Overexpression ofHUT1 gene stimulatesin vivo galactosylation by enhancing UDP-galactose transport activity inSaccharomyces cerevisiae

Yeast ◽  
2001 ◽  
Vol 18 (6) ◽  
pp. 533-541 ◽  
Author(s):  
Mami Kainuma ◽  
Yasunori Chiba ◽  
Makoto Takeuchi ◽  
Yoshifumi Jigami
Keyword(s):  
Transport Activity ◽  
Galactose Transport

scholarly journals SLC35A5 Protein—A Golgi Complex Member with Putative Nucleotide Sugar Transport Activity

2019 ◽  
Vol 20 (2) ◽  
pp. 276 ◽  
Author(s):  
Paulina Sosicka ◽  
Bożena Bazan ◽  
Dorota Maszczak-Seneczko ◽  
Yauhen Shauchuk ◽  
Teresa Olczak ◽  
...  
Keyword(s):  
Protein A ◽  
Sugar Transport ◽  
Uridine Diphosphate ◽  
Transport Activity ◽  
Nucleotide Sugar ◽  
Knock Out ◽  
Sugar Transporters ◽  
C Terminus ◽  
Glycolipid Synthesis ◽  
Galactose Transport

Solute carrier family 35 member A5 (SLC35A5) is a member of the SLC35A protein subfamily comprising nucleotide sugar transporters. However, the function of SLC35A5 is yet to be experimentally determined. In this study, we inactivated the SLC35A5 gene in the HepG2 cell line to study a potential role of this protein in glycosylation. Introduced modification affected neither N- nor O-glycans. There was also no influence of the gene knock-out on glycolipid synthesis. However, inactivation of the SLC35A5 gene caused a slight increase in the level of chondroitin sulfate proteoglycans. Moreover, inactivation of the SLC35A5 gene resulted in the decrease of the uridine diphosphate (UDP)-glucuronic acid, UDP-N-acetylglucosamine, and UDP-N-acetylgalactosamine Golgi uptake, with no influence on the UDP-galactose transport activity. Further studies demonstrated that SLC35A5 localized exclusively to the Golgi apparatus. Careful insight into the protein sequence revealed that the C-terminus of this protein is extremely acidic and contains distinctive motifs, namely DXEE, DXD, and DXXD. Our studies show that the C-terminus is directed toward the cytosol. We also demonstrated that SLC35A5 formed homomers, as well as heteromers with other members of the SLC35A protein subfamily. In conclusion, the SLC35A5 protein might be a Golgi-resident multiprotein complex member engaged in nucleotide sugar transport.

Characterization of aSchizosaccharomyces pombe mutant deficient in UDP-galactose transport activity

Yeast ◽  
2001 ◽  
Vol 18 (10) ◽  
pp. 903-914 ◽  
Author(s):  
Naotaka Tanaka ◽  
Mami Konomi ◽  
Masako Osumi ◽  
Kaoru Takegawa
Keyword(s):  
Transport Activity ◽  
Galactose Transport

Glucose as regulator of glucose transport activity and glucose-transporter mRNA in hamster beta-cell line

Diabetes ◽  
1992 ◽  
Vol 41 (5) ◽  
pp. 592-597 ◽  
Author(s):  
N. Inagaki ◽  
K. Yasuda ◽  
G. Inoue ◽  
Y. Okamoto ◽  
H. Yano ◽  
...  
Keyword(s):  
Beta Cell ◽  
Cell Line ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Transport Activity ◽  
Beta Cell Line ◽  
Glucose Transporter Mrna

Modulation of a Cellular Transport Activity by Capsicum Extracts

2018 ◽  
Vol 14 (2) ◽  
pp. 149-152
Author(s):  
Jie Chen ◽  
Vai H. Fong ◽  
Amandio Vieira
Keyword(s):  
Cellular Transport ◽  
Transport Activity

scholarly journals B0AT1 amino acid transporter complexed with SARS-CoV-2 receptor ACE2 forms a heterodimer functional unit: in situ conformation using radiation inactivation analysis

Function ◽  
2021 ◽  
Author(s):  
Bruce R Stevens ◽  
J Clive Ellory ◽  
Robert L Preston
Keyword(s):  
Amino Acid ◽  
Membrane Trafficking ◽  
Functional Unit ◽  
Membrane Vesicles ◽  
High Energy ◽  
Amino Acid Transporter ◽  
Neutral Amino Acid ◽  
Transport Activity ◽  
Acid Transporter

Abstract The SARS-CoV-2 receptor, Angiotensin Converting Enzyme-2 (ACE2), is expressed at levels of greatest magnitude in the small intestine as compared to all other human tissues. Enterocyte ACE2 is co-expressed as the apical membrane trafficking partner obligatory for expression and activity of the B0AT1 sodium-dependent neutral amino acid transporter. These components are assembled as an [ACE2: B0AT1]2 dimer-of-heterodimers quaternary complex that putatively steers SARS-CoV-2 tropism in the gastrointestinal (GI) tract. GI clinical symptomology is reported in about half of COVID-19 patients, and can be accompanied by gut shedding of virion particles. We hypothesized that within this 4-mer structural complex, each [ACE2: B0AT1] heterodimer pair constitutes a physiological “functional unit.” This was confirmed experimentally by employing purified lyophilized enterocyte brush border membrane vesicles that were exposed to increasing doses of high-energy electron radiation from a 16 MeV linear accelerator. Based on established target theory, the results indicated the presence of Na+-dependent neutral amino acid influx transport activity functional unit with target size mw = 183.7 ± 16.8 kDa in situ in intact apical membranes. Each thermodynamically stabilized [ACE2: B0AT1] heterodimer functional unit manifests the transport activity within the whole ∼345 kDa [ACE2: B0AT1]2 dimer-of-heterodimers quaternary structural complex. The results are consistent with our prior molecular docking modeling and gut-lung axis approaches to understanding COVID-19. These findings advance the understanding of the physiology of B0AT1 interaction with ACE2 in the gut, and thereby potentially contribute to translational developments designed to treat or mitigate COVID-19 variant outbreaks and/or GI symptom persistence in long-haul Post-Acute Sequelae of SARS-CoV-2 (PASC).

scholarly journals L1210/B23.1 cells express equilibrative, inhibitor-sensitive nucleoside transport activity and lack two parental nucleoside transport activities.

1992 ◽  
Vol 267 (24) ◽  
pp. 16951-16956
Author(s):  
D Vijayalakshmi ◽  
L Dagnino ◽  
J.A. Belt ◽  
W.P. Gati ◽  
C.E. Cass ◽  
...  
Keyword(s):  
Nucleoside Transport ◽  
Transport Activity
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