• The Korean Journal of Physiology
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• v.24 no.2
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• pp.331-344
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• 1990

What makes glucose transport function sensitive to insulin in one cell type such as adipocyte, and insensitive in another such as liver cells is unresolved question at this time. Recently it is known that insulin stimulates glucose transport in adipocytes largely by redistributing transporter from the storage pool that is included in a low density microsomal fraction to plasma membrane. Therefore, insulin sensitivity may depend upon the relative distribution of gluscose transporters between the plasma membrane and in an intracellular storage compartment. In hepatocytes, the subcellular distribution of glucose transporter is less well documented. It is thus possible that the apparent insensitivity of the hepatocyte system could be either due to lack of the constitutively maintained, intracellular storage pool of glucose transporter or lack of insulin-mediated transporter translocation mechanism in this cell. In this study, I examined if any intracellular glucose transporter pool exists in hepatocytes and this pool is affected by insulin. The results obtained summarized as followings: 1) Distribution of subcellular fractions of hepatocyte showed that there are $24.9{\pm}1.3%$ of plasma membrane, $36.9{\pm}1.7%$ of nucleus-mitochondria enriched fraction, $23.5{\pm}1.2%$ of lysosomal fraction, $9.6{\pm}1.0%$ of high density microsomal fraction and $4.9{\pm}0.5%$ of low density microsomal fraction. 2) In adipocyte, there were $29.9{\pm}2.6%$ of plasma membrane, $19.4{\pm}1.9%$ of nucleus-mitochondria enriched fraction, $26.7{\pm}1.8%$ of high density microsomal fraction and $23.9{\pm}2.1%$ of low density microsomal fraction. 3) Surface labelling of sodium borohydride revealed that plasma membrane contaminated to lysosomal fraction by $26.8{\pm}2.8%$, high density microsomal fraction by $8.3{\pm}1.3%$ and low density microsomal fraction by $1.7{\pm}0.4%$ respectively. 4) Cytochalasin B bound to all of subcellular fractions with a Kd of $1.0{\times}10^{-6}M$. 5) Photolabelling of cytochalasin B to subcellular fractions occurred on 45 K dalton protein band, a putative glucose transporter and D-glucose inhibited the photolabelling. 6) Insulin didn't affect on the distribution of subcellular fractions and translocation of intracellular glucose transporters of hepatocytes. 7) HEGT reconstituted into hepatocytes was largely associated with plasma membrane and very little was found in low density microsomal fraction which equals to the native glucose transporter distribution. Insulin didn't affect on the distribution of exogeneous glucose transporter in hepatocytes. From the above results it is concluded that insulin insensitivity of hepatocyte may due to lack of intracellular storage pool of glucose transporter and thus intracellular storage pool of glucose transporter is an essential feature of the insulin action.

• Korean Journal of Microbiology
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• v.16 no.3
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• pp.122-130
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• 1978

During the sporulation stage in Saccharomyces cerevisiae J170, the incorporation of $D^{14}$ C-glucose into starved cells of sporulation stage as well as the vegetative one is appeared higher at pH 6.0. Glucose transport system, in both the vegetative and sporulation stage, is associated with "energy dependent" as the result of repression by such a respiratory inhibitor as 2, 4-dinitrophenol. The Km value of glucose uptake in vegetative stage and sporulation stage was 2.1 mM and 2.5 mM respectively, indicating that the glucose is considerably reuqired for vegetative growth. Competition and countertranspoer of glucose by frutose and galactose are more distinct in vegetative stage, comparing with sporulation stage. The main sugar components of yeast cells consists of ribose, mannose, and ${\alpha}, \;{\beta}-glucose$. Amounts of mannose is lower in the aporulation stage than that in the vegetative stage.

