Synthesis of hyaluronate in differentiated teratocarcinoma cells. Mechanism of chain growth.
Hyaluronate could be labelled in vivo with [32P]phosphate. [32P]UDP in an alpha-glycosidic linkage constituted the reducing end of membrane-bound hyaluronate. The UDP is liberated during further chain elongation, indicating that chain growth occurs at the reducing end. [3H]Uridine could be incorporated into hyaluronate during synthesis on the isolated membraneous fraction from [3H]UDP-GlcNAc and [3H]UDP-GlcA, confirming the identification of UDP as a constituent of membrane-bound hyaluronate. These results led to a model of hyaluronate chain elongation at the reducing end by alternate addition of the chains to the substrates. Membrane-bound pyrophosphatases or 5'-nucleotidase are suggested as modulators of hyaluronate synthesis.
D002462:Cell Membrane / Q000378:metabolism; D002471:Cell Transformation, Neoplastic; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006820:Hyaluronic Acid / Q000096:biosynthesis*; D010761:Phosphorus Radioisotopes; D013724:Teratoma / Q000378:metabolism*; D014529:Uridine / Q000378:metabolism; D014536:Uridine Diphosphate N-Acetylgalactosamine / Q000378:metabolism; D014537:Uridine Diphosphate N-Acetylglucosamine / Q000378:metabolism
D010761:Phosphorus Radioisotopes; D014537:Uridine Diphosphate N-Acetylglucosamine; D014536:Uridine Diphosphate N-Acetylgalactosamine; D006820:Hyaluronic Acid; D014529:Uridine