High impact information on SLC2A9

• Identification and characterization of human glucose transporter-like protein-9 (GLUT9): alternative splicing alters trafficking [1].
• The recently cloned human GLUT9 gene, which maps to chromosome 4p15.3-p16, consists of 12 exons coding for a 540-amino acid protein [1].
• Deoxyglucose transport mediated by GLUT9 was not inhibited by cytochalasin B [1].
• Localization of GLUT9 and GLUT9DeltaN in three kidney-derived cell lines revealed a plasma membrane distribution for GLUT9 in COS-7 and HEK293 cells, whereas GLUT9DeltaN showed a perinuclear pattern and plasma membrane staining in COS-7 and HEK293 cells, respectively [1].
• Using heterologous expression of GLUT9 in Xenopus oocytes, GLUT9 appears to be a functional isoform with low affinity for deoxyglucose [1].

Biological context of SLC2A9

• GLUT9 was localized to chromosome 4 using a monochromosomal human/rodent somatic cell hybrid mapping panel [2].
• A portion of the GLUT9 cDNA is represented in a National Center for Biotechnology Information UniGene cluster, which maps to chromosome 4p15.3-p16 [2].
• Based on a sequence entry (NCBI accession number BC018897) and screening of expressed sequence tags, we have cloned an alternative splice variant of GLUT9 from human kidney cDNA [1].
• The predicted amino acid sequence of GLUT10 is nearly identical in length to the recently described GLUT9 homologue, but is longer than other known members of the GLUT family [3].

Anatomical context of SLC2A9

• Results showed that at least three GLUT isoforms (GLUT1, GLUT3 and GLUT9) are expressed by normal chondrocytes [4].
• Screening human tissue RNA by reverse transcription-PCR showed that GLUT9 is expressed mainly in kidney, liver, placenta, and leukocytes, whereas GLUT9DeltaN was detected only in kidney and placenta [1].
• The GLUT9 protein localized by immunohistochemistry to human kidney proximal tubules, and subcellular fractionation of human kidney revealed the GLUT9 protein in plasma membranes and high density microsomal membranes [1].
• Expression of the GLUT1 and GLUT9 facilitative glucose transporters in embryonic chondroblasts and mature chondrocytes in ovine articular cartilage [5].

Associations of SLC2A9 with chemical compounds

• IL-1beta induces an increased expression of glucose transporter (GLUT) 1 mRNA and protein, and GLUT9 mRNA [6].

Other interactions of SLC2A9

• Human articular chondrocytes express three facilitative glucose transporter isoforms: GLUT1, GLUT3 and GLUT9 [4].
• GLUT9 did not bind cytochalasin B as shown by a cytochalasin B binding assay, indicating a similar behavior of GLUT9 compared with GLUT5 [1].
• RESULTS: We identified 2 novel genes (GLUT8 and GLUT9) that are members of the facilitative glucose transporter family [7].

Analytical, diagnostic and therapeutic context of SLC2A9

• Western blotting confirmed the presence of the GLUT1 protein which migrated between the 50 and 64 kDa markers and two specific GLUT9 bands migrating under the 50 and 60 kDa markers, respectively [5].
• We have previously used RT-PCR to show that fully developed human articular chondrocytes express transcripts for the GLUT1 and GLUT9 glucose transporters [5].

References