Direct Interaction of Guinea Pig Eosinophils and Adrenergic Agents

1985 ◽  
Vol 78 (3) ◽  
pp. 243-248 ◽  
Author(s):  
Keisuke Masuyama ◽  
Takeru Ishikawa
1981 ◽  
Vol 31 ◽  
pp. 228
Author(s):  
Kayoko Yamamoto ◽  
Ikuo Maruyama ◽  
Tetsuya Kamimura ◽  
Hisayuki Ohata ◽  
Shigeo Yamada
Keyword(s):  

1988 ◽  
Vol 251 (1) ◽  
pp. 189-194 ◽  
Author(s):  
G Jakab ◽  
S T Rapundalo ◽  
R J Solaro ◽  
E G Kranias

Phosphorylation of phospholipids was studied in Langendorff perfused guinea pig hearts subjected to beta-adrenergic stimulation. Hearts were perfused with Krebs-Henseleit buffer containing [32P]Pi and freeze-clamped in a control condition or at the peak of the inotropic response to isoprenaline. 32P incorporation into total phospholipids, individual phospholipids and polyphosphoinositides was analysed in whole tissue homogenates and membranes, enriched in sarcoplasmic reticulum, prepared from the same hearts. Isoprenaline stimulation of the hearts did not result in any significant changes in the levels of phosphate incorporation in the total phospholipid present in cardiac homogenates (11.6 +/- 0.4 nmol of 32P/g for control hearts and 12.4 +/- 0.5 nmol of 32P/g for isoprenaline-treated hearts; n = 6), although there was a significant increase in the degree of phospholipid phosphorylation in sarcoplasmic reticulum (3.5 +/- 0.3 nmol of 32P/mg for control hearts and 6.7 +/- 0.2 nmol of 32P/mg for isoprenaline-treated hearts; n = 6). Analysis of 32P incorporation into individual phospholipids and polyphosphoinositides revealed that isoprenaline stimulation of the hearts was associated with a 2-3-fold increase in the degree of phosphorylation of phosphatidylinositol monophosphate and bisphosphate as well as phosphatidic acid in both cardiac homogenates and sarcoplasmic reticulum membranes. In addition, there was increased phosphate incorporation into phosphatidylinositol in sarcoplasmic reticulum membranes. Thus, perfusion of guinea pig hearts with isoprenaline is associated with increased formation of polyphosphoinositides and these phospholipids may be involved, at least in part, in mediating the effects of beta-adrenergic agents in the mammalian heart.


Reproduction ◽  
2014 ◽  
Vol 148 (6) ◽  
pp. 623-634 ◽  
Author(s):  
Karina Pastén ◽  
Yadira Bastian ◽  
Ana L Roa-Espitia ◽  
Deneb Maldonado-García ◽  
Guillermo Mendoza-Hernández ◽  
...  

Mammalian fertilization is completed by direct interaction between sperm and egg. This process is primarily mediated by both adhesion and membrane-fusion proteins found on the gamete surface. ADAM1, 2, and 3 are members of the ADAMs protein family, and have been involved in sperm–egg binding. In this study, we demonstrate the proteolytic processing of ADAM15 during epididymal maturation of guinea pig spermatozoa to produce a mature form a size of 45 kDa. We find that the size of the mature ADAM15, 45 kDa, in cauda epididymal spermatozoa indicates that the pro-domain and metalloprotease domain are absent. In addition, using indirect immunofluorescence, ADAM15 was found throughout the acrosome, at the equatorial region and along the flagellum of guinea pig spermatozoa. After acrosome reaction, ADAM15 is lost from the acrosomal region and retained in the equatorial region and flagellum. In this study, we also report the first evidence of a complex between ADAM15 and acrogranin. By immunoprecipitation, we detected a protein band of 65 kDa which co-immunoprecipated together ADAM15. Analysis of the N-terminal sequence of this 65 kDa protein has revealed its identity as acrogranin. In addition, using cell-surface labeling, ADAM15 was found to be present on the cell surface. Assays of heterologous fertilization showed that the antibody against acrogranin inhibited the sperm–egg adhesion. Interestingly, ADAM15 and acrogranin were also found associated in two breast cancer cell lines. In conclusion, our results demonstrated that ADAM15 and acrogranin are present on and associated with the surface of guinea pig spermatozoa; besides both proteins may play a role during sperm–egg binding.


1962 ◽  
Vol 202 (5) ◽  
pp. 841-844 ◽  
Author(s):  
Philip A. Khairallah ◽  
Irvine H. Page

Evidence has been presented previously indicating that angiotensin acts indirectly on guinea pig intestines by stimulating the ganglion cells of Auerbach's plexus. Further studies have shown that the adrenergic nerves are not directly involved in this mechanism, although adrenergic blocking agents suppress the response to angiotensin, probably by acting directly on the cell membrane. Epinephrine, and to a lesser extent norepinephrine and isoproterenol, inhibited the contraction of ileum and uterus to angiotensin, and to electrical stimulation, possibly by reversing or blocking sodium or potassium ion flux across the cell membrane resulting from the action of the peptide. Most of the adrenergic blocking agents studied, with the exception of Dibenamine, also inhibited the response to angiotensin. Reserpine, guanethidine, and bretylium block its action, possibly by releasing catecholamines from bound tissue stores, and phentolamine and piperoxane, by their sympathetic actions imitating the catecholamines.


1980 ◽  
Vol 58 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Robert L. Rodgers ◽  
Thomas E. Tenner Jr. ◽  
Ismail E. Laher ◽  
John H. McNeill

Clonidine was administered to isolated guinea pig right atria in order to characterize its chronotropic activity and its interaction with other chronotropic agents at the postjunctional level. Clonidine either had no significant effect (10−7–10−4 M) or decreased (10−3 M) atrial rate. Pretreatment of the atria with clonidine noncompetitively antagonized (10−6–10−4 M) the positive chronotropic actions of isoproterenol, and competitively antagonized (10−4 M) the negative chronotropic actions of pilocarpine. At doses of 10−6 or 3 × 10−6 M, clonidine also noncompetitively antagonized the positive chronotropic effects of 4-methylhistamine and glucagon. The results show that clonidine antagonizes both adrenergic and cholinergic influences on atrial rate at the postjunctional level and suggest that the antagonism of adrenergic influences does not involve a direct interaction with β-adrenergic receptors.


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