Document Detail


Ultrastructural localization of acid phosphatase in human laryngeal carcinoma.
MedLine Citation:
PMID:  7458755     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The subcellular distribution of acid phosphatase in malignant keratinocytes of invasive laryngeal carcinoma was studied by ultrastructureal cytochemistry. The reaction product was localized in Golgi, ER, and some cytoplasmic vesicles. Acid phosphatase activity was also observed in lysosomal structures in the cortical cytoplasm of basal carcinoma cells. Extracellular acid phohphatase activity also occurred at the tumor-stroma junction in membrane-bound vesicular structures. The localization of acid phosphatase in this report is discussed in relation to acid phosphatase activity in other tumors. The findings lend further support to the important role of hydrolytic enzyme release in respect to tumor invasion into surrounding tissues.
Authors:
P Schenk; K Konrad
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Archives of oto-rhino-laryngology     Volume:  226     ISSN:  0302-9530     ISO Abbreviation:  Arch Otorhinolaryngol     Publication Date:  1980  
Date Detail:
Created Date:  1981-03-24     Completed Date:  1981-03-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0414105     Medline TA:  Arch Otorhinolaryngol     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  213-8     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / metabolism*
Carcinoma, Squamous Cell / enzymology*,  ultrastructure
Humans
Laryngeal Neoplasms / enzymology*,  ultrastructure
Laryngectomy
Larynx / ultrastructure
Lysosomes / enzymology,  ultrastructure
Chemical
Reg. No./Substance:
EC 3.1.3.2/Acid Phosphatase

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


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