Summary
A histochemical study ofα-d-mannosidase revealed that normal human melanocytes (resting state, activated, lentigo simplex) exhibit either no or just detectable activity, as do melanocytes in the initial phase of lentigo maligna. Junctional, or occasionally zone A naevocytes displayed a very low enzyme activity. On the other hand, melanocytes in the initial stage of neoplastic transformation (dysplastic naevi, advanced stage of lentigo maligna) and also melanoma cells in disorders of low malignant potential (initial naevogenic melanoma, superficial spreading melanoma) displayed a high activity uniformly throughout the cell population. In the malignant forms (nodular melanoma, recurrences, metastases), the enzyme activity was remarkably heterogeneous, suggesting a breakdown of uniformity during malignant transformation. The significance of α-mannosidase activity induction in the course of melanocyte neoplastic transformation is not clear at present. The results of biochemical assays suggest that the lysosomal isoenzyme is mainly responsible. Other lysosomal enzymes, and dehydrogenases studied concomitantly, did not display any comparable phenomena of induction or similar behaviour. However, the results of a comparison ofα-mannosidase with the melanocyte reference enzyme tyrosinase suggested activity patterns in the enzyme pair which may provide a better insight into the biochemical differentiation of human melanocytes in neoplastic disorders. The possible relationship ofα-mannosidase to melanogenesis is also discussed.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
BARRETT, J. (1972) Lysosomal enzymes. InLysosomes: A Laboratory Handbook (edited by DINGLE, J. T.), pp. 46–135. Amsterdam and London: North Holland.
BECKER, S. W., PRAVER, L. L. & THATCHER, H. (1935) Improved (paraffin section) method for dopa reaction, with considerations of dopa-positive cells, as studied by this method.Arch. Derm. Syph. (Berlin) 31, 190–205.
BOROVANSKÝ, J. (1978) Quantitative parameters of melanoma differentiation.Neoplasma 25, 349–52.
BRAUN-FALCO, O. & BURG, G. (1973) Zur Enzym-Histochemie des malignen Melanoms: Untersuchungen an Primärtumoren und Metastasen.Arch. Dermatol. Forsch. 246, 303–16.
BRESLOW, A. (1970) Thickness, cross-sectional areas and depths of invasion in the prognosis of cutaneous melanoma.Ann. Surg. 172, 902–8.
CALABRESI, P. & DEXTER, D. L. (1982) Clinical implications of cancer cell heterogeneity. InTumor Cell Heterogeneity, Origins and Implications (edited by OWENS, A. H., Jr., COFFEY, D. S. and BAYLIN, S. B.), pp. 181–204. New York: Academic Press.
CHEN, Y. M. & CHAVIN, W. (1975) Melanogenesis in human melanomas.Cancer Res. 35, 606–12.
CLARK, W. H., FROM, L., BERNARDINO, E. A. & MIHM, M. C. (1969) The histogenesis and biologic behaviour of primary human malignant melanomas of the skin.Cancer Res. 29, 705–27.
DEWALD, D. & TOUSTER, O. (1973) A newα-d-mannosidase occuring in Golgi membranes.J. biol. Chem. 248 7223–33.
ELDER, D. E., GOLDMAN, L. J., GOLDMAN, S. C., GREENE, M. H. & CLARK, W. H. (1980) Dysplastic nevus syndrome: a phenotypic association of sporadic cutaneous melanoma.Cancer 46, 1787–94.
ELLEDER, M. (1975) Activity of α-d-mannosidase in human Langerhans epidermal cells.Virchows Arch. B Cell Path. 19, 93–6.
ELLEDER, M., POVÝŠIL, C., ROZKOVCOVÁ, J. & ČIHULA, J. (1977)α-d-mannosidase activity in histiocytosis X.Virchows Arch. B Cell Path. 26, 139–54.
HEARING, V. J., NICHOLSON, J. M., MONTAGNE, P. M., EHEL, T. M. & TOMECKI, K. J. (1978) Mammalian tyrosinase. Structural and functional interrelationship of isoenzymes.Biochim. Biophys. Acta 522, 327–49.
