Glycogenesis and glyconeogenesis in human platelets: <i>Incorporation of glucose, pyruvate, and citrate into platelet glycogen; glycogen synthetase and fructose-1,6-diphosphatase activity</i>

Simon Karpatkin; Arthur Charmatz; Richard M. Langer

doi:10.1172/JCI106212

Glycogenesis and glyconeogenesis in human platelets: Incorporation of glucose, pyruvate, and citrate into platelet glycogen; glycogen synthetase and fructose-1,6-diphosphatase activity

Simon Karpatkin, Arthur Charmatz, and Richard M. Langer

Published January 1, 1970 - More info

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Abstract

Washed human platelets are capable of depositing 1-4 as well as probable 1-6 glucosyl linkages onto preexistent glycogen primer. They are also capable of degrading (glycogenolysis) newly synthesized 1-4 as well as probable 1-6 glucosyl linkages. A higher rate of glycogen synthesis was found in platelet suspensions containing lower concentrations of platelets. This was shown to result from decreased glycogen degradation and consequent increased residual glycogen primer in low platelet suspensions. The increased glycogen content of low platelet suspensions was not a result of platelet washing, removal of platelets from plasma, or release of platelet metabolites into the media. The enzyme glycogen synthetase was found to be present at a rate of 5.2 μmoles of uridine diphosphate (UDP) glucose incorporated into glycogen per gram platelets per hour at 37°C. The K_m for UDP glucose was 6.6 mmoles/liter. At optimum concentration of glucose 6-phosphate, the K_m was reduced 4.6 fold and V_max was increased 4.3-fold.

Human platelets contain the glyconeogenic pathway. They incorporate pyruvate-¹⁴C and citrate-¹⁴C into platelet glycogen and contain an apparent fructose-1,6-diphosphatase. The apparent fructose-1,6-diphosphatase was activated by adenosine monophosphate (AMP) and adenosine diphosphate (ADP), inhibited by adenosine triphosphate (ATP), and shown to be rate limiting for glyconeogenesis at physiologic concentration of adenine nucleotide.