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Dadun > Depósito Académico > CIMA (Centro de Investigación Médica Aplicada) > Área de Oncología > Biomarcadores > DA - CIMA - Oncología - Biomarcadores - Artículos de Revista >

Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas
Authors: Martinez, A. (Alfredo)
Montuenga, L.M. (Luis M.)
Springall, D.R. (David R.)
Treston, A.M. (Anthony M.)
Cuttitta, F. (Frank)
Polak, J.M. (Julia M.)
Keywords: PAM
PHM
PAL
Human pancreatic islets
Glucagon
PP
Insulin
Somatostatin
Immunocytochemistry
Double immunogold staining
Issue Date: 1993
Publisher: Histochemical Society
Publisher version: http://jhc.sagepub.com/content/41/3/375
ISSN: 1551-5044
Citation: Martinez A, Montuenga LM, Springall DR, Treston A, Cuttitta F, Polak JM. Immunocytochemical localization of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in human endocrine pancreas. J Histochem Cytochem 1993 Mar;41(3):375-380.
Abstract
We studied the distribution of the enzymes that are involved in the post-translational alpha-amidation of regulatory peptides in human endocrine pancreas, using immunocytochemical methods for light and electron microscopy. Immunoreactivity for the two enzymes involved, peptidylglycine alpha-hydroxylating monooxygenase (PHM) and peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL), was located in the periphery of the islets of Langerhans and in ductal endocrine cells. Staining of reverse-face serial sections demonstrated that these immunoreactivities co-localize with glucagon but not with pancreatic polypeptide (PP), insulin, or somatostatin. Double immunogold staining for electron microscopy confirmed the previous results and revealed a different localization for each enzyme inside the secretory granule: PHM is present in the central core of the glucagon-containing granules, whereas PAL is predominantly located near the granule membrane. The existence of an amidated peptide, GLP1, in the A-cells explains the presence of peptidylglycine alpha-amidating monooxygenase enzymes (PAM) in these cells. The absence of the enzymes in the PR-cells raises the possibility that a different form of amidating enzyme may be involved in the post-translational processing of this peptide.
Permanent link: http://hdl.handle.net/10171/20127
Appears in Collections:DA - Ciencias - HAP - Artículos de revista
DA - CIMA - Oncología - Biomarcadores - Artículos de Revista

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