Peptidylglycine α-amidating monooxygenase (PAM) immunoreactivity and messenger RNA in human pituitary and increased expression in pituitary tumours View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-04

AUTHORS

Jennifer H. Steel, Alfredo Martínez, David R. Springall, Anthony M. Treston, Frank Cuttitta, Julia M. Polak

ABSTRACT

Bioactivity of many peptides depends upon post-translational α-amidation of inactive precursors by two enzyme activities known collectively as peptidylglycine α-amidating monooxygenase (PAM). PAM enzymes are particularly abundant in the pituitary. The distribution of PAM immunoreactivity and messenger ribonucleic acid (mRNA) in the adult human pituitary and in pituitary tumours was investigated by use of immunocytochemistry and in situ hybridisation. Immunoreactivity was present in numerous cells of the anterior lobe: staining was intense in a proportion of gonadotrophs and folliculo-stellate cells, but weaker in the majority of somatotrophs and lactotrophs, a few corticotrophs and occasional thyrotrophs. PAM staining was also present in nerves, pituicytes and some endocrine cells within the posterior lobe (the human intermediate zone). Forty pituitary tumours of various types were immunoreactive for PAM; more intensely and uniformly stained than normal anterior lobe. In situ hybridisation with digoxigenin-labelled probes demonstrated intense labelling for PAM mRNA in numerous cells in normal anterior pituitary and in tumours. Many regulatory peptides that require amidation for activity, potential targets for PAM, are present in the pituitary. Many tumour growth factors also require amidation and PAM may regulate these mitogenic peptides in tumours. More... »

PAGES

197-207

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00354800

DOI

http://dx.doi.org/10.1007/bf00354800

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1007234855

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8187161


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