scholarly journals Insulin-Like Growth Factor Binding Protein 3 Has Opposing Actions on Malignant and Nonmalignant Breast Epithelial Cells that Are Each Reversible and Dependent upon Cholesterol-Stabilized Integrin Receptor Complexes

Endocrinology ◽  
2006 ◽  
Vol 147 (7) ◽  
pp. 3484-3500 ◽  
Author(s):  
C. Burrows ◽  
J. M. P. Holly ◽  
N. J. Laurence ◽  
E. G. Vernon ◽  
J. V. Carter ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Integrin Receptor ◽  
Breast Epithelial Cells ◽  
Factor Binding ◽  
Receptor Complexes ◽  
Breast Epithelial

Insulin-like growth factor-binding protein-3 expression and secretion by cultures of human prostate epithelial cells and stromal fibroblasts

1994 ◽  
Vol 141 (3) ◽  
pp. 535-540 ◽  
Author(s):  
R S Birnbaum ◽  
J L Ware ◽  
S R Plymate
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Conditioned Medium ◽  
Binding Protein ◽  
Human Prostate ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Cell Extracts ◽  
Prostate Epithelial Cells ◽  
Igfbp 3

Abstract Prostate-specific antigen (PSA) was recently shown to be an insulin-like growth factor-binding protein (IGFBP)-3 protease. However, only IGFBPs-2 and -4 have been identified in conditioned medium of prostate epithelial cells. Using cultures of human prostate epithelial and stromal fibroblastic cells, we examined conditioned medium and cell extracts for evidence of IGFBP-3 expression and secretion. Western ligand blotting of conditioned medium from epithelial or stromal cultures revealed the presence of IGFBPs in the molecular weight range 36–48 kDa, suggestive of IGFBP-3. Western immunoblots of these media confirmed the presence of IGFBP-3. Northern analyses of extracts of both stromal and epithelial cells showed a 2·5 kb band, the size of IGFBP-3 mRNA. We conclude that prostate cells express IGFBP-3 and that local proteolysis by PSA could modify this binding protein's actions in the prostate. Journal of Endocrinology (1994) 141, 535–540

scholarly journals Citrullination regulates the expression of insulin-like growth factor-binding protein 1 (IGFBP1) in ovine uterine luminal epithelial cells

Reproduction ◽  
2017 ◽  
Vol 153 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Coleman H Young ◽  
Heather M Rothfuss ◽  
Philip F Gard ◽  
Aaron Muth ◽  
Paul R Thompson ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Cross Sections ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Histone H4 ◽  
Uterine Epithelial Cells ◽  
Factor Binding ◽  
Arginine Residues ◽  
Histone Citrullination

There are five peptidylarginine deiminase (PAD) isozymes designated as PADs 1, 2, 3, 4 and 6, and many are expressed in female reproductive tissues. These enzymes post-translationally convert positively charged arginine amino acids into neutral citrulline residues. Targets for PAD-catalyzed citrullination include arginine residues on histone tails, which results in chromatin decondensation and changes in gene expression. Some of the first studies examining PADs found that they are localized to rodent uterine epithelial cells. Despite these findings, the function of PAD-catalyzed citrullination in uterine epithelial cells is still unknown. To address this, we first examined PAD expression in uterine cross-sections from pregnant ewes on gestation day 25 (d25). Immunohistochemistry revealed that the levels of PADs 2 and 4 are robust in luminal and glandular epithelia compared with those of PADs 1 and 3. As PADs 2 and 4 have well-characterized roles in histone citrullination, we next hypothesized that PADs citrullinate histones in these uterine cells. Examination of caruncle lysates from pregnant ewes on gestation d25 and an ovine luminal epithelial (OLE) cell line shows that histone H3 arginine residues 2, 8, 17 and 26 are citrullinated, but histone H4 arginine 3 is not. Using a pan-PAD inhibitor, we next attenuated histone citrullination in OLE cells, which resulted in a significant decrease in the expression of insulin-like growth factor-binding protein 1 (IGFBP1) mRNA. As IGFBP1 is important for the migration and attachment of the trophectoderm to uterine endometrium, our results suggest that PAD-catalyzed citrullination may be an important post-translational mechanism for the establishment of pregnancy in ewes.

Sign in / Sign up

Export Citation Format

Share Document