Localisation of mRNA and co-expression and molecular forms of GRP gene products in endocrine cells of fetal human lung View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1988-07

AUTHORS

M. Bhatnagar, D. R. Springall, M. A. Ghatei, P. W. J. Burnet, Q. Hamid, A. Giaid, N. B. N. Ibrahim, F. Cuttitta, E. R. Spindel, R. Penketh, C. Rodek, S. R. Bloom, J. M. Polak

ABSTRACT

The presence of bombesin (gastrin-releasing peptide, GRP)-like immunoreactivity in mucosal endocrine cells of human fetal lung is well established. In this study we have investigated the localisation of pro-GRP mRNA and GRP gene products and compared the distribution and levels of extractable GRP-and C-terminal flanking peptide of human pro-GRP-like immunoreactivity in order to verify synthesis and to investigate their coexistence and molecular forms. Human fetal lungs (14 to 23 weeks gestation) were immunostained, and extracts were assayed using regionspecific antisera to pro-GRP. Additional antisera to chromogranin and protein gene product 9.5 (PGP 9.5) were used for immunostaining by the peroxidase anti-peroxidase technique and for double immunofluorescence staining using antisera raised in two species. Immunoreactivity for both bombesin (GRP) and flanking peptide was seen mainly in the same endocrine cells, but more cells were stained with antisera to flanking peptide than with antiserum to bombesin (GRP). In situ hybridisation showed that pro-GRP mRNA was present and thus synthesis of the peptides was taking place. Endocrine cells and nerve fibres were PGP 9.5-immunoreactive, and a subset of cells was immunoreactive for bombesin gene products. Radioimmunoassay and chromatography show that pro-GRP is present in both the uncleaved and cleaved forms, and, in agreement with immunocytochemistry results, that an excess of C-terminal peptide of pro-GRP is detectable. It is therefore concluded that GRP-like peptides and flanking peptide are co-local-ised in human pulmonary endocrine cells, but the latter is found in larger concentrations than free GRP. Thus GRP-like peptides may be secreted separately from the flanking peptide(s) of pro-GRP. Furthermore PGP 9.5 appears to be a useful marker for endocrine cells in the respiratory epithelium of human fetal lung. More... »

PAGES

299-307

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00495974

DOI

http://dx.doi.org/10.1007/bf00495974

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051418640

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/3068217


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27 schema:description The presence of bombesin (gastrin-releasing peptide, GRP)-like immunoreactivity in mucosal endocrine cells of human fetal lung is well established. In this study we have investigated the localisation of pro-GRP mRNA and GRP gene products and compared the distribution and levels of extractable GRP-and C-terminal flanking peptide of human pro-GRP-like immunoreactivity in order to verify synthesis and to investigate their coexistence and molecular forms. Human fetal lungs (14 to 23 weeks gestation) were immunostained, and extracts were assayed using regionspecific antisera to pro-GRP. Additional antisera to chromogranin and protein gene product 9.5 (PGP 9.5) were used for immunostaining by the peroxidase anti-peroxidase technique and for double immunofluorescence staining using antisera raised in two species. Immunoreactivity for both bombesin (GRP) and flanking peptide was seen mainly in the same endocrine cells, but more cells were stained with antisera to flanking peptide than with antiserum to bombesin (GRP). In situ hybridisation showed that pro-GRP mRNA was present and thus synthesis of the peptides was taking place. Endocrine cells and nerve fibres were PGP 9.5-immunoreactive, and a subset of cells was immunoreactive for bombesin gene products. Radioimmunoassay and chromatography show that pro-GRP is present in both the uncleaved and cleaved forms, and, in agreement with immunocytochemistry results, that an excess of C-terminal peptide of pro-GRP is detectable. It is therefore concluded that GRP-like peptides and flanking peptide are co-local-ised in human pulmonary endocrine cells, but the latter is found in larger concentrations than free GRP. Thus GRP-like peptides may be secreted separately from the flanking peptide(s) of pro-GRP. Furthermore PGP 9.5 appears to be a useful marker for endocrine cells in the respiratory epithelium of human fetal lung.
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34 schema:keywords Double immunofluorescence staining
35 GRP
36 GRP gene products
37 GRP-like peptides
38 Localisation of mRNA
39 PGP 9.5
40 PGP 9.5-immunoreactive
41 additional antisera
42 agreement
43 anti-peroxidase technique
44 antiserum
45 bombesin
46 bombesin gene products
47 cells
48 chromatography show
49 cleaved forms
50 coexistence
51 concentration
52 distribution
53 endocrine cells
54 epithelium
55 excess
56 extractable GRP
57 extracts
58 fetal human lung
59 fetal lung
60 fibers
61 flanking peptide
62 form
63 free GRP
64 gastrin-releasing peptide
65 gene product 9.5
66 gene products
67 human fetal lung
68 human lung
69 human pulmonary endocrine cells
70 hybridisation
71 immunocytochemistry results
72 immunofluorescence staining
73 immunoreactivity
74 large concentrations
75 levels
76 like immunoreactivity
77 localisation
78 lung
79 mRNA
80 markers
81 molecular forms
82 more cells
83 mucosal endocrine cells
84 nerve fibers
85 order
86 peptides
87 peroxidase anti-peroxidase technique
88 place
89 presence
90 presence of bombesin
91 pro-GRP mRNA
92 product 9.5
93 products
94 protein gene product 9.5
95 pulmonary endocrine cells
96 regionspecific antisera
97 respiratory epithelium
98 results
99 same endocrine cells
100 show
101 situ hybridisation
102 species
103 staining
104 study
105 subset
106 subset of cells
107 synthesis
108 technique
109 terminal flanking peptide
110 terminal peptide
111 useful marker
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