HERRMANN, W. P. & UNHLENBRUCK, G. (1975) Serological studies on the carbohydrate moiety of human tyrosinase.Arch. Derm. Res. 254, 275–80.
HUNTER, J. A. A., PATERSON, W. D. & FAIRLEY, D. J. (1978) Human malignant melanoma. Melanosomal polymorphism and the ultrastructural dopa reaction.Brit. J. Derm. 98, 381–90.
IMOKAWA, G. & MISHIMA, Y. (1982) Loss of melanogenic properties in tyrosinases induced by glycosylation inhibitors within malignant melanoma cell.Cancer Res. 42, 1994–2002.
LOJDA, Z., GOSSRAU, R. & SCHIEBLER, T. H. (1979)Enzyme Histochemistry. A Laboratory Manual. Berlin, Heidelberg and New York: Springer.
MCGOVERN, V. J. (1982)Melanoma. Histological Diagnosis and Prognosis. (Biopsy Interpretation Series), pp. 3–36. New York: Raven Press.
MISHIMA, Y. M. & MATSUNAKA, M. (1973) Macromolecular pathology of pagetoid melanoma. InPigment Cell I. pp. 292–299. Basel: Karger.
NISHIOKA, K. (1978) Particulate tyrosinase of human malignant melanoma. Solubilization, purification following trypsin treatment, and characterization.Eur. J. Biochem. 85, 137–46.
NOVIKOFF, A. B., ALBALA, A. & BIEMPICA, L. (1968) Ultrastructural and cytochemical observations on N-16 and Harding—Passey mouse melanomas.J. Histochem. Cytochem. 16, 299–319.
NOWELL, P. C. (1982) Genetic instability of cancer cells: relationship to tumor heterogeneity. InTumor Cell Heterogeneity. Origin and Implications (edited by OWENS, A. H., COFFEY, D. S. and BAYLIN, S. B.), pp. 351–69. New York: Academic Press.
OHTAKI, N. (1970) Melanosome and lysosome. I. Lysosomal activity in relation to growth of melanoma.Bull. Tokyo Med. Dental Univ. 17, 89–102.
OWENS, A. H. (1982) Tumor cell heterogeneity: a perspective. InTumor Cell Heterogeneity. Origin and Implications (edited by OWENS, A. H., COFFEY, D. S. and BAYLIN, S. B.), pp. 3–8. New York: Academic Press.
PAUL, E. (1975) Histochemical findings in different types of malignant melanoma: biological and clinical significance.Arch. Derm. Res. 254, 159–74.
PAUL, E. & GERNAND, E. (1975) Increase of melanocytes around malignant melanoma.Arch. Derm. Forsch. 252, 275–83.
PAWELEK, J., WONG, G., SANSONE, M. & MOROWITZ, J. (1973) Molecular controls in mammalian pigmentation.Yale J. Biol. Med. 46, 430–43.
PHILLIPS, N. C., ROBINSON, D. & WINCHESTER, B. G. (1974) Human liver α-mannosidase activity.Clin. chim. Acta 55, 11–19.
PRASAD, R., ROMSDAHL, M. M., SHAW, C. R., MUMFORD, D. M. & SMITH, J. L. (1974) Isoenzyme variations in human malignant melanoma.Cancer Res. 34, 1435–8.
RODRIGUEZ, H. H. & MCGAVRAN, M. H. (1969) A modified dopa reaction for the diagnosis and investigation of pigment cells.Amer. J. clin. Pathol. 52, 219–27.
SHOUP, V. A. & TOUSTER, O. (1976) Purification and characterization of the α-d-mannosidase of rat liver cytosol.J. biol. chem. 251, 3845–52.
VAQUERO, C., MASSON, C., GUIGON, M. & HEWITT, J. (1975)β-Glucuronidase in human cutaneous tumours.Europ. J. Cancer 11, 731–42.
WOLF, K. & SCHREINER, E. (1971) Melanosomal acid phosphatase.Arch. Derm. Forsch. 241, 255–72.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Elleder, M., Borovanský, J., Mazánek, J. et al. Enzyme histochemistry of human melanomas and pigmented naevi with special reference toα-d-mannosidase activity. Histochem J 18, 472–480 (1986). https://doi.org/10.1007/BF01675614
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF01675614