Role of ?-aminobutyric acid (GABA) in the extrapyramidal motor system 1. Regional distribution of GABA in rabbit, rat, guinea pig and baboon CNS

1971 ◽  
Vol 13 (5) ◽  
Author(s):  
Y. Okada ◽  
C. Nitsch-Hassler ◽  
J.S. Kim ◽  
I.J. Bak ◽  
R. Hassler
Keyword(s):  
Guinea Pig ◽  
Motor System ◽  
Regional Distribution ◽  
Aminobutyric Acid ◽  
System 1 ◽  
Extrapyramidal Motor

Role of ?-aminobutyric acid (GABA) in the extrapyramidal motor system

1971 ◽  
Vol 14 (1) ◽  
Author(s):  
J.S. Kim ◽  
I.J. Bak ◽  
R. Hassler ◽  
Y. Okada
Keyword(s):  
Motor System ◽  
Aminobutyric Acid ◽  
Extrapyramidal Motor

Uptake and release of gamma-aminobutyric acid in guinea pig gallbladder

1985 ◽  
Vol 249 (2) ◽  
pp. G192-G196 ◽  
Author(s):  
N. Saito ◽  
K. Taniyama ◽  
C. Tanaka
Keyword(s):  
Guinea Pig ◽  
Ganglion Cells ◽  
Regional Distribution ◽  
Gaba Release ◽  
Aminobutyric Acid ◽  
Transport Systems ◽  
Gamma Aminobutyric Acid ◽  
Beta Alanine ◽  
High Affinity ◽  
Uptake And Release

The presence of gamma-aminobutyric acid (GABA)-ergic neuron in guinea pig gallbladder was investigated by measuring GABA contents and glutamate decarboxylase (GAD) activity and by demonstrating the uptake and release of [3H]GABA. GABA and GAD are both present in the gallbladder, and a positive correlation in regional distribution was observed among GABA, GAD, and the number of ganglion cells. The uptake of [3H]GABA by the gallbladder showed two saturable components; a high-affinity component (Km = 23.3 microM, Vmax = 7.63 nmol X g-1 X 10 min-1) and a low-affinity component (Km = 515 microM, Vmax = 57.1 nmol X g-1 X 10 min-1). These high-affinity and low-affinity transport systems corresponded to those obtained in the presence of beta-alanine and L-2,4-diaminobutyric acid, respectively, thereby suggesting the presence of neuronal and nonneuronal GABA transport systems in this tissue. Electrical transmural stimulation produced an increase in [3H]-GABA release from the isolated gallbladder preloaded with [3H]GABA, in the presence of beta-alanine. The stimulation-evoked release of [3H]GABA was prevented by calcium-free medium containing 1 mM EGTA and tetrodotoxin, thereby indicating that the released GABA originates from the nerve terminals. These results provide evidence for the presence of GABA-ergic neurons in the guinea pig gallbladder.

Studies of Vegetative Plant Tissue Compatibility/Incompatibility: The Role of Acid Phosphatase in Lethal Cell Senescence in an Incompatible Heterograft

1980 ◽  
Vol 38 ◽  
pp. 530-531
Author(s):  
Randy Moore
Keyword(s):  
Acid Phosphatase ◽  
Thick Layer ◽  
Cell Necrosis ◽  
Enzyme Localization ◽  
Vegetative Plant ◽  
Cell Autolysis ◽  
Graft Interface ◽  
System 1 ◽  
Thin Fibril

Previous work has indicated that the graft incompatihility between Sedrmi telephoides and Solanum pennellil involves cell necrosis that results In a thick layer of collapsed cells at the graft Interface. This necrotic layer insulates the stock from the scion, which results in abscission of the Sedum scion after 4-6 weeks due to desiccation and starvation. Thus, cell autolysis (which is restricted to Sedum) characterizes the Incompatibility response in this system (1). In order to elucidate the events that lead to cell autolysis, and thus better understand the cellular site and mode of action of cellular incompatibility, the appearance and fate of the hydrolytlc enzyme acid phosphatase (AP) was followed in both the compatible Sedum autograft and the incompatible Sedum/Solanum heterograft. Acid phosphatase was localized by a modified Gomori-type reaction; positive (i.e., including NaF inhibitor) and negative (lacking substrate) controls showed no enzymatic precipitate. Following an initial association with the endoplasmic reticulum (ER) and dictyosomes at 6-10 hours after grafting, AP activity in the compatible Sedum autograft is associated primarily with the plasmalemma (Fig. 1). By 18-24 hours after grafting, the AP activity is restricted to the tono-plast and vacuole (Fig. 2). This strict compartmentation and absence of enzyme from the cytosol is maintained throughout the development of the compatible graft. While AP activity in the incompatible Sedum/Solanum heterograft is Initially similar to the compatible Sedum autograft (i.e., initially found on the ER and dictyosomes), there is a marked difference in enzyme localization in the two graft partners as the incompatibility response develops. As in the compatible autograft, Solanum cells at the graft interface show an Increase in AP activity that Is restricted to the vacuole and tonoplast, with little or no enzyme activity in the cytosol (Fig. 3). In comparable Sedum cells, however, there is a dramatic Increase In AP activity in the cytosol (Fig. h); this cytosollc AP activity is associated with thin fibril-like structures (Fig. 5) measuring approximately 60 A in diameter. This high cytoplasmic AP activity In Sedum cells results in cell autolysis, death, and eventual cell collapse to form the characteristic necrotic layer separating the two graft partners.

scholarly journals Role of chloride channels in bradykinin-induced guinea pig airway vagal C-fibre activation

2005 ◽  
Vol 566 (1) ◽  
pp. 205-212 ◽  
Author(s):  
Min-Goo Lee ◽  
Donald W. MacGlashan ◽  
Bradley J. Undem
Keyword(s):  
Guinea Pig ◽  
Chloride Channels ◽  
C Fibre
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