Insulin-like growth factor-I (IGF-I) and its binding protein IGFBP-4 in human prostatic hyperplastic tissue: gene expression and its cellular localization.

1994 ◽  
Vol 78 (3) ◽  
pp. 778-783
Author(s):  
T Barni ◽  
B G Vannelli ◽  
R Sadri ◽  
C Pupilli ◽  
P Ghiandi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Growth Factor ◽  
Cellular Localization ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Hyperplastic Tissue ◽  
Growth Factor I ◽  
Tissue Gene Expression

Colocalization of insulin-like growth factor-binding protein with insulin-like growth factor I

1991 ◽  
Vol 261 (1) ◽  
pp. F22-F28 ◽  
Author(s):  
S. Kobayashi ◽  
D. R. Clemmons ◽  
M. A. Venkatachalam
Keyword(s):  
Growth Factor ◽  
Cultured Cells ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Intense Staining ◽  
Factor Binding ◽  
Factor I ◽  
Collecting Ducts ◽  
Igf I ◽  
Growth Factor I

We report the localization of insulin-like growth factor I (IGF-I) and a 25-kDa form of insulin-like growth factor-binding protein (IGF-BP-1) in adult rat kidney. The antigens were localized using a rabbit anti-human IGF-I antibody, and a rabbit anti-human IGF-BP-1 antibody raised against human 25-kDa IGF-BP-1 purified from amniotic fluid. Immunohistochemistry by the avidin-biotin peroxidase conjugate technique showed that both peptides are located in the same nephron segments, in the same cell types. The most intense staining was in papillary collecting ducts. There was moderate staining also in cortical collecting ducts and medullary thick ascending limbs of Henle's loop. In collecting ducts the antigens were shown to be present in principal cells but not in intercalated cells. In distal convoluted tubules, cortical thick ascending limbs, and in structures presumptively identified as thin limbs of Henle's loops there was only modest staining. The macula densa, however, lacked immunoreactivity. Colocalization of IGF-I and IGF-BP-1 in the same cells supports the notion, derived from studies on cultured cells, that the actions of IGF-I may be modified by IGF-BPs that are present in the same location.

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