Disease relevance of HK1

• Effects of transformation by Rous sarcoma virus on sugar uptake and activity and the subcellular distribution of hexokinase isozymes in chick embryo fibroblasts were examined [1].
• Changes in muscle mRNAs for hexokinase, phosphofructokinase-1 and glycogen synthase in acute and persistent hypoglycemia induced by tolbutamide in chickens [2].
• The increase in hexokinase activity in hereditary avian muscular dystrophy [3].

High impact information on HK1

• No difference was found in the level of hexokinase activity in homogenates prepared from cells incubated glucose-free medium or standard medium when either 2-deoxy-D-[14C]glucose or D-glucose was used as substrate [4].
• Over this time period, insulin provoked selective increases (up to 5-fold) in factors relevant to the control of glycolysis: the activities of phosphofructokinase-1 (PFK-1), phosphofructokinase-2 (PFK-2) and hexokinase isoenzymes and the content of fructose 2,6-bisphosphate (F26BP) [5].
• Thymocyte Glut-1, Glut-3, and HK-1 mRNA abundance increased from e17 to d14 (P < 0.05) [6].
• Bursacyte glucose transporter-3 (Glut-3) mRNA abundance increased from d1 to d14 and hexokinase-1 (HK-1) mRNA abundance was maximum on e20 (P < 0.05) [6].
• Neither hexokinase nor glyceraldehyde-3-phosphate dehydrogenase activity differed between genotypes (p > 0.05) [7].

Chemical compound and disease context of HK1

• To elucidate the specificity of glucose metabolism in chicken skeletal muscle, changes in mRNA levels of hexokinase I (HKI), hexokinase II (HKII), phosphofructokinase-1 (PFK-1) and glycogen synthase (GS) were characterized in acute and persistent hypoglycemia induced by tolbutamide administration [2].

Anatomical context of HK1

• Heat-inactivation and electrophoretic mobility studies showed that although hexokinase Type I is the major form in both normal and transformed fibroblasts, there is a significant increase in the proportion of the Type II isozyme in the transformed cells [1].
• Hexokinase and glucose-6-phosphate dehydrogenase reveal only slight activity changes during muscle cell development under the conditions studied [8].

Associations of HK1 with chemical compounds

• There was no effect of thyroid hormone manipulation on particulate glucokinase activity although there was a significant reduction in particulate hexokinase activity (p less than 0.05) in thyroidectomized birds [9].
• The enzymes involved in the parasite pathway include mannitol-1-phosphate dehydrogenase (EC 1.1.1.17), mannitol-1-phosphatase (EC 3.1.3.22), mannitol dehydrogenase (EC 1.1.1.67), and hexokinase (EC 2.7.1.1) [10].
• Treatment of fed chickens for 2 weeks with thyroxine (50 micrograms: i.m. daily) plus triiodothyronine (50 micrograms) resulted in a marginal decrease (NS) in soluble glucokinase activity but significantly increased soluble hexokinase (p less than 0.05) activity [9].
• The activities of hexokinase, glucokinase, phosphofructokinase, glucose-6-phosphate dehydrogenase, citrate synthase, glycogen synthetase, glutamate dehydrogenase and aspartate transaminase were measured at 4, 8 and 20 weeks of age [11].
• The intracellular distribution of the glycolytic enzymes hexokinase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase and the pyruvate kinase isoenzymes type M1 and type M2 within unfertilized hen eggs was studied [12].

Other interactions of HK1

• The action of hydrocortisone, insulin, and glucagon on chicken liver hexokinase and glucose-6-phosphatase and on the plasma glucose and free fatty acid concentrations [13].

References