Expression and localization of transforming growth factor-beta receptors type I and type II in the rat ventral prostate during regression

1996 ◽  
Vol 10 (1) ◽  
pp. 107-115 ◽  
Author(s):  
I. Y. Kim
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Ventral Prostate ◽  
Type I ◽  
Type Ii ◽  
Rat Ventral Prostate ◽  
Beta Receptors ◽  
Growth Factor Beta

scholarly journals Formation of hetero-oligomeric complexes of type I and type II receptors for transforming growth factor-beta.

1994 ◽  
Vol 269 (31) ◽  
pp. 20172-20178 ◽  
Author(s):  
H. Yamashita ◽  
P. ten Dijke ◽  
P. Franzén ◽  
K. Miyazono ◽  
C.H. Heldin
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Type I ◽  
Type Ii ◽  
Growth Factor Beta

scholarly journals The types II and III transforming growth factor-beta receptors form homo-oligomers.

1994 ◽  
Vol 126 (1) ◽  
pp. 139-154 ◽  
Author(s):  
Y I Henis ◽  
A Moustakas ◽  
H Y Lin ◽  
H F Lodish
Keyword(s):  
Growth Factor ◽  
Cell Surface ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Type Ii ◽  
Tgf Beta ◽  
Double Labeling ◽  
Beta Receptors ◽  
Growth Factor Beta ◽  
In Cells

Affinity-labeling experiments have detected hetero-oligomers of the types I, II, and III transforming growth factor beta (TGF-beta) receptors which mediate intracellular signaling by TGF-beta, but the oligomeric state of the individual receptor types remains unknown. Here we use two types of experiments to show that a major portion of the receptor types II and III forms homo-oligomers both in the absence and presence of TGF-beta. Both experiments used COS-7 cells co-transfected with combinations of these receptors carrying different epitope tags at their extracellular termini. In immunoprecipitation experiments, radiolabeled TGF-beta was bound and cross-linked to cells co-expressing two differently tagged type II receptors. Sequential immunoprecipitations using anti-epitope monoclonal antibodies showed that type II TGF-beta receptors form homo-oligomers. In cells co-expressing epitope-tagged types II and III receptors, a low level of co-precipitation of the ligand-labeled receptors was observed, indicating that some hetero-oligomers of the types II and III receptors exist in the presence of ligand. Antibody-mediated cross-linking studies based on double-labeling immunofluorescence explored co-patching of the receptors at the cell surface on live cells. In cells co-expressing two differently tagged type II receptors or two differently tagged type III receptors, forcing one receptor into micropatches by IgG induced co-patching of the receptor carrying the other tag, labeled by noncross-linking monovalent Fab'. These studies showed that homo-oligomers of the types II and III receptors exist on the cell surface in the absence or presence of TGF-beta 1 or -beta 2. In cells co-expressing types II and III receptors, the amount of heterocomplexes at the cell surface was too low to be detected in the immunofluorescence co-patching experiments, confirming that hetero-oligomers of the types II and III receptors are minor and probably transient species.

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