Topic
Mannose transport
About: Mannose transport is a research topic. Over the lifetime, 28 publications have been published within this topic receiving 623 citations.
Papers
TL;DR: In this article, two novel genes affecting hexose transport in the yeast Saccharomyces cerevisiae have been identified: HXT1 (hexose transport) and ORF2 (ORF2) which are homologous to the large family of sugar transporter proteins from eucaryotes and procaryotes.
Abstract: Two novel genes affecting hexose transport in the yeast Saccharomyces cerevisiae have been identified. The gene HXT1 (hexose transport), isolated from plasmid pSC7, was sequenced and found to encode a hydrophobic protein which is highly homologous to the large family of sugar transporter proteins from eucaryotes and procaryotes. Multicopy expression of the HXT1 gene restored high-affinity glucose transport to the snf3 mutant, which is deficient in a significant proportion of high-affinity glucose transport. HXT1 was unable to complement the snf3 growth defect in low copy number. The HXT1 protein was found to contain 12 putative membrane-spanning domains with a central hydrophilic domain and hydrophilic N- and C-terminal domains. The HXT1 protein is 69% identical to GAL2 and 66% identical to HXT2, and all three proteins were found to have a putative leucine zipper motif at a consensus location in membrane-spanning domain 2. Disruption of the HXT1 gene resulted in loss of a portion of high-affinity glucose and mannose transport, and wild-type levels of transport required both the HXT1 and SNF3 genes. Unexpectedly, expression of beta-galactosidase activity by using a fusion of the lacZ gene to the HXT1 promoter in a multicopy plasmid was maximal during lag and early exponential phases of growth, decreasing approximately 100-fold upon further entry into exponential growth. Deletion analysis of pSC7 revealed the presence of another gene (called ORF2) capable of suppressing the snf3 null mutant phenotype by restoring high-affinity glucose transport and increased low-affinity transport.
107 citations
TL;DR: It is determined that mannose could enter the cells by two distinct transporters, one sensitive to dMM, present at the basolateral membrane of differentiated Caco-2 cells, and one insensitive to the drug localized at the brush border membrane of these cells.
32 citations
TL;DR: MAGP-36 might be multifunctional and present in a wide variety of sites in various organs and involved in mannose transport in the S3 segment of proximal tubules in kidney.
Abstract: By using quantitative Western blot analysis and the real time polymerase chain reaction technique, we investigated the differential gene expression of microfibril-associated glycoprotein (MAGP-36) in rat organs. The gene was expressed highly in sites rich in elastic fibers, such as aorta, skin, and esophagus. However, MAGP-36 was also expressed highly in some other sites containing no elastic fibers. In lung and trachea, the expression levels of MAGP-36 mRNA were about seven times higher than those in other elastic tissues, although the protein abundances were almost at the same levels as other elastic tissues. MAGP-36 seemed to be secreted outside these organs. In brain, kidney, and spleen, although the expression levels of MAGP-36 mRNA were low, substantial amounts of MAGP-36 protein were detected. An immunohistochemical study revealed that MAGP-36 was present at the brush border of the S3 segment of proximal tubules in kidney. Since MAGP-36 is known to bind to mannan, MAGP-36 might be involved in mannose transport in the S3 segment. Thus, MAGP-36 might be multifunctional and present in a wide variety of sites in various organs.
29 citations
TL;DR: A metformin-stimulated d-mannose transport (MSMT) activity in dermal fibroblasts is identified, suggesting that AMP-activated protein kinase may be a regulator of mannose metabolism and implies a therapy for congenital disorders of glycosylation-Ia.
28 citations
TL;DR: A novel effect of dMM on highly differentiated intestinal cells is demonstrated and it is suggested that a carrier-mediated mannose transport could exist in those cells and lead to a careful use of drugs acting on N-glycan processing.
26 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2010 | 2 |
| 2008 | 1 |
| 2005 | 1 |
| 2004 | 2 |
| 2001 | 2 |
| 2000 | 1 |