &Doughty, C. C. (1976) Isolation and characterization of aldose reductase from calf brain.Biochim. biophys. Acta 452, 1–12.Google Scholar
  4. Engerman, R. L. (1976) Animal models of diabetic retinopathy.Trans. Am. Acad. Ophthalmol. Otol. 81, 710–5.Google Scholar
  5. Engerman, R., Bloodworth, J. M. B., Jr &Nelson, S. (1977) Relationship of microvascular disease in diabetes to metabolic control.Diabetes 26, 760–9.Google Scholar
  6. Frank, R. N., Chang, S. S. &Mikus, K. P. (1978) Aldose reductase activity of retinal and cerebral microvessels.Diabetes 27, Suppl. 2, 475.Google Scholar
  7. Gabbay, K. H. (1973) Role of sorbitol pathway in neuropathy. InVascular and Neurological Changes in Early Diabetes (edited byCamerini-Davalos, R. A. andCole, H. S.), pp. 417–424. New York: Academic Press.Google Scholar
  8. Gabbay., K. H. (1975) Hyperglycemia, polyol metabolism, and complications of diabetes mellitus.Ann. Rev. Med. 26, 521–36.Google Scholar
  9. Gabbay, K. H. &Cathcart, E. S. (1974) Purification and immunologic, identification of aldose reductase.Diabetes 23, 460–8.Google Scholar
  10. Gornall, A. G., Bardawill C. J. &David, M. M. (1949) Determination of serum proteins by means of the biuret reaction.J. biol. Chem. 177, 751–66.Google Scholar
  11. Hartman, B. K. &Udenfriend, S. (1969) A method for immediate visualization of proteins in acrylamide gels and its use for preparation of antibodies to enzymes.Analyt. Biochem. 30, 391–4.Google Scholar
  12. Kern, T. S. (1980)Tissue distribution of aldose reductase and polyol-producing enzyme activity. Ph.D. thesis, University of Wisconsin-Madison.Google Scholar
  13. Kern, T. S. &Engerman, R. L. (1981) Distribution of aldose reductase in ocular tissues.Expl Eye Res. 33, 175–82.Google Scholar
  14. Kibrick, A. C. &Blonstein, M. (1948) Fractionation of serum into albumen and α-, β-, and γ-globulin by sodium sulfate.J. biol. Chem. 176, 983–7.Google Scholar
  15. Kinoshita, J. H. (1974) Mechanisms initiating cataract formation (Proctor Lecture).,Invest. Ophthalmol. 13, 713–24.Google Scholar
  16. Ludvigson, M. A. &Sorenson, R. L. (1980a) Immunohistochemical localization of aldose reductase. I. Enzyme purification and antibody preparation-localization in peripheral nerve, artery, and testis.Diabetes 29, 438–49.Google Scholar
  17. Ludvigson, M. A. &Sorenson, R. L. (1980b) Immunohistochemical localization of aldose reductase. II. Rat eye and kidney.Diabetes 29, 450–9.Google Scholar
  18. Morrison, A. D., Clements, R. S., Jr. &Winegrad, A. I. (1972) Effects of elevated glucose concentrations on the metabolism of the aortic wall.J. clin. Invest. 51, 3114–23.Google Scholar
  19. Rasio, E. A. &Morrison, A. D. (1978) Glucose-induced alterations of the metabolism of an isolated capillary preparation.Diabetes 27, 108–13.Google Scholar
  20. Sternberger, L. A., Hardy, P. H., Jr, Cuculia, J. J. &Meyer, H. G. (1970) The unlabeled antibody enzyme method of immunohistochemistry. Preparation and properties of a soluble antigen-antibody complex (horseradish peroxidase-antihorseradish peroxidase) and its use in identification of spirochetes.J. Histochem. Cytochem. 18, 315–33.Google Scholar
  21. Streefkerk, J. G. (1972) Inhibition of erythrocyte pseudoperoxidase activity by treatment with hydrogen peroxide following methanol.J. Histochem. Cytochem. 20, 829–31.Google Scholar
  22. Varma, S. D. &Kinoshita, J. H. (1974) Sorbitol pathway in diabetic and galastosemic rat lens.Biochim. biophys. Acta 338, 632–40.Google Scholar
  23. Winegrad, A. I., Morrison, A. D. &Clements, R. S., Jr, (1972) Alterations in the composition and metabolism of the inner aortic wall associated with increased polyol pathway activity.Hormone Metabol. Res. 4, 169–71.Google Scholar

Copyright information

© Chapman and Hall Ltd 1982

Authors and Affiliations

  • Timothy S. Kern
    • 1
  • Ronald L. Engerman
    • 1
  1. 1.Department of OphthalmologyUniversity of WisconsinMadisonUSA

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