Expression of placental glucose transporter proteins in pregnancies complicated by fetal growth disorders

2020 ◽  
Author(s):  
Paweł Jan Stanirowski ◽  
Michał Lipa ◽  
Dorota Bomba-Opoń ◽  
Mirosław Wielgoś
Keyword(s):  
Fetal Growth ◽  
Glucose Transporter ◽  
Growth Disorders ◽  
Transporter Proteins ◽  
Glucose Transporter Proteins

scholarly journals Effect of insulin on the rates of synthesis and degradation of GLUT1 and GLUT4 glucose transporters in 3T3-L1 adipocytes

1993 ◽  
Vol 290 (3) ◽  
pp. 913-919 ◽  
Author(s):  
R J Sargeant ◽  
M R Pâquet
Keyword(s):  
Glucose Transporter ◽  
Insulin Treatment ◽  
Fold Increase ◽  
Glucose Transporters ◽  
Synthesis Rate ◽  
Insulin Stimulation ◽  
Transporter Proteins ◽  
Specific Manner ◽  
Glucose Transporter Proteins ◽  
Synthesis And Degradation

The effect of continuous insulin stimulation on the rates of turnover and on the total cellular contents of the glucose-transporter proteins GLUT1 and GLUT4 in 3T3-L1 adipocytes was investigated. Pulse-and-chase studies with [35S]methionine followed by immunoprecipitation of GLUT1 and GLUT4 with isoform-specific antibodies revealed the half-lives of these proteins to be 19 h and 50 h respectively. Inclusion of 100 nM insulin in the chase medium resulted in a decrease in the half-lives of both proteins to about 15.5 h. This effect of insulin was specific for the glucose-transporter proteins, as the average half-life of all proteins was found to be 55 h both with and without insulin stimulation. The effect of insulin on the rate of synthesis of the glucose transporters was determined by the rate of incorporation of [35S]methionine. After 24 h of insulin treatment, the rate of synthesis of GLUT1 and GLUT4 were elevated over control levels by 3.5-fold and 2-fold respectively. After 72 h of treatment under the same conditions, the rate of synthesis of GLUT1 remained elevated by 2.5-fold, whereas the GLUT4 synthesis rate was not different from control levels. Western-blot analysis of total cellular membranes revealed a 4.5-fold increase in total cellular GLUT1 content and a 50% decrease in total cellular GLUT4 after 72 h of insulin treatment. These observations suggest that the rates of synthesis and degradation of GLUT1 and GLUT4 in 3T3-L1 adipocytes are regulated independently and that these cells respond to prolonged insulin treatment by altering the metabolism of GLUT1 and GLUT4 proteins in a specific manner.

Glucose transporter proteins in brain

1994 ◽  
Vol 8 (13) ◽  
pp. 1003-1011 ◽  
Author(s):  
Frances Maher ◽  
Susan J. Vannucci ◽  
Ian A. Simpson
Keyword(s):  
Glucose Transporter ◽  
Transporter Proteins ◽  
Glucose Transporter Proteins

Glucose transporter proteins GLUT1 and GLUT3 like immunoreactivities in the fetal sheep brain are not reduced by maternal betamethasone treatment

2006 ◽  
Vol 403 (3) ◽  
pp. 261-265 ◽  
Author(s):  
Iwa Antonow-Schlorke ◽  
Martin Ebert ◽  
Thomas Müller ◽  
Harald Schubert ◽  
Andrea Gschanes ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Fetal Sheep ◽  
Transporter Proteins ◽  
Sheep Brain ◽  
Glucose Transporter Proteins

scholarly journals Effects of Hypoxia-Ischemia on GLUT1 and GLUT3 Glucose Transporters in Immature Rat Brain

