Glucose Transport Proteins, Facilitative ; deficiency ; Humans ; Syndrome

No abstract available.
Glucose Transport Proteins, Facilitative* ; Glucose* ; Humans ; Insulin* ; Metabolome*

Facilitative glucose transporters (GLUT) are proteins that mediate glucose transmembrane transport in the form of facilitated diffusion, which play an important role in regulating cell energy metabolism. There are many breakthroughs in researches of facilitative GLUT in recent years. It has been known that there are 14 subtypes of facilitative GLUT with obvious tissue specificity in distribution and physiological function. In the present review, the tissue and cellular distribution, subcellular localization, expression regulation, physiological function and the relationship to diseases of facilitative GLUT subtypes were summarized, in order to further understand their physiological and pathophysiological significances.
Biological Transport ; Disease ; Energy Metabolism ; Glucose ; Glucose Transport Proteins, Facilitative ; physiology ; Humans

We found the changed distribution of glucose transporter (GLUT) proteins in the skin during rat development. At 15 days of gestation, GLUT1 and 2 proteins were expressed in the stratum corneum of epidermal cells. In postnatal skin, however, GLUT1 and 2 exhibit different expression patterns. While GLUT1 expression becomes more restricted to the stratum basale with development, GLUT2 was found mainly in stratum spinosum and granulosum, but not being localized in the stratum basale at any stages of perinatal skin development. Considering all these, it can be speculated that each GLUT protein plays its specific role in different epidermal layers and that the glucose used in mammalian skin in utero could be originated from the amniotic fluid during skin development.
Amniotic Fluid ; Animals ; Epidermis ; Female ; Glucose Transport Proteins, Facilitative ; Glucose* ; Immunohistochemistry ; Pregnancy ; Rats* ; Skin*

Glucose is essential for testicular function; the uptake of carbohydrate-derived glucose by cells is mediated by glucose transporters (GLUTs). In the present study, we investigated the activity of GLUT1 and GLUT3, the two main isoforms of GLUTs found in testes, in the left scrotal and right abdominal testes of a German Shepherd dog. Immunohistochemical analysis showed that GLUT1 immunoreactivity was absent in the scrotal and abdominal testes. In contrast, weak to moderate GLUT3 immunoreactivity was observed in mature spermatocytes as well as spermatids in the scrotal testis. In the abdominal testis, relatively strong GLUT3 immunoreactivity was detected in Leydig cells only and was absent in mature spermatocytes and spermatids. GLUT3 immunoreactivity was significantly decreased in the tubular region of abdominal testis and significantly increased in the extra-tubular (interstitial) region of abdominal testis compared to observations in the each region of scrotal testis, respectively. These results suggest that GLUT3 is the major glucose transporter in the testes and that abdominal testes may increase the uptake of glucose into interstitial areas, leading to an increased risk of developing cancer.
Animals ; Cryptorchidism ; Dogs* ; Glucose Transport Proteins, Facilitative* ; Glucose* ; Leydig Cells ; Male ; Protein Isoforms ; Spermatids ; Spermatocytes ; Testis*

Cancer tissues are characterized by increased glucose uptake. 18F-fluorodeoxyglucose(FDG), a glucose analogue is used for the diagnosis of cancer in PET studies. This study was aimed to compare the glucose uptake and glucose transporter l(GLUT1) expression in various human colon cancer cells. We measured FDG uptake by cell retention study and expression of GLUTI using Western blotting. Human colon cancer cells, SNU-C2A, SNU-C4 and SNU-C5, were used. The cells were incubated with 1micro Ci/ml of FDG in HEPES-buffered saline for one hour. The FDG uptake of SNU-C2A,SNU-C4 and SNU-C5 were 16.8+/-1.36, 12.3+/-5.55 and 61.0+/-2.17cpm/microgram of protein, respectively. Dose-response and time-course studies represent that FDG uptake of cancer cells were dose dependent and time dependent. The rate of FDG uptake of SNU-C2A, SNU-C4 and SNU-C5 were 0.29+/-0.03, 0.21+/-0.09 and 1.07+/-0.07cpm/min/microgram of protein, respectively. Western blot analysis showed that the GLUT1 expression of SNU-C5 was significantly higher than those of SNU-C2A and SNU-C4. These results represent that FDG uptake into human colon cancer cells are different from each other. In addition, FDG uptake and expression of CLUT1 are closely related in human colon cancer cells.
Blotting, Western ; Colon* ; Colonic Neoplasms* ; Diagnosis ; Glucose ; Glucose Transport Proteins, Facilitative ; Humans*

In this study, we observed the ontogenetic changes in glucose transporter 3 (GLUT3) immunoreactivity, a major neuronal GLUT, in the dentate gyrus of mouse brains at various ages: postnatal day (P) 1, 7, 14, 28, and 56. At P1, cresyl violet staining showed abundant neurons in the dentate gyrus, whereas the granule cell layer was ill-defined. At P7, the granule cell layer was observed, and cresyl violet-positive cells were dispersed throughout the polymorphic layer. At P14, the granule cell layer was well-defined, and cresyl violet positive cells were detected abundantly in the polymorphic layer. At P28 and P56, cresyl violet-positive cells were observed in the granule cell layer, as well as in the polymorphic layer. At P1, GLUT3 immunoreactivity was detected in the dentate gyrus. At P7, GLUT3 immunoreactive cells were scattered in the polymorphic and molecular layer. However, at P14, GLUT3 immunoreactivity was observed in the polymorphic layer as well as subgranular zone of the dentate gyrus. At P28, GLUT3 immunoreactivity was detected in the polymorphic layer of the dentate gyrus. At P56, GLUT3 immunoreactivity was observed predominantly in the subgranular zone of the dentate gyrus. GLUT3 immunoreactive cells were mainly colocalized with doublecortin, which is a marker for differentiated neuroblasts, in the polymorphic layer and subgranular zone of dentate gyrus at P14 and P56. These results suggest that the expression of GLUT3 is closely associated with postnatal development of the dentate gyrus and adult neurogenesis.
Adult ; Animals ; Brain ; Dentate Gyrus* ; Glucose Transport Proteins, Facilitative* ; Glucose* ; Humans ; Mice* ; Neurogenesis ; Neurons ; Viola

