Integration of laboratory exercises in developmental biology and neurobiology courses using the Xenopus oocyte expression system

2000 ◽  
Vol 24 (5) ◽  
pp. 353-358
Author(s):  
W L Silver ◽  
C L Browne
Keyword(s):  
Developmental Biology ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System

scholarly journals Novel Mutations in the TMPRSS3 Gene May Contribute to Taiwanese Patients with Nonsyndromic Hearing Loss

2020 ◽  
Vol 21 (7) ◽  
pp. 2382
Author(s):  
Swee-Hee Wong ◽  
Yung-Chang Yen ◽  
Shuan-Yow Li ◽  
Jiann-Jou Yang
Keyword(s):  
Hearing Loss ◽  
Serine Protease ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Missense Mutations ◽  
Nonsyndromic Hearing Loss ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System ◽  
Transmembrane Serine Protease

A previous study indicated that mutations in the transmembrane protease serine 3 (TMPRSS3) gene, which encodes a transmembrane serine protease, cause nonsyndromic hearing loss (NSHL). This was the first description of a serine protease involved in hearing loss (HL). In Taiwan, however, data on the TMPRSS3 gene’s association with NSHL is still insufficient. In this study, we described 10 mutations of TMPRSS3 genes found in 14 patients after screening 230 children with NSHL. The prevalence of the TMPRSS3 mutation appeared to be 6.09% (14/230). Of the 10 mutations, three were missense mutations: c.239G>A (p.R80H), c.551T>C (p.L184S), and 1253C>T (p.A418V); three were silent mutations, and four were mutations in introns. To determine the functional importance of TMPRSS3 mutations, we constructed plasmids carrying TMPRSS3 mutations of p.R80H, p.L184S, and p.A418V. TMPRSS3 function can be examined by secretory genetic assay for site-specific proteolysis (sGASP) and Xenopus oocyte expression system. Our results showed that p.R80H, p.L184S, and p.A418V TMPRSS3 mutations gave ratios of 19.4%, 13.2%, and 27.6%, respectively, via the sGASP system. Moreover, these three TMPRSS3 mutations failed to activate the epithelial sodium channel (ENaC) in the Xenopus oocyte expression system. These results indicate that the p.R80H, p.L184S, and p.A418V missense mutations of TMPRSS3 resulted in greatly diminishing the proteolytic activity of TMPRSS3. Our study provides information for understanding the importance of TMPRSS3 in the NSHL of Taiwanese children and provides a novel molecular explanation for the role of TMPRSS3 in HL.

scholarly journals Signal transduction of rodent opioid μ, δ, κ-receptor in Xenopus oocyte expression system.

1994 ◽  
Vol 64 ◽  
pp. 129
Author(s):  
Takeaki Miyamae ◽  
Nobuyuki Fukushima ◽  
Yoshimi Misu ◽  
Hiroshi Takeshima ◽  
Kazuhiko Fukuda ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System ◽  
Κ Receptor

Lipid mediators modulate NMDA receptor currents in a Xenopus oocyte expression system

1997 ◽  
Vol 237 (1) ◽  
pp. 13-16 ◽  
Author(s):  
Sadaharu Tabuchi ◽  
Kazuhiko Kume ◽  
Makoto Aihara ◽  
Satoshi Ishii ◽  
Masayoshi Mishina ◽  
...  
Keyword(s):  
Nmda Receptor ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Lipid Mediators ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System

Concanavalin A potentiates NMDA-evoked responses in the Xenopus oocyte expression system

1989 ◽  
Vol 166 (2) ◽  
pp. 355-356 ◽  
Author(s):  
Marianne Geoffroy ◽  
Bertrand Lambolez ◽  
Lia Prado de Carvalho ◽  
Jean Rossier ◽  
Jacques Stinnakre
Keyword(s):  
Concanavalin A ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Evoked Responses ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System

[28] In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system

1998 ◽  
pp. 504-529 ◽  
Author(s):  
Mark W. Nowak ◽  
Justin P. Gallivan ◽  
Scott K. Silverman ◽  
Cesar G. Labarca ◽  
Dennis A. Dougherty ◽  
...  
Keyword(s):  
Amino Acids ◽  
Ion Channels ◽  
Unnatural Amino Acids ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Oocyte Expression ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System

Involvement of G protein βγ-subunits in diverse signaling induced by Gi/o-coupled receptors: study using the Xenopus oocyte expression system

2004 ◽  
Vol 287 (4) ◽  
pp. C885-C894 ◽  
Author(s):  
Yasuhito Uezono ◽  
Muneshige Kaibara ◽  
Osamu Murasaki ◽  
Kohtaro Taniyama
Keyword(s):  
Adenylate Cyclase ◽  
Opioid Receptor ◽  
Xenopus Oocyte ◽  
Expression System ◽  
Oocyte Expression ◽  
Intracellular Ca ◽  
Xenopus Oocyte Expression ◽  
Oocyte Expression System ◽  
Δ Opioid Receptor ◽  
Camp Levels

We studied the functions of βγ-subunits of Gi/o protein using the Xenopus oocyte expression system. Isoproterenol (ISO) elicited cAMP production and slowly activating Cl− currents in oocytes expressing β2-adrenoceptor and the protein kinase A-dependent Cl− channel encoded by the cystic fibrosis transmembrane conductance regulator (CFTR) gene. 5-Hydroxytryptamine (5-HT), [d-Ala2, d-Leu5]-enkephalin (DADLE), and baclofen enhanced ISO-induced cAMP levels and CFTR currents in oocytes expressing β2-adrenoceptor-CFTR and 5-HT1A receptor (5-HT1AR), δ-opioid receptor, or GABAB receptor, respectively. 5-HT also enhanced pituitary adenylate cyclase activating peptide (PACAP) 38-induced cAMP levels and CFTR currents in oocytes expressing PACAP receptor, CFTR and 5-HT1AR. The 5-HT-induced enhancement of Gs-coupled receptor-mediated currents was abrogated by pretreatment with pertussis toxin (PTX) and coexpression of G transducin α (Gtα). The 5-HT-induced enhancement was further augmented by coexpression of the Gβγ-activated form of adenylate cyclase (AC) type II but not AC type III. Thus βγ-subunits of Gi/o protein contribute to the enhancement of Gs-coupled receptor-mediated responses. 5-HT and DADLE did not elicit any currents in oocytes expressing 5-HT1AR or δ-opioid receptor alone. They elicited Ca2+-activated Cl− currents in oocytes coexpressing these receptors with the Gβγ-activated form of phospholipase C (PLC)-β2 but not with PLC-β1. These currents were inhibited by pretreatment with PTX and coexpression of Gtα, suggesting that βγ-subunits of Gi/o protein activate PLC-β2 and then cause intracellular Ca2+ mobilization. Our results indicate that βγ-subunits of Gi/o protein participate in diverse intracellular signals, enhancement of Gs-coupled receptor-mediated responses, and intracellular Ca2+ mobilization.

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