1996 ◽  
Vol 16 (1) ◽  
pp. 77-81 ◽  
Author(s):  
Susan J. Vannucci ◽  
Lisa B. Seaman ◽  
Robert C. Vannucci
Keyword(s):  
Rat Brain ◽  
Glucose Transporter ◽  
Recovery Period ◽  
Neuronal Loss ◽  
Cerebral Hypoxia ◽  
Immature Rat ◽  
Transporter Proteins ◽  
Unilateral Brain Damage ◽  
Hypoxia Ischemia ◽  
Glucose Transporter Proteins

Cerebral hypoxia-ischemia produces major alterations in energy metabolism and glucose utilization in brain. The facilitative glucose transporter proteins mediate the transport of glucose across the blood–brain barrier (BBB) (55 kDa GLUT1) and into the neurons and glia (GLUT3 and 45 kDa GLUT1). Glucose uptake and utilization are low in the immature rat brain, as are the levels of the glucose transporter proteins. This study investigated the effect of cerebral hypoxia-ischemia in a model of unilateral brain damage on the expression of GLUT 1 and GLUT3 in the ipsilateral (damaged, hypoxic-ischemic) and contralateral (undamaged, hypoxic) hemispheres of perinatal rat brain. Early in the recovery period, both hemispheres exhibited increased expression of BBB GLUT1 and GLUT3, consistent with increased glucose transport and utilization. Further into recovery, BBB GLUT1 increased and neuronal GLUT3 decreased in the damaged hemisphere only, commensurate with neuronal loss.

scholarly journals Differential Expression of Glucose Transporter Proteins GLUT-1, GLUT-3, GLUT-8 and GLUT-12 in the Placenta of Macrosomic, Small-for-Gestational-Age and Growth-Restricted Foetuses

2021 ◽  
Vol 10 (24) ◽  
pp. 5833
Author(s):  
Paweł Jan Stanirowski ◽  
Dariusz Szukiewicz ◽  
Agata Majewska ◽  
Mateusz Wątroba ◽  
Michał Pyzlak ◽  
...  
Keyword(s):  
Gestational Age ◽  
Small For Gestational Age ◽  
Glucose Transporter ◽  
Placental Tissue ◽  
Glucose Transporters ◽  
Computer Assisted ◽  
Vascular Density ◽  
Transporter Proteins ◽  
Glut 1 ◽  
Glucose Transporter Proteins

Placental transfer of glucose constitutes one of the major determinants of the intrauterine foetal growth. The objective of the present study was to evaluate the expression of glucose transporter proteins GLUT-1, GLUT-3, GLUT-8 and GLUT-12 in the placenta of macrosomic, small-for-gestational-age (SGA) and growth-restricted foetuses (FGR). A total of 70 placental tissue samples were collected from women who delivered macrosomic ≥4000 g (n = 26), SGA (n = 11), growth-restricted (n = 13) and healthy control neonates (n = 20). Computer-assisted quantitative morphometry of stained placental sections was performed to determine the expression of selected GLUT proteins. Immunohistochemical staining identified the presence of all glucose transporters in the placental tissue. Quantitative morphometric analysis performed for the vascular density-matched placental samples revealed a significant decrease in GLUT-1 and increase in GLUT-3 protein expression in pregnancies complicated by FGR as compared to other groups (p < 0.05). In addition, expression of GLUT-8 was significantly decreased among SGA foetuses (p < 0.05). No significant differences in GLUTs expression were observed in women delivering macrosomic neonates. In the SGA group foetal birth weight (FBW) was negatively correlated with GLUT-3 (rho = −0.59, p < 0.05) and positively with GLUT-12 (rho = 0.616, p < 0.05) placental expression. In addition, a positive correlation between FBW and GLUT-12 expression in the control group (rho = 0.536, p < 0.05) was noted. In placentas derived from FGR-complicated pregnancies the expression of two major glucose transporters GLUT-1 and GLUT-3 is altered. On the contrary, idiopathic foetal macrosomia is not associated with changes in the placental expression of GLUT-1, GLUT-3, GLUT-8 and GLUT-12 proteins.

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