• Reproductive and Developmental Biology
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• v.39 no.4
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• pp.97-104
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• 2015

Glucose is universal and essential fuel of energy metabolism and in the synthesis pathways of all mammalian cells. Glucose is the one of the major precursors of lactose synthesis using glycolysis result in producing milk fat and protein. During the milk fat synthesis, lipoprotein lipase (LPL) and CD36 are required for glucose uptake. Various morecules such as acyl-CoA synthetase 1 (ACSL1) activity of acetyl-CoA synthetase 2 (ACSS2), ACACA, FASN AGPAT6, GPAM, LPIN1 are closely related with milk fat synthesis. Additionally, glucose plays a major role for synthesizing lactose. Activations of lactose synthesize enzymes such as membranebound enzyme, beta-1,4-galactosyl transferase (B4GALT), glucose-6-phosphate dehydrogenase (G6PD) are changed by concentration of glucose in blood resulting change of amount of lactose production. Glucose transporters are a wide group of membrane proteins that facilitate the transport of glucose over a plasma membrane. There are 2 types of glucose transporters which consisted facilitative glucose transporters (GLUT); and sodium-dependent transport, mediated by the Na+/glucose cotransporters (SGLT). Among them, GLUT1, GLUT8, GLUT12, SGLT1, SGLT2 are main glucose transporters which involved in mammary gland development and milk synthesis. However, more studies are required for revealing clear mechanism and function of other unknown genes and transporters. Therefore, understanding of the mechanisms of glucose usage and its regulation in mammary gland is very essential for enhancing the glucose utilization in the mammary gland and improving dairy productivity and efficiency.

• The Korean Journal of Physiology and Pharmacology
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• v.3 no.3
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• pp.357-364
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• 1999

We investigated the role of $Ca^{2+}$ and protein kinases/phosphatases in the stimulatory effect of insulin on glucose transport. In isolated rat adipocytes, the simple omission of $CaCl_2$ from the incubation medium significantly reduced, but did not abolish, insulin-stimulated 2-deoxy glucose (2-DG) uptake. Pre-loading adipocytes with intracellular $Ca^{2+}$ chelator, 5,5'-dimethyl bis (o-aminophenoxy)ethane-N,N,N'N' tetraacetic acetoxymethyl ester (5,5'-dimethyl BAPTA/AM) completely blocked the stimulation. Insulin raised intracellular $Ca^{2+}$ concentration $([Ca^{2+}]_i)$ about 1.7 times the basal level of $72{\pm}5$ nM, and 5,5'-dimethyl BAPTA/AM kept it constant at the basal level. This correlation between insulin-induced increases in 2-DG uptake and $[Ca^{2+}]_i$ indicates that the elevation of $[Ca^{2+}]_i$ may be prerequisite for the stimulation of glucose transport. Studies with inhibitors (ML-9, KN-62, cyclosporin A) of $Ca^{2+}-calmodulin$ dependent protein kinases/phosphatases also indicate an involvement of intracellular $Ca^{2+}.$ Additional studies with okadaic acid and calyculin A, protein phosphatase-1 (PP-1) and 2A (PP-2A) inhibitors, indicate an involvement of PP-1 in insulin action on 2-DG uptake. These results indicate an involvement of $Ca^{2+}-dependent$ signaling pathway in insulin action on glucose transport.

• Proceedings of the Korean Aquaculture Society Conference
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• 2003.10a
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• pp.105-106
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• 2003

Physiological responses (cortisol, glucose, lactic acid, osmolality and hematology) of olive flounder (Paralichthys olivaceus) to stressors associated with confinement and subsequent transport were investigated. Specimens were subjected to confinement stress for 3 h, prior to transport for 15 h. Two different size cohorts of the fish, large (839.6$\pm$162.7 g) and small (98.2$\pm$14.8 g), were used. Experimental cohorts of the fish were divided into 3 groups for blood sampling: group A, sampled at the beginning of confinement and 3 h before transport (BT, -3 h), after confinement and at the beginning of transport (BT, 0 h), 3 h after transport had begun (AT, 3 h), and after 15 h transport (AT, 15 h); group B, sampled at BT, 0 h, at AT, 3 h, and at AT, 15 h; and, group C, sampled at AT, 3 h, and at AT, 15 h. In the cohort of large fish, plasma cortisol levels of the A group were increased over time, from 4.2 ng/ml (BT, -3 h), to 92.0 ng/ml (BT, 0 h), 118.5 ng/ml (AT, 3 h) and 105.5 ng/ml (AT, 15 h). A similar pattern was evident in the B group, in which cortisol increased from 47.5 ng/ml (BT, 0 h) to 53.5 ng/ml (AT, 15 h); and, for the C group, in which cortisol increased from 43.5 ng/ml (AT, 3 h) to 71.5 ng/ml (AT, 15 h). Glucose levels of the A group also were significantly increased, from 39.5 mg/dl (BT, -3 h), to 121.0 mg/dl (BT, 0 h), 298.0 mg/dl (AT, 3 h) and 260.5 mg/dl (AT, 15 h). Lactic acid levels increased markedly during transport, from less than 1 mmol/L (BT, 0 h) to 12.0 mmol/L (AT, 15 h). Plasma osmolality increased from 405.5 mOsm/kg (BT, -3 h, for group A) to values near 500 mOsm/kg subsequent to confinement and transport. In the small-size cohort, plasma cortisol, glucose, lactic acid and osmolality levels showed similar but less pronounced trends than those observed for the large-size cohort. This research provides baseline data on cortisol, glucose, lactic acid, osmolality and hematological responses to confinement and transport, which should be useful to aquaculturists working with olive flounder and to scientists studying other flatfish species.

