| Acid hydrolases of the epidermis: subcellular localization and relationship to cornification. | |
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MedLine Citation:
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PMID: 6188789 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Three lysosomal-type acid hydrolases were examined in subcellular fractions of the developing epidermis of fetal rats to assess the relationship of degradative enzymes to cornification. As the granular layer developed and cornified between 18 and 20 days (D) of gestation, epidermal acid phosphatase increased, acid phospholipase A remained constant, and beta-glucuronidase activity declined. The enzymes were present in 3,000, 17,000, and 100,000 g particulate fractions and soluble cytoplasm. However distribution differed: acid phosphatase and phospholipase A were more preferentially localized than was glucuronidase in the 17,000 g fraction which excluded mitochondria and ribosomes and was enriched in lamellar granules. The findings suggested that acid phosphatase and phospholipase were present in membrane-bound organelles (e.g., lamellar granules) in the granular layer. Particulate acid phosphatase increased with granular layers on days 19 and 20 while a 7-fold increase in soluble enzyme coincided with cornification on day 20. As shown by isoelectric focusing, the enzyme became more heterogeneous at day 20 than at day 18, suggesting increased glycosylation. The particulate fraction displayed lysosomal characteristics with respect to release of acid phosphatase, which was inhibited by hydrocortisone and enhanced by retinol. When fetal epidermis was allowed to cornify in organ cultures, similar increases in acid phosphatase occurred. The presence of hydrocortisone did not affect increase in total enzyme but a greater proportion remained in the particulate fraction. The findings suggest that particulate acid phosphatase and phospholipase are compartmentalized in organelles with lysosomal characteristics during development of granular cells and that release of phosphatase is coincident with cornification. This may reflect not only exocytosis of lamellar granules but also intracellular release of the hydrolytic enzyme. |
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Authors:
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R K Freinkel; T N Traczyk |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The Journal of investigative dermatology Volume: 80 ISSN: 0022-202X ISO Abbreviation: J. Invest. Dermatol. Publication Date: 1983 May |
Date Detail:
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Created Date: 1983-06-17 Completed Date: 1983-06-17 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 0426720 Medline TA: J Invest Dermatol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 441-6 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acid Phosphatase
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physiology Animals Female Glucuronidase / physiology Hydrolases / physiology* Keratins / biosynthesis* Microscopy, Electron Phospholipases A / physiology Pregnancy Rats Skin / enzymology*, growth & development, ultrastructure Skin Physiological Phenomena Subcellular Fractions / enzymology |
| Grant Support | |
ID/Acronym/Agency:
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AM-16441/AM/NIADDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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68238-35-7/Keratins; EC 3.-/Hydrolases; EC 3.1.1.-/Phospholipases A; EC 3.1.3.2/Acid Phosphatase; EC 3.2.1.31/Glucuronidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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