Role of Peg and Socket Junctions in Stretch Coupling in Intestinal Smooth Muscle

2011 ◽  
Vol 294 (6) ◽  
pp. 929-930
Author(s):  
M. Jimenez
2001 ◽  
Vol 120 (5) ◽  
pp. A534-A534
Author(s):  
A ZHAO ◽  
D MULLOY ◽  
J URBANJR ◽  
W GAUSE ◽  
T SHEADONOHUE

2001 ◽  
Vol 120 (5) ◽  
pp. A534 ◽  
Author(s):  
Aiping Zhao ◽  
Daniel P. Mulloy ◽  
Joseph F. Urban ◽  
William C. Gause ◽  
Terez Shea-Donohue

2012 ◽  
Vol 142 (5) ◽  
pp. S-497
Author(s):  
Karen S. Uray ◽  
Elizabeth Dial ◽  
Tri M. Phan ◽  
Lenard M. Lichtenberger

2000 ◽  
Vol 118 (2) ◽  
pp. 316-327 ◽  
Author(s):  
Jörg C. Kalff ◽  
Wolfgang H. Schraut ◽  
Timothy R. Billiar ◽  
Richard L. Simmons ◽  
Anthony J. Bauer

1983 ◽  
Vol 61 (5) ◽  
pp. 535-538 ◽  
Author(s):  
G. T. Bolger ◽  
C. R. Triggle ◽  
D. J. Triggle

The ionophore ionomycin produced concentration-dependent (5 × 10−9 to 5 × 10−6 M) contractions in guinea-pig ileal longitudinal smooth muscle. Responses were dependent on extracellular Ca2+, consistent with the known role of this Ca2+ source in supporting excitation–contraction coupling to a variety of stimulants in this tissue. Responses were insensitive to atropine (10−6 M) but were dependent upon extracellular Na+ and were completely blocked by low concentrations of the Ca2+-channel antagonists nicardipine. YC-93 (5 × 10−7 M), and D-600 (5 × 10−6 M). The behaviour of ionomycin is very similar to that shown by A 23187 in this tissue. Ionomycin, like A 23187, can apparently activate D-600 sensitive Ca2+ channels in the guinea-pig intestinal smooth muscle rather than simply translocating Ca2+EXT.


2000 ◽  
Vol 279 (5) ◽  
pp. G975-G982 ◽  
Author(s):  
John F. Kuemmerle ◽  
Baiqin Teng

Human intestinal smooth muscle cells in culture produce insulin-like growth factor-I (IGF-I), IGF binding protein-3 (IGFBP-3), IGFBP-4, and IGFBP-5, which can modulate the effects of IGF-I on growth. This study examined the role of IGFBP-4 on IGF-I-induced growth and the mechanisms regulating IGFBP-4 levels. IGFBP-4 inhibited IGF-I-induced [3H]thymidine incorporation. IGFBP-4 mRNA levels were not altered by IGF-I. IGF-I caused a concentration-dependent activation of an endogenous IGFBP-4 protease, resulting in time-dependent degradation of intact IGFBP-4 into inactive fragments. Protease activity was measured in a cell-free assay using smooth muscle cell conditioned medium containing the IGFBP-4 protease. The protease was inhibited by EDTA and benzamidine. Protease activity was highest in proliferating cells and lowest in postconfluent cells. The role of endogenous IGF-I in regulating IGFBP-4 degradation was confirmed by the ability of an IGF-I antagonist to inhibit IGF-I-activated IGFBP-4 proteolysis in intact cells. We conclude that in human intestinal smooth muscle cells levels of secreted IGFBP-4 are determined by the confluence-dependent production of a cation-dependent serine protease that is activated by endogenous IGF-I.


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