Document Detail


Enzyme histochemistry of human melanomas and pigmented naevi with special reference to alpha-D-mannosidase activity.
MedLine Citation:
PMID:  3096914     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A histochemical study of alpha-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 alpha-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 of alpha-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 of alpha-mannosidase to melanogenesis is also discussed.
Authors:
M Elleder; J Borovanský; J Mazánek; F Vosmík
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Histochemical journal     Volume:  18     ISSN:  0018-2214     ISO Abbreviation:  Histochem. J.     Publication Date:  1986 Sep 
Date Detail:
Created Date:  1987-01-22     Completed Date:  1987-01-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0163161     Medline TA:  Histochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  472-80     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / analysis
Alkaline Phosphatase / analysis
Carboxylesterase
Carboxylic Ester Hydrolases / analysis
Glucuronidase / analysis
Histocytochemistry
Humans
Mannosidases / analysis*
Melanoma / analysis*
Monophenol Monooxygenase / analysis
Nevus, Pigmented / analysis*
Oxidoreductases / analysis
Skin Neoplasms / analysis*
alpha-Mannosidase
Chemical
Reg. No./Substance:
EC 1.-/Oxidoreductases; EC 1.14.18.1/Monophenol Monooxygenase; EC 3.1.1.-/Carboxylic Ester Hydrolases; EC 3.1.1.-/chloroacetate esterase; EC 3.1.1.1/Carboxylesterase; EC 3.1.3.1/Alkaline Phosphatase; EC 3.1.3.2/Acid Phosphatase; EC 3.2.1.-/Mannosidases; EC 3.2.1.24/alpha-Mannosidase; EC 3.2.1.31/Glucuronidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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