Cellular localization of lectin-affinity in tissue sections of normal human duodenum

1983 ◽  
Vol 402 (1) ◽  
pp. 1-9 ◽  
Author(s):  
K. Wurster ◽  
P. Peschke ◽  
W. D. Kuhlmann
1985 ◽  
Vol 52 (3) ◽  
pp. 249-252 ◽  
Author(s):  
J. P. Gorvel ◽  
J. Sarles ◽  
S. Maroux ◽  
D. Olive ◽  
C. Mawas

1994 ◽  
Vol 143 (1) ◽  
pp. 127-137 ◽  
Author(s):  
T-A Jaatinen ◽  
T-L Penttilä ◽  
A Kaipia ◽  
T Ekfors ◽  
M Parvinen ◽  
...  

Abstract We studied the cellular distribution of inhibin α, βA and βB mRNAs in the normal human ovary and in polycystic ovarian syndrome (PCOS) by in situ hybridization. Our results show that human granulosa cells express inhibin α, βA and βB subunit mRNAs, and theca cells express inhibin α and βA subunit mRNAs. The co-localization of α and βA mRNAs in theca cells supports the hypothesis that inhibin also has an autocrine function in these cells. We did not detect any inhibin subunit mRNA in the granulosa cells of atretic follicles, while theca cells also expressed α subunit mRNA in those follicles. The present findings suggest that the expression of inhibin subunits is regulated differently in human follicular granulosa and theca cells. It has been speculated that inhibin may be involved in the development of PCOS. Our results show that the cellular localization of inhibin subunit mRNAs is not disturbed in PCOS ovaries. Journal of Endocrinology (1994) 143, 127–137


1992 ◽  
Vol 23 (6) ◽  
pp. 686-694 ◽  
Author(s):  
Sung Sik Shin ◽  
Khalil Sheibani ◽  
Janice Kezirian ◽  
Auayporn Nademanee ◽  
Stephen J. Forman ◽  
...  

1987 ◽  
Vol 84 (21) ◽  
pp. 7735-7738 ◽  
Author(s):  
F. Thiebaut ◽  
T. Tsuruo ◽  
H. Hamada ◽  
M. M. Gottesman ◽  
I. Pastan ◽  
...  

1995 ◽  
Vol 26 ◽  
pp. S104-106
Author(s):  
Uberto Pagotto ◽  
Thomas Arzberger ◽  
Ursula Hopfner ◽  
Adolf Weindl ◽  
Günter K. Stalla

1998 ◽  
Vol 46 (2) ◽  
pp. 157-164 ◽  
Author(s):  
Michael R. D'Andrea ◽  
Claudia K. Derian ◽  
Didier Leturcq ◽  
Sherry M. Baker ◽  
Anders Brunmark ◽  
...  

PAR-2 is a second member of a novel family of G-protein-coupled receptors characterized by a proteolytic cleavage of the amino terminus, thus exposing a tethered peptide ligand that autoactivates the receptor. The physiological and/or pathological role(s) of PAR-2 are still unknown. This study provides tissue-specific cellular localization of PAR-2 in normal human tissues by immunohistochemical techniques. A polyclonal antibody, PAR-2C, was raised against a peptide corresponding to the amino terminal sequence SLIGKVDGTSHVTGKGV of human PAR-2. Significant PAR-2 immunoreactivity was detected in smooth muscle of vascular and nonvascular origin and stromal cells from a variety of tissues. PAR-2 was also present in endothelial and epithelial cells independent of tissue type. Strong immunolabeling was observed throughout the gastrointestinal tract, indicating a possible function for PAR-2 in this system. In the CNS, PAR-2 was localized to many astrocytes and neurons, suggesting involvement of PAR-2 in neuronal function. A role for PAR-2 in the skin was further supported by its immunolocalization in the epidermis. PAR-2C antibody exemplifies an important tool to address the physiological role(s) of PAR-2.


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