BACKGROUND: Malignant cells exhibit increased glycolytic metabolism, and in many cases increased glucose transporter gene expression. The authors hypothesized that GLUT1 glucose transporter expression is increased in gallbladder carcinoma, and the degree of expression might have prognostic significance. METHODS: To evaluate a possible prognostic factor, we studied the expression of GLUT1 glucose transporter by an immunohistochemical method in 56 gallbladder carcinomas from patients and we compared these results with established prognostic factors. RESULTS: Of the 56 cases, 34 (60.7%) were positive for GLUT1. The expression of GLUT1 was not associated with patient age, sex and histologic type. Whereas the expression of GLUT1 was significantly correlated with depth of tumor invasion and lymph node and distant metastases. CONCLUSIONS: GLUT1 glucose transporter expression is strongly associated with poor prognostic factors of the gallbladder carcinoma and the assessment of the extent of GLUT1 immunostaining identifies patient with poorer prognosis.
Gallbladder* ; Gene Expression ; Glucose Transport Proteins, Facilitative* ; Glucose* ; Humans ; Lymph Nodes ; Metabolism ; Neoplasm Metastasis ; Prognosis

PURPOSE: The aim of this study was to assess the expression of metabolism-related proteins including glucose transporter 1 (Glut-1), carbonic anhydrase IX (CAIX) and monocarboxylate transporter 4 (MCT4) in breast mucinous carcinoma and to evaluate the implications of the results. METHODS: Immunohistochemical staining for Glut-1, CAIX, and MCT4 was performed on tissue sections from 59 cases of mucinous carcinoma to evaluate the association between the expression of metabolism-related proteins and clinicopathologic factors. Mucinous carcinoma was subclassified into type A and type B according to histopathological characteristics. RESULTS: Of the 59 patients, 35 patients (59.3%) were type A mucinous carcinoma and 24 patients (40.7%) were type B mucinous carcinoma. Stromal expression of MCT4 was significantly associated with a high histologic grade (p=0.022) and type B mucinous carcinoma (p=0.016). There were significant positive correlations between the expression of Glut-1, CAIX and tumoral expression of MCT4 (p<0.05). CONCLUSION: We assessed the expression of metabolism-related proteins including Glut-1, CAIX, and MCT4 in breast mucinous carcinoma and found that the stromal expression of MCT4 was higher in type B mucinous carcinoma than in type A, which reflected a difference in the tumor microenvironment.
Adenocarcinoma, Mucinous ; Breast ; Carbonic Anhydrases ; Glucose Transport Proteins, Facilitative ; Humans ; Mucins ; Proteins ; Tumor Microenvironment

PURPOSE: Mediastinal staging of non-small cell lung cancer can be markedly improved by FDG-PET scan, but the problem of false staging of mediastinal nodes by PET scan in non-small cell lung cancer has not yet been overcome. The aim of this study was to identify the mechanism underlying the false staging of mediastinal nodes by FDG-PET in the case of non-small cell lung cancer. MATERIALS AND METHODS: To evaluate the factors determining the FDG uptake in mediastinal nodes, FDG-PET was performed preoperatively, and mediastinal dissection with pulmonary resection was performed in 62 patients with NSCLC. GLUT-1 expression was studied by immunohistochemistry of the mediastinal nodes (n=111, true positive 31, true negative 41, false positive 27, false negative 12) using the anti-GLUT-1 antibody. The size, percentage of tumor (tumor ratio), labeling index (rate of stained tumor), staining intensity of the tumor, level of follicular hyperplasia, and staining intensity of the follicle center in the mediastinal node were also studied. RESULTS: There was no significant difference in size among the 4 nodal groups (TP, TN, FP, FN), nor in the tumor ratio of the metastatic nodes between the TP and FN groups. The labeling index and staining intensity of the TP group were higher than those of the FN group (Mann-Whitney test, p=.001, p=.007) in the case of the metastatic nodes. The level of follicular hyperplasia of the FP group was higher than that of the TN group in the case of the non-metastatic nodes (p=.000). CONCLUSION: These results suggest that in mediastinal staging of non-small cell lung cancer by FDG-PET, the FN node is associated with low uptake of FDG due to low expression of GLUT-1, and that the FP node is associated with a high level of follicular hyperplasia as a result of there being a reactive change to an inflammatory and/or immune reaction. This is the first report on the mechanism underlying the false results that are sometimes obtained, and which constitute a major problem in the clinical application of FDG-PET to the mediastinal staging of non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung* ; Glucose Transport Proteins, Facilitative ; Humans ; Hyperplasia ; Immunohistochemistry ; Positron-Emission Tomography