scholarly journals Effect of S-312, a New Calcium Channel Blocker, on the 1,4-Dihydropyridine Binding Sites in Porcine Basilar Blood Vessels and Rat Aortic Smooth Muscle Cells.

1991 ◽  
Vol 56 (3) ◽  
pp. 249-259 ◽  
Author(s):  
Shin-ichi Mihara ◽  
Masafumi Fujimoto
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Calcium Channel ◽  
Blood Vessels ◽  
Calcium Channel Blocker ◽  
Binding Sites ◽  
Channel Blocker ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle

Vasopressin and angiotensin II receptors in rat aortic smooth muscle cells in culture

1983 ◽  
Vol 244 (1) ◽  
pp. E72-E82 ◽  
Author(s):  
J. Penit ◽  
M. Faure ◽  
S. Jard
Keyword(s):  
Smooth Muscle ◽  
Angiotensin Ii ◽  
Smooth Muscle Cells ◽  
Binding Sites ◽  
Binding Capacity ◽  
Specific Binding ◽  
Muscle Cells ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
Specific Binding Sites

Rat aortic smooth muscle cells were isolated and maintained in primary culture. After 2-3 days, cells recovered their contractile phenotype and could be induced to contract in response to vasopressin and angiotensin II. Vasopressin- and angiotensin-specific binding sites were detected on these cells, using tritiated Lys8-vasopressin, Asn1-Val5-angiotensin II, and Sarc1-Ile8-angiotensin II. Vasopressin binding sites had Kd values of 30 and 12 nM for Lys8-and Arg8-vasopressin, respectively, and a maximal binding capacity of 25,000 sites/cell. They displayed several of the expected characteristics of vasopressin receptors involved in the vasopressor response in vivo. A highly significant correlation was found between the relative agonistic or antagonistic vasopressor potencies of a series of vasopressin structural analogues and their relative abilities to inhibit [3H]vasopressin binding to aortic smooth muscle cells. Specific binding sites for Asn1-Val5-angiotensin II and Sarc1-Ile8-angiotensin II had the following characteristics: Kd = 2.3 and 1.3 nM, respectively; maximal capacity: 50,000 sites/cell. Vasopressin and angiotensin did not modify the intracellular cyclic AMP content of aortic smooth muscle cells.

scholarly journals Heparin inhibits the binding of basic fibroblast growth factor to cultured human aortic smooth-muscle cells

1997 ◽  
Vol 326 (3) ◽  
pp. 661-668 ◽  
Author(s):  
Françoise BONO ◽  
Patrice RIGON ◽  
Isabelle LAMARCHE ◽  
Pierre SAVI ◽  
Véronique SALEL ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Growth Factor ◽  
Smooth Muscle Cells ◽  
Binding Sites ◽  
Muscle Cells ◽  
Platelet Factor ◽  
Protamine Sulphate ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
High Affinity

Basic fibroblast growth factor (bFGF) and its specific receptors have diverse roles on a variety of cell types, such as the induction of vascular smooth-muscle cell proliferation which contributes to restenosis after coronary balloon angioplasty. bFGF is also known to interact with heparan sulphate proteoglycans present on the cell surface or in the extracellular matrix. In this study, the binding of 125I-bFGF to human aortic smooth-muscle cells was investigated. 125I-bFGF binding to these cells was reversible and saturable. Scatchard analysis revealed the presence of two distinct binding sites: a high-affinity receptor (Kd = 38±7 pM; 1480±220 sites/cell) and a low-affinity non-saturable binding site (Kd= 8.0±2.0 nM). Pretreatment of the cells with heparinase resulted in a large reduction of 125I-bFGF binding to its low-affinity receptors, suggesting that they are heparin-like molecules. The specificity of the low- and high-affinity binding sites for bFGF was determined with acidic FGF, platelet-derived growth factor-BB and epidermal growth factor, which did not compete for 125I-bFGF binding. Expression of FGF receptor isoforms analysed by reverse transcriptase-PCR revealed the presence of only the type-1 receptor. Binding to low-affinity binding sites was antagonized by heparin, suramin, protamine sulphate and platelet factor 4. Unexpectedly, these molecules also reduced the binding of 125I-bFGF to its high-affinity sites. Consistent with these results, heparin, suramin, protamine sulphate and platelet factor 4 inhibited bFGF-induced proliferation of human aortic smooth-muscle cells. Heparin abrogated bFGF-induced release of tissue-type plasminogen activator by these cells. These observations suggest that the interaction of bFGF with human aortic smooth-muscle cells is different from that described for other cells such as endothelial cells, in which heparin acts as a potentiating factor of the mitogenic activity of bFGF.

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