• Biomolecules & Therapeutics
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• v.24 no.1
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• pp.94-98
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• 2016

The objective of the present study was to elucidate the effect of bisphosphonates, anti-osteoporosis agents, on glucose uptake in retinal capillary endothelial cells under normal and high glucose conditions. The change of glucose uptake by pre-treatment of bisphosphonates at the inner blood-retinal barrier (iBRB) was determined by measuring cellular uptake of $[^3H]3$-O-methyl glucose (3-OMG) using a conditionally immortalized rat retinal capillary endothelial cell line (TR-iBRB cells) under normal and high glucose conditions. $[^3H]3$-OMG uptake was inhibited by simultaneous treatment of unlabeled D-glucose and 3-OMG as well as glucose transport inhibitor, cytochalasin B. On the other hand, simultaneous treatment of alendronate or pamidronate had no significant inhibitory effect on $[^3H]3$-OMG uptake by TR-iBRB cells. Under high glucose condition of TR-iBRB cells, $[^3H]3$-OMG uptake was increased at 48 h. However, $[^3H]3$-OMG uptake was decreased significantly by pre-treatment of alendronate or pamidronate compared with the values for normal and high glucose conditions. Moreover, geranylgeraniol (GGOH), a mevalonate pathway intermediate, increased the uptake of $[^3H]3$-OMG reduced by bisphosphonates pre-treatment. But, pre-treatment of histamine did not show significant inhibition of $[^3H]3$-OMG uptake. The glucose uptake may be down regulated by inhibiting the mevalonate pathway with pre-treatment of bisphosphonates in TR-iBRB cells at high glucose condition.

• The Korean Journal of Physiology and Pharmacology
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• v.3 no.2
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• pp.191-198
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• 1999

This study was undertaken to examine the effect of ethanol on $Na^+-dependent$ transport systems (glucose, phosphate, and dicarboxylate) in renal brush-border membrane vesicles (BBMV). Ethanol inhibited $Na^+-dependent$ uptakes of glucose, phosphate, and succinate in a dose-dependent manner, but not the uptakes of $Na^+-dependent.$ The $H^+/TEA$ antiport was reduced by 8% ethanol. Kinetic analysis showed that ethanol caused a decrease in $V_{max}$ of three transport systems, leaving $K_m$ values unchanged. Ethanol decreased phlorizin binding, which was closely correlated with the decrease in $V_{max}$ of $Na^+-glucose$ uptake. These results indicate that ethanol inhibits $Na^+-dependent$ uptakes of glucose, phosphate, and dicaboxylate and that the reduction in $V_{max}$ of $Na^+-glucose$ uptake is caused by a decrease in the number of active carrier proteins in the membrane.

