Journal of Histochemistry and Cytochemistry Priciples for Free Access to Science
  Search:   
    >> Advanced Search

Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Saldise, L.
Right arrow Articles by Vazquez, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Saldise, L.
Right arrow Articles by Vazquez, J. J.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Distribution of peptidyl-glycine alpha-amidating mono-oxygenase (PAM) enzymes in normal human lung and in lung epithelial tumors

L Saldise, A Martinez, LM Montuenga, A Treston, DR Springall, JM Polak and JJ Vazquez

Department of Cytology and Histology, University of Navarra, Pamplona, Spain.

C-terminal alpha-amidation is a post-translational modification necessary for the biological activity of many regulatory peptides produced in the respiratory tract. This modification is a two-step process catalyzed by two separate enzyme activities, both derived from the peptidyl-glycine alpha-amidating mono-oxygenase (PAM) precursor. The distribution of these two enzymes, peptidyl-glycine alpha- hydroxylating monoxygenase (PHM) and peptidyl-alpha-hydroxyglycine a amidating lyase (PAL), was studied in the normal lung and in lung tumors using immunocytochemical methods and in situ hybridization. In normal lung the enzymes were located in some cells of the airway epithelium and glands, the endothelium of blood vessels, some chondrocytes of the bronchial cartilage, the alveolar macrophages, smooth muscle cells, neurons of the intrinsic ganglia, and in myelinated nerves. A total of 24 lung tumors of seven different histological types were studied. All cases contained PAM-immunoreactive cells with various patterns of distribution. All immunoreactive cells were positive for the PHM antiserum but only some of them for the PAL antiserum. The distribution of PAM co-localizes with some other previously described amidated peptides, suggesting that amidation is an important physiological process taking place in the normal and malignant human lung tissue.

Volume 44, Issue 1, pp. 3-12, 01/01/1996
Copyright © 1996 by The Histochemical Society


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Cancer Res.Home page
J. Jongsma, M. H. Oomen, M. A. Noordzij, W. M. Van Weerden, G. J. M. Martens, T. H. van der Kwast, F. H. Schröder, and G. J. van Steenbrugge
Androgen Deprivation of the Prohormone Convertase-310 Human Prostate Cancer Model System Induces Neuroendocrine Differentiation
Cancer Res., February 1, 2000; 60(3): 741 - 748.
[Abstract] [Full Text]

Home page
 J. Histochem. Cytochem.Home page
L. Guembe, A. C. Villaro, and A. M. Treston
Immunocytochemical Mapping of the Amidating Enzyme PAM in the Developing and Adult Mouse Lung
J. Histochem. Cytochem., May 1, 1999; 47(5): 623 - 636.
[Abstract] [Full Text]

Home page
 J. Histochem. Cytochem.Home page
A. Martinez, M. J. Miller, K. J. Catt, and F. Cuttitta
Adrenomedullin Receptor Expression in Human Lung and in Pulmonary Tumors
J. Histochem. Cytochem., February 1, 1997; 45(2): 159 - 164.
[Abstract] [Full Text] [PDF]



Guidelines | Subscriptions | About | exPRESS - Current - Archive | Business Information | Contact
The Journal of Histochemistry & Cytochemistry is owned, published, and licensed by The Histochemical Society © 1996