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PMID: 3546102 Published · ppublish English Journal Article

An immunohistochemical study of endopeptidase-24.11 and aminopeptidase N in lymphoid tissues.

Immunology ·Vol. 60 ·No. 2 ·1987-02-00 ·Pages 247-53

Bowes MA, Kenny AJ

Abstract

Two cell surface peptidases, endopeptidase-24.11 and aminopeptidase N, thought to be involved in metabolizing regulatory peptides, have been immunohistochemically mapped in pig lymphoid organs using specific monoclonal and polyclonal antibodies. In tonsil, spleen, thymus and Peyer's patches, the endopeptidase-24.11 immunoreactivity exhibited a reticular pattern similar to that previously observed in lymph nodes, where this enzyme is much more abundant. Apart from this location in reticular cells, the only structures seen to express endopeptidase-24.11 were Hassall's corpuscles in the thymus, confirming their reticular cell origin. Aminopeptidase N exhibited a cellular distribution quite distinct from that of the endopeptidase. It was associated with cells scattered throughout the lymphoid organs studied, consistent with its localization in macrophages. In lymph nodes, some fibroblasts buried in trabeculae also stained for aminopeptidase, but this was not observed in spleen and thymus.

MeSH Terms
Aminopeptidases/analysis Animals Endopeptidases/analysis Fluorescent Antibody Technique Immunoenzyme Techniques Lymph Nodes/enzymology Lymphoid Tissue/enzymology Neprilysin Palatine Tonsil/enzymology Spleen/enzymology Swine Thymus Gland/enzymology
Chemicals
Endopeptidases Aminopeptidases Neprilysin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bowes M A
Kenny A J
References (13)
13 references, click to expand
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Article Info
Journal
Immunology
Abbr.
Immunology
ISSN
0019-2805
Published
1987-02-00
Pages
247-53
Language
English
Region
England
NLM ID
0374672
PMCID
PMC1453211
Subset
IM
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