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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diabetologia 28 (1985), S. 852-856 
    ISSN: 1432-0428
    Keywords: Glucose-6-phosphatase ; glucose-6-phosphate ; diabetes ; antibodies ; blood glucose levels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Hepatic microsomal glucose-6-phosphatase activity levels and the hepatic output of glucose are increased in diabetes. We have used protein chemistry and immunological techniques to determine the mechanism by which the activity levels of the glucose-6-phosphatase system are increased in streptozotocin-induced diabetic rats. In the streptozotocin-induced diabetic rats, the activity of the glucose-6-phosphatase enzyme increased four-fold without appreciably altering the transport capacity of the glucose-6-phosphatase system. The solubilized diabetic rat liver glucose-6-phosphatase enzyme appeared to be very similar to the solubilized enzyme from control rat liver microsomes. They exhibit the same Km, are labile at 30 °C, are stabilized by sodium fluoride and they migrate to the same position during density gradient centrifugation. Immunological studies demonstrated that a greater amount of hepatic microsomal glucose-6-phosphatase enzyme protein is present in diabetic rats than in control rats. Thus, we have determined for the first time that increased levels of the glucose-6-phosphatase protein are present in streptozotocin-induced diabetes. The significance of this finding in relation to the regulation of the hepatic microsomal glucose-6-phosphatase system is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European journal of pediatrics 152 (1993), S. 18-21 
    ISSN: 1432-1076
    Keywords: Glucose-6-phosphatase ; Glycogen storage disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The understanding of type 1 glycogen storage diseases (GSDs) has been greatly hindered by a lack of knowledge of the molecular basis of glucose-6-phosphatase (Glc-6-P'ase). The problem has been the complete failure of many laboratories, including our own, to purify to homogeneity a single polypeptide with high levels of Glc-6-P'ase activity. The best preparations to date all contain five or six different polypeptide bands and have specific activities in the range 17–50 μmoles/min per milligram. The two major reasons for failure have been that Glc-6-P'ase is extremely difficult to solubilise from the microsomal membrane (large amounts of detergents are needed) and that it is not a single polypeptide as originally thought, but a multicomponent system. Recent studies of patients with type 1 GSD have proved that Glc-6-P'ase comprises at least five different polypepetides. Four of the proteins have now been purified and three have been cloned. We have assayed the Glc-6-P'ase system in over 600 human biopsy samples and developed microassays to diagnose deficiencies of each of the proteins. Ways of avoiding possible problems which have the potential to lead to the wrong diagnosis will be discussed.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    European journal of pediatrics 152 (1993), S. 14-17 
    ISSN: 1432-1076
    Keywords: Glucose-6-phosphatase ; Glycogen storage disease ; Transport proteins ; Pyrophosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Hepatic microsomal glucose-6-phosphatase (Glc-6-P'ase) is a complex multicomponent system containing at least three transport proteins, in addition to the catalytic subunit and a Ca2+ binding regulatory protein. The transport proteins have been designated T1 the glucose-6-phosphate transport protein, T2 a phosphate/pyrophosphate transport protein and T3 a glucose transport protein. Diagnosis of the genetic deficiencies of these transport proteins at present requires a complex kinetic analysis of the Glc-6-P'ase system as a whole. Here we describe the progress to date in our attempts to identify, purify and clone each transport protein with the ultimate aim of isolating specific cDNA probes for each transport protein which can be used for the diagnosis of types 1b, 1c and the putative 1d glycogen storage diseases.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 107 (1982), S. 1046-1052 
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Molecular Basis of Disease 1097 (1991), S. 31-36 
    ISSN: 0925-4439
    Keywords: Glucose 6-phosphate transport ; Glucose-6-phosphatase ; Microsome ; Pentamidine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Current Opinion in Cell Biology 1 (1989), S. 712-717 
    ISSN: 0955-0674
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Clinica Chimica Acta 173 (1988), S. 183-191 
    ISSN: 0009-8981
    Keywords: Development ; Glucose-6-phosphatase ; Glycogenosis ; Type 1 glycogen storage disease
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd.
    Child 28 (2002), S. 0 
    ISSN: 1365-2214
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine , Psychology
    Notes: Background Developmental failures to adequately control postnatal blood glucose levels are common in the transition from fetal to infant life and can persist for many months. The standard method of functionally measuring hepatic glucose production and/or disordered glucose production is the response to a glucagon tolerance test. Method We adapted the standard glucagon tolerance test used for children and adults for use in preterm infants. 79 consecutive preterm infants gestational age range 25–36 weeks (mean 32.2 weeks), mean birth weight 1.66 kg admitted to the Neonatal Intensive Care Unit, Ninewells Hospital, Dundee and who survived to discharge home were recruited into the study. At the time of discharge home the characteristics of the group were as follows: adjusted mean gestational age 36.7 weeks, mean discharge weight 2.23 kg. Results In this study of preterm infants the maximal increase in plasma glucose following administration of a glucagon tolerance test is 1.39 ± 07 mmol/L, n = 78 (range 0–3.98 mmol/L). Conclusions An increase in plasma glucose of less than 4 mmol/L is considered abnormal in adults following administration of a fasting glucagon tolerance test. The responses of preterm infants and adults to glucagon are clearly different. The attenuated response to glucagon in the preterm infants is consistent with the low levels of hepatic glucose-6-phosphatase activity in premature infants as glucose-6-phosphatase is the terminal step of the two main pathways of liver glucose production.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Science Ltd.
    Child 28 (2002), S. 0 
    ISSN: 1365-2214
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine , Psychology
    Notes: Background Infants with intra-uterine growth retardation have an increased risk of Sudden Infant Death Syndrome (SIDS). Hypoglycaemia is also significantly correlated with retardation of intra-uterine growth. A number of mutations in key proteins involved in regulation of blood glucose (e.g. glucokinase) have been found to result in reduced birth weight. Heterozygous mutations in the coding region of the glucokinase gene have been shown to cause MODY (a form of early onset Type II diabetes mellitus). The aim was to screen a cohort of SIDS and control infants who were either growth retarded or appropriately grown for gestational age to determine if any mutations and/or polymorphisms were present in the glucokinase gene. Methods PCR, denaturing high performance liquid chromatography on an automated Transgenomic WAVE DNA fragment analysis system and DNA sequencing. Results Genomic DNA was isolated from 129 infants who were either growth retarded or appropriately grown for gestational age. We found several rare novel polymorphisms in the glucokinase gene in the infant samples. However, none of the samples contained any of the mutations in the glucokinase gene previously reported in cases of MODY. Conclusions We have found rare novel polymorphisms in the glucokinase gene in the infant samples. In contrast in these samples, we have not found any examples of the previously reported mutations in the coding region of the glucokinase gene found in MODY. This clearly shows that while MODY babies are often small, MODY is not a common cause of either intra-uterine growth retardation or of SIDS.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 1073 (1991), S. 161-167 
    ISSN: 0304-4165
    Keywords: (Human placenta) ; Chorionic villi ; Glucose-6-phosphatase ; Microsome
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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