Enzyme-ultracytochemical study of adenylate and guanylate cyclases in normal and pathologic human nasal mucosa.
The ultracytochemical localization of adenylate cyclase (AC) and guanylate cyclase B (GC-B) and C (GC-C) activity was studied after stimulation with pituitary adenylate cyclase activating peptide, C-type natriuretic peptide and guanylin, respectively, in normal human respiratory nasal mucosa and mucosa of nasal polyps. To demonstrate these enzymatic activities, we employed enzyme-ultracytochemical methods for electron microscopy. Both normal and pathologic nasal mucosa contained AC, GC-B and GC-C activity. In the upper portion of respiratory epithelium, the enzymes were detected on ciliary and microvillar membranes. In ciliary membranes, GC-B was the predominant form expressed. In goblet cells and in glands of the lamina propria, enzymatic activities were localized mainly on plasma membranes and on membranes lining secretory granules. The results did not reveal any evident differences between the enzymatic activities in normal and pathological nasal mucosa and suggest complementary activities for these enzymes and their stimulators in the regulation of mucociliary transport and glandular secretion.
Rambotti
M G
MG
Section of Anatomy, Department of Experimental Medicine and Biochemical Sciences, University of Perugia, Italy.
Altissimi
G
G
Spreca
A
A
D000262:Adenylyl Cyclases / Q000032:analysis / Q000096:biosynthesis*; D006162:Guanylate Cyclase / Q000032:analysis / Q000096:biosynthesis*; D006651:Histocytochemistry / Q000379:methods; D006801:Humans; D007527:Isoenzymes / Q000032:analysis / Q000096:biosynthesis; D009297:Nasal Mucosa / Q000201:enzymology* / Q000473:pathology; D009298:Nasal Polyps / Q000201:enzymology* / Q000473:pathology
D007527:Isoenzymes; D000262:Adenylyl Cyclases; D006162:Guanylate Cyclase