Regulation of human erythrocyte hexokinase by glucose‐1, 6‐diphosphate and inorganic phosphate

Rijksen, Gert; Staal, Gerard E.J.

doi:10.1016/0014-5793(77)80407-9

Cited by 30 publications

(18 citation statements)

References 13 publications

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“…For lymphocyte hexokinase the f(Pi) was about 2 at Pi concentrations of 5.0 mM and higher. This value is comparable with the data obtained for erythrocyte hexokinase [15]. For stimulated lymphoblasts hexokinase I a f(Pi) value of about 1.6 at a Pt concentration of 5.0 mM is reached.…”

Section: Influence Of P+supporting

confidence: 89%

“…The Pi-induced restoration of hexokinase activity at inhibition by phosphorylated hexoses is an important regulatory mechanism for glycolysis [15,16,19].…”

Section: Discussionmentioning

confidence: 99%

“…Glucose-l,6<liphosphate, which is one of these, is a well known inhibitor of hexokinase type I [14,15]. Inorganic phosphate (Pi) is capable of overcoming this inhibition in part [15--17].…”

Section: Introductionmentioning

confidence: 99%

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Hexokinase isozyme distribution and regulatory properties in lymphoid cells

Kraaijenhagen

Rijksen

Staal

1980

Biochimica et Biophysica Acta (BBA) - General Subjects

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SummaryThe glycolytic enzyme hexokinase is studied in cultured leukemic lymphoblasts, in normal lymphocytes and in lymphoblasts obtained by stimulation of normal lymphocytes with phytohaemagglutinin.Hexokinase activity levels in cultured lymphoblasts and in normal lymphocytes are identical, but somewhat higher levels are found in stimulated lymphocytes. Cultured leukemic lymphoblasts differ in isozyme content in comparison to the other lymphoid cells. Besides hexokinase I, which is detected in all the lymphoid cells, they are characterized by the presence of hexokinase II. The concentration of type II increases during cell growth. Another difference between leukemic lymphoblasts and mature and stimulated lymphocytes is found in the regulatory properties of hexokinase I. Hexokinase I from both normal and stimulated lymphocytes is inhibited by glucose-l,6-diphosphate. This inhibition is decreased in part by addition of inorganic phosphate. Hexokinase I from leukemic lymphocytes, however, is inhibited to a lesser extent by glucose-l,6-diphosphate. Inorganic phosphate has no effect at all on this inhibition.In accordance with these findings a different pattern in the hexokinase I region was detected in electrophoresis with several cell types. The subisozyme hexokinase Ib, which appears to be the phosphate-regulated form, is predominant in lymphocytes, whereas it is present in a minor fraction in the cultured leukemic lymphoblasts. In these cells hexokinase Ic predominates.

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Section: Influence Of P+supporting

confidence: 89%

“…The Pi-induced restoration of hexokinase activity at inhibition by phosphorylated hexoses is an important regulatory mechanism for glycolysis [15,16,19].…”

Section: Discussionmentioning

confidence: 99%

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Hexokinase isozyme distribution and regulatory properties in lymphoid cells

Kraaijenhagen

Rijksen

Staal

1980

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…Both bisphosphates are known effectors of phosphofructokinase. Glucose 1,6-bisphosphate acts not only as a stimulator of phosphofructokinase [12][13][14] but also as an inhibitor of hexokinase [13][14][15], which is another key enzyme of glycolysis. The dual role of this effector might be of importance in relation to glycogen breakdown and accelerated glycolysis during surfactant synthesis.…”

Section: Introductionmentioning

confidence: 99%

Phosphofructokinase in rat lung during perinatal development: characterization of subunit composition and regulation by fructose 2,6-bisphosphate and glucose 1,6-bisphosphate

Heesbeen¹,

Rijksen²,

Batenburg

et al. 1987

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…The hexokinase activity of the patienit's erythrocytes was only slightly decreased, but was markedly lowered when the degree of reticulocytosis was taken into account. The kinetic (2) and Received for publication 9 September 1977 and in revised formn 3 April 1978. electrophoretic (3) behavior of the enzyme showed no abnormalities. Since the report of Valentine et al (2), some other variants of hexokinase deficiency related to hereditary nonspherocytic hemolytic anemia have been reported (4)(5)(6)(7).…”

Section: Introductionmentioning

confidence: 99%

Human erythrocyte hexokinase deficiency. Characterization of a mutant enzyme with abnormal regulatory properties.

Rijksen¹,

Staal²

1978

J. Clin. Invest.

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A B S T R A C T In the erythrocytes of a patient with hereditary nonspherocytic hemolytic anemia, a homozygous expression of hexokinase deficiency was detected. The mutant enzyme was characterized by normal kinetic parameters with respect to its substrates, glucose and MgATP2-, normal pH optimum, normal heat stability at 40°C, but abnormal behavior with respect to its regulation by glucose-1,6-diphosphate and inorganic phosphate, and an altered electrophoretic pattern. Interpretation of the results revealed the presence of two different hexokinases type I in normal human erythrocytes: one enzyme with a high affinity for glucose-1,6-diphosphate, the inhibition of which is regulated by inorganic phosphate; and another enzyme with a lower affinity for the inhibitor, not regulated by inorganic phosphate. The former enzyme was not detectable in the erythrocytes of the patient, whereas the presence of the latter enzyme could be demonstrated.

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Regulation of human erythrocyte hexokinase by glucose‐1, 6‐diphosphate and inorganic phosphate

Cited by 30 publications

References 13 publications

Hexokinase isozyme distribution and regulatory properties in lymphoid cells

Hexokinase isozyme distribution and regulatory properties in lymphoid cells

Phosphofructokinase in rat lung during perinatal development: characterization of subunit composition and regulation by fructose 2,6-bisphosphate and glucose 1,6-bisphosphate

Human erythrocyte hexokinase deficiency. Characterization of a mutant enzyme with abnormal regulatory properties.

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