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
-
The purification and specificity of a neutral endopeptidase from rabbit kidney brush border.
Biochem J. 1974 Mar;137(3):477-88
PMID: 4423492
-
Changes in membrane-bound aminopeptidase on bone marrow-derived macrophages during their maturation in vitro.
Exp Cell Res. 1977 Oct 15;109(2):269-76
PMID: 913492
-
Immunological characterization of human membrane-bound arylamidases from small intestine, lung, kidney, liver, placenta and renal cell carcinoma.
Clin Chim Acta. 1980 Feb 14;101(1):139-43
PMID: 6766825
-
Topology of microvillar membrance hydrolases of kidney and intestine.
Physiol Rev. 1982 Jan;62(1):91-128
PMID: 6119713
-
Organisation of the lymphoreticular system and lymphocyte markers in the pig.
Vet Immunol Immunopathol. 1982 Jan;3(1-2):95-146
PMID: 7048722
-
A monoclonal antibody to kidney endopeptidase-24.11. Its application in immunoadsorbent purification of the enzyme and immunofluorescent microscopy of kidney and intestine.
Biochem J. 1983 Aug 15;214(2):377-86
PMID: 6351851
-
Endopeptidase-24.11 in pig lymph nodes. Purification and immunocytochemical localization in reticular cells.
Biochem J. 1986 Jun 15;236(3):801-10
PMID: 3539105
-
The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11.
Biochem J. 1984 Oct 15;223(2):433-40
PMID: 6149747
-
Are there neuropeptide-specific peptidases?
Biochem Pharmacol. 1985 May 1;34(9):1347-56
PMID: 2986644
-
An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues.
Biochem J. 1985 May 15;228(1):119-26
PMID: 3890837
-
Proteins of the kidney microvillar membrane. The 130 kDa protein in pig kidney, recognized by monoclonal antibody GK5C1, is an ectoenzyme with aminopeptidase activity.
Biochem J. 1985 Sep 15;230(3):753-64
PMID: 4062876
-
An immunohistochemical study of endopeptidase-24.11 ("enkephalinase") in the pig nervous system.
Neuroscience. 1986 Aug;18(4):991-1012
PMID: 3093917
-
Antigen processing and presentation by macrophages.
Am J Anat. 1984 Jul;170(3):483-90
PMID: 6433692