Immunological detection of nitric oxide synthase(s) in human tissues using heterologous antibodies suggesting different isoforms View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1992-11

AUTHORS

D. R. Springall, V. Riveros-Moreno, L. Buttery, A. Suburo, A. E. Bishop, M. Merrett, S. Moncada, J. M. Polak

ABSTRACT

Nitric oxide (NO) is generated from l-arginine by NO synthases. Localization of the brain enzyme has been carried out in the rat; however, despite data suggesting that NO is a major regulator of vascular and neural functions in man, there is no information about the localization of NO synthase in human tissues. Rabbit antisera to NO synthase purified from rat brain (antisera A and B) were raised, tested by Western blotting, affinity purification and enzyme immunoprecipitation assay, and used to investigate the distribution of the enzyme in a variety of human tissues by immunohistochemistry. Antisera to two synthetic peptides from cloned neural NO synthase were used to aid specificity testing. Antisera A and B reacted with a ∼ 160-kDa protein in Western blots of human brain extracts, gave immunostaining of nerves, and precipitated enzyme activity from rat brain homogenates. Antiserum B to NO synthase also reacted with proteins of Mr between 125 and 140 kDa in extracts of well-vascularised tissues, and immunostained vascular endothelium; the neural and vascular immunoreactivity persisted after affinity purification of antiserum B with the ∼ 160 kDa protein. Endothelial staining with antiserum B was seen in respiratory tract, liver, skin and umbilicus; syncytial trophoblasts stained in the placenta. Neural staining with antiserum A and B was seen in the myenteric and submucous plexus, and in nerve fibres in smooth muscle of the gut and in many areas of the central nervous system, particularly cortex, hippocampus, hypothalamus, cerebellum, brain stem and spinal cord. Therefore, antibodies to rat brain enzyme react with the human equivalent and also with other NO synthase isoforms in human endothelium. These findings support the contention that the endothelial enzyme is a different form with partial homology to that in nerves and also provide an anatomical distribution of NO synthase isoforms. More... »

PAGES

259-266

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00271040

DOI

http://dx.doi.org/10.1007/bf00271040

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036857784

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1281146


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