scholarly journals A-type gamma-aminobutyric acid receptor (gabaar) and glutamic acid decarboxylase (gad) in type ii pneumocytes

2006 ◽  
Vol 53 (1) ◽  
pp. 26167-26167
Author(s):  
Wei-Yang Lu ◽  
Yun-Yan Xiang ◽  
William Ju ◽  
Mingyao Liu ◽  
Beverley Orser
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Aminobutyric Acid ◽  
Acid Decarboxylase ◽  
Type Ii ◽  
Gamma Aminobutyric Acid ◽  
Acid Receptor ◽  
Type Ii Pneumocytes

Gamma-aminobutyric acid- and glutamic acid decarboxylase-immunoreactive neurons in the retina of different vertebrates

1987 ◽  
Vol 258 (4) ◽  
pp. 622-630 ◽  
Author(s):  
E. Agardh ◽  
A. Bruun ◽  
B. Ehinger ◽  
P. Ekström ◽  
T. van Veen ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Aminobutyric Acid ◽  
Acid Decarboxylase ◽  
Gamma Aminobutyric Acid

scholarly journals Action of Phenylalanine Metabolites on Glutamic Acid Decarboxylase and gamma-Aminobutyric Acid---alpha-Ketoglutaric Acid Transaminase in Brain.

1959 ◽  
Vol 13 ◽  
pp. 1366-1374 ◽  
Author(s):  
Arne Hanson ◽  
Salo Gronowitz ◽  
Sigvard Eriksson ◽  
C.-G. Hedén ◽  
B. Malmgren ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Aminobutyric Acid ◽  
Acid Decarboxylase ◽  
Gamma Aminobutyric Acid

Stiff-person syndrome with acute recurrent peripheral vertigo: possible evidence of gamma aminobutyric acid as a neurotransmitter in the vestibular periphery

2007 ◽  
Vol 122 (6) ◽  
pp. 636-638 ◽  
Author(s):  
R Teggi ◽  
L O Piccioni ◽  
G Martino ◽  
C Bellini ◽  
M Bussi
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Aminobutyric Acid ◽  
Acid Decarboxylase ◽  
Stiff Person Syndrome ◽  
Gamma Aminobutyric Acid ◽  
Vestibular Damage ◽  
Peripheral Vertigo

AbstractObjective:We report a case of a 58-year-old man suffering from stiff-person syndrome and recurrent peripheral vertigo.Method:A case report and a review of the recent literature on stiff-person syndrome are presented.Results:The patient presented with recurrent episodes of vertigo with a pure peripheral pattern and with concomitant episodes of burning muscle pain, muscle twitching, weight gain and fatigue, worsening with tension or stress that also occurred in periods without vertigo. Cochlear examinations only showed presbyacusis-like hearing loss. The diagnosis of stiff-person syndrome was made with electromyographic examination and from findings in the blood and cerebrospinal fluid of high titres of anti-glutamic acid decarboxylase (GAD67) autoantibodies. In a two-year follow-up period, therapy for stiff-person syndrome abolished episodes of both stiffness and vertigo.Conclusion:As far as we know, no other clinical case of acute vestibular damage with a possible correlation with anti-glutamic acid decarboxylase antibodies has been described. Peripheral vertigo possibly related to a lack of gamma aminobutyric acid underlines a possible role of gamma aminobutyric acid as a neurotransmitter in the peripheral vestibular system.

Distinct protein forms are produced from alternatively spliced bicistronic glutamic acid decarboxylase mRNAs during development

1994 ◽  
Vol 14 (11) ◽  
pp. 7535-7545
Author(s):  
G Szabo ◽  
Z Katarova ◽  
R Greenspan
Keyword(s):  
Glutamic Acid ◽  
Glutamic Acid Decarboxylase ◽  
Aminobutyric Acid ◽  
In Vitro Translation ◽  
Start Codon ◽  
Leader Peptide ◽  
Acid Decarboxylase ◽  
Gamma Aminobutyric Acid ◽  
Adult Type ◽  
Alternatively Spliced

It has been shown that the enzyme glutamic acid decarboxylase (GAD; EC 4.1.1.15), which catalyzes the conversion of L-glutamate to gamma-aminobutyric acid in the central nervous system of vertebrates, can be first detected in rodents at late embryonic stages. In contrast, we have found that the gene coding for the 67-kDa form of GAD is already transcriptionally active at embryonic day E10.5 in the mouse. In addition to the 3.5-kb adult-type mRNA, we have detected two 2-kb embryonic messages that contain alternatively spliced exons of 80 (I-80) and 86 (I-86) bp, respectively. The overlapping stop-start codon TGATG, found in the embryonic exons, converts the monocistronic adult-type transcript into a bicistronic one, coding for a 25-kDa leader peptide and a 44-kDa enzymatically active truncated GAD. A second stop codon at the 3' end of the 86-bp exon abolishes the expression of truncated GAD. The products of the two embryonic mRNAs were identified in a rabbit reticulocyte in vitro translation system, COS cells, and mouse embryos. The two GAD embryonic forms represent distinct functional domains and display characteristic developmental patterns, consistent with a possible role in the formation of the gamma-aminobutyric acid-ergic inhibitory synapses.

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