scholarly journals Physiological Modulation of Intestinal Motility by Enteric Dopaminergic Neurons and the D2 Receptor: Analysis of Dopamine Receptor Expression, Location, Development, and Function in Wild-Type and Knock-Out Mice

2006 ◽  
Vol 26 (10) ◽  
pp. 2798-2807 ◽  
Author(s):  
Z. S. Li
2016 ◽  
Vol 62 ◽  
pp. 1-10 ◽  
Author(s):  
Ariane Scoumanne ◽  
Patricia Molina-Ortiz ◽  
Daniel Monteyne ◽  
David Perez-Morga ◽  
Christophe Erneux ◽  
...  

Life Sciences ◽  
1997 ◽  
Vol 60 (13-14) ◽  
pp. 1101-1104 ◽  
Author(s):  
Lise A. McKinnon ◽  
Marc Rosoff ◽  
Susan E. Hamilton ◽  
Michael L. Schlador ◽  
Sarabeth L. Thomas ◽  
...  

2004 ◽  
Vol 89 (4) ◽  
pp. 1674-1683 ◽  
Author(s):  
Rosario Pivonello ◽  
Carmela Matrone ◽  
Mariagiovanna Filippella ◽  
Luigi M. Cavallo ◽  
Carolina Di Somma ◽  
...  

Abstract The aim of this study was to correlate dopamine receptors and D2 isoform expression with the cabergoline effect on α-subunit secretion in vitro and tumor mass in vivo in clinically nonfunctioning pituitary tumors. Eighteen patients were subjected to neurosurgery, and a tumor sample was used for dopamine receptor and D2 isoform expression evaluation by RT-PCR and the in vitro functional studies. After neurosurgery, nine of 18 patients with persistent tumor were treated with cabergoline and tumor mass was evaluated before and after 1 yr treatment. D2 receptor was expressed in 67% of cases. D2long was found in 50%, D2short in 17%, and both D2 isoforms in 33% of cases. D4 receptor was also expressed in 17% of cases. The in vitro inhibition of α-subunit concentration was found in 56% of cases and was associated with D2 expression (χ2 = 5.6; P < 0.05). After 1 yr of cabergoline treatment, tumor shrinkage was evident in 56% of patients and was associated with D2 expression (χ2 = 5.6; P < 0.05). The expression of D2short rather than D2long isoform is associated with the most favorable response of the tumor to cabergoline treatment. In conclusion, this study demonstrates D2 receptor expression and function in nearly 70% of cases, suggesting a role of this drug in the treatment schedule of clinically nonfunctioning pituitary tumors.


Endocrinology ◽  
2010 ◽  
Vol 152 (2) ◽  
pp. 718-729 ◽  
Author(s):  
Laura O'Hara ◽  
Michelle Welsh ◽  
Philippa T.K. Saunders ◽  
Lee B. Smith

Abstract The epididymis plays an essential role in male fertility, and disruption of epididymal function can lead to obstructive azoospermia. Formation and function of the epididymis is androgen-dependent. The androgen receptor (AR) is expressed in both the stromal and epithelial compartments of the epididymis, and androgen action mediated via stromal cells is vital for its normal development and function. However the impact of epithelial specific AR-dependent signaling in the epididymis remains underexplored. To address this, we used conditional gene-targeting in mice to selectively ablate AR from the caput epididymal epithelium, and characterized the resulting phenotype at multiple postnatal ages. Caput epithelium androgen receptor knock-out mice have normal serum testosterone concentrations at day (d) 21 and d100, but do not develop an epididymal initial segment. The remaining caput epithelium displays a significant decrease in epithelial cell height from d11 and lumen diameter from d21 and disruption of the smooth muscle layer of the caput epididymis at d100. From d21, caput epithelium androgen receptor knock-out mice accumulate cell debris, proteinaceous material, and, at later ages, spermatozoa in their efferent ducts, which prevents normal passage of spermatozoa from the testis into the cauda epididymis resulting in infertility when tested at d100. This efferent duct obstruction leads to fluid back-pressure and disruption of the seminiferous epithelium of the adult testis. We conclude that epithelial AR signaling is essential for postnatal development and function of the epididymal epithelium and that disruption of this signaling can contribute to obstructive azoospermia.


2007 ◽  
Vol 45 (05) ◽  
Author(s):  
A Schnur ◽  
P Hegyi ◽  
V Venglovecz ◽  
Z Rakonczay ◽  
I Ignáth ◽  
...  

2017 ◽  
Vol 94 (3) ◽  
pp. 93-99
Author(s):  
Tetsu HAYAKAWA ◽  
Masaki HATA ◽  
Sachi KUWAHARA-OTANI ◽  
Hideshi YAGI ◽  
Haruki OKAMURA

1997 ◽  
Vol 110 (22) ◽  
pp. 2855-2860 ◽  
Author(s):  
J.M. Verbavatz ◽  
T. Ma ◽  
R. Gobin ◽  
A.S. Verkman

Freeze-fracture electron microscopy (FFEM) of kidney collecting duct, muscle, astrocytes in brain, and other mammalian tissues has revealed regular square arrays of intramembrane particles called orthogonal arrays of particles (OAPs). Their possible role in membrane structure and transport have been proposed, and their absence or decrease has been noted in a variety of hereditary and acquired diseases. A transgenic mouse lacking water channel AQP4 was used to show that AQP4 is the OAP protein. FFEM was done on kidney, skeletal muscle, and brain from AQP4 wild-type [+/+], heterozygous [+/−] and knock-out [-/-] mice. The [-/-] mice did not express detectable AQP4 protein, but were grossly indistinguishable from [+/+] mice. FFEM was done on blinded samples of kidney, brain and muscle from 9 mice. In all 6 kidney samples from [+/+] and [+/−] mice, OAPs similar to those in AQP4-transfected CHO cells were found in basolateral membranes of collecting duct principal cells. In all muscle and brain samples from [+/+] and [+/−] mice, OAPs of identical ultrastructure to those in kidney were seen, but in smaller patch sizes. OAPs were not seen in any sample from [-/-] mice. Label-fracture analysis using a peptide-derived AQP4 polyclonal antibody showed immunogold labeling of OAPs in AQP4-expressing CHO cells. These studies provide direct evidence that AQP4 is required for formation of OAPs and is a component of OAPs, thus establishing the identity and function of OAPs.


Sign in / Sign up

Export Citation Format

Share Document