• Journal of Aquaculture
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• v.16 no.3
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• pp.135-141
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• 2003

Physiological responses (cortisol, glucose, lactic acid, osmolality and hematology) of olive flounder (Paralichthys olivaceus) to stressors associated with confinement and subsequent transport were investigated. Specimens were subjected to confinement stress for 3 h, prior to transport for 15 h. Two different size cohorts of the fish, large (839.6$\pm$162.7 g) and small (98.2$\pm$14.8 g), were used. Experimental cohorts of the fish were divided into 3 groups for blood sampling: group A, sampled at the beginning of confinement and 3 h before transport (BT, -3 h), after confinement and at the beginning of transport (BT, 0 h), 3 h after transport had begun (AT, 3 h), and after 15 h transport (AT, 15 h); group B, sampled at BT, 0 h, at AT, 3 h, and at AT, 15 h; and, group C, sampled at AT, 3 h, and at AT, 15 h. In the cohort of large fish, plasma cortisol levels of the A group were increased over time, from 4.2 ng/ml (BT,-3 h), to 92.0 ng/ml (BT, 0 h), 118.5 ng/ml (AT, 3 h) and 105.5 ng/ml (AT, 15 h). A similar pattern was evident in the B group, in which cortisol increased from 47.5 ng/ml (BT, 0 h) to 53.5 ng/ml (AT, 15 h); and, for the C group, in which cortisol increased from 43.5 ng/ml (AT, 3 h) to 71.5 ng/ml (AT, 15 h). Glucose levels of the A group also were significantly increased, from 39.5 mg/dl (BT,-3 h), to 121.0 mg/dl (BT, 0 h),298.0 mg/dl (AT, 3 h) and 260.5 mg/dl (AT, 15 h). Lactic acid levels increased markedly during transport, from less than 1 mmol/L (BT, 0 h) to 12.0 mmol/L (AT, 15 h). Plasma osmolality increased from 405.5 mOsm/kg (BT, -3 h, for group A) to values near 500 mOsM/kg subsequent to confinement and transport. In the small-size cohort, plasma cortisol, glucose, lactic acid and osmolality levels showed similar but less pronounced trends than those observed for the large-size cohort. This research provides baseline data on cortisol, glucose, lactic acid, osmolality and hematological responses to confinement and transport, which should be useful to aquaculturists working with olive flounder and to scientists studying other flatfish species.

• Journal of Animal Science and Technology
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• v.51 no.6
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• pp.493-502
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• 2009

Glucose is a major source of metabolic fuel and lipid and protein syntheses. Transport of glucose into the cell is regulated by an action of glucose transport.associated transporters, especially solute carriers 2A (Slc2a, protein symbol GLUT). The present study was focused on examination of mRNA expression of various Slc2a isoforms in the epididymis during postnatal development. Total RNAs isolated from different epididymal segments (caput, corpus, and caudal epididymis) were utilized for real-time polymerase chain reaction analyses. Results showed that Slc2a 1, 3, 4, 5, and 8 were expressed in the entire epididymal regions. In addition, the abundance of these Slc2a isoforms' transcripts was different within each epididymal regions. Moreover, the present study showed differential expression of these Slc2a isoforms among different epididymal segments according to postnatal ages. The current study suggests that glucose transport in the epididymis via various Slc2a isoforms would be necessary for maintenance of the epididymal functions.

• Preventive Nutrition and Food Science
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• v.7 no.2
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• pp.113-118
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• 2002

Alpha-lipoic acid is a known hypoglycemic agent that may be useful in the treatment of diabetes. The objective of this study was to investigate the fate of glucose in isolated muscles incubated with lipoic acid by determining its direct effects on specific metabolic and signaling pathways. Soleus muscles from healthy rats were incubated with lipoic acid in the absence or presence of insulin. Glucose transport, glycogen synthesis, glucose oxidation and lipid synthesis were determined and affects on major pathways associated with insulin signaling were evaluated. Glucose transport was not significantly altered by the addition of lipoic acid to the incubation medium. However, lipoic acid decreased glycogen synthesis in comparison to controls. Glucose oxidation was moderately increased while de-novo lipid synthesis from glucose was inhibited. Wortmannin repressed insulin stimulation of glucose incorporation into glycogen, an effect that was augmented by the combined treatment of wortmannin and lipoic acid. Basal and insulin-stimulated serine phosphorylation of Akt was not changed by the addition of lipoic acid to the incubation medium. These data show that in this in vitro model, lipoic acid did not significantly affect glucose uptake but dramatically modified pathways of glucose metabolism within muscle tissue.