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. 1979 Nov 1;83(2):348–356. doi: 10.1083/jcb.83.2.348

Association of glycogen synthase phosphatase and phosphorylase phosphatase activities with membranes of hepatic smooth endoplasmic reticulum

PMCID: PMC2111548  PMID: 227915

Abstract

A detailed investigation was conducted to determine the precise subcellular localization of the rate-limiting enzymes of hepatic glycogen metabolism (glycogen synthase and phosphorylase) and their regulatory enzymes (synthase phosphatase and phosphorylase phosphatase). Rat liver was homogenized and fractionated to produce soluble, rough and smooth microsomal fractions. Enzyme assays of the fractions were performed, and the results showed that glycogen synthase and phosphorylase were located in the soluble fraction of the livers. Synthase phosphatase and phosphorylase phosphatase activities were also present in soluble fractions, but were clearly identified in both rough and smooth microsomal fractions. It is suggested that the location of smooth endoplasmic reticulum (SER) within the cytosome forms a microenvironment within hepatocytes that establishes conditions necessary for glycogen synthesis (and degradation). Thus the location of SER in the cell determines regions of the hepatocyte that are rich in glycogen particles. Furthermore, the demonstration of the association of synthase phosphatase and phosphorylase phosphatase with membranes of SER may account for the close morphological association of SER with glycogen particles (i.e., disposition of SER membranes brings the membrane-bound regulatory enzymes in close contact with their substrates).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Gilboe D. P., Larson K. L., Nuttall F. Q. Radioactive method for the assay of glycogen phosphorylases. Anal Biochem. 1972 May;47(1):20–27. doi: 10.1016/0003-2697(72)90274-6. [DOI] [PubMed] [Google Scholar]
  2. HIZUKURI S., LARNER J. STUDIES ON UDPG: ALPHA-1,4-GLUCAN ALPHA-4-GLUCOSYLTRANSFERASE. VII. CONVERSION OF THE ENZYME FROM GLUCOSE-6-PHOSPHATE-DEPENDENT TO INDEPENDENT FORM IN LIVER. Biochemistry. 1964 Nov;3:1783–1788. doi: 10.1021/bi00899a034. [DOI] [PubMed] [Google Scholar]
  3. Takeda Y., Brewer H. B., Jr, Larner J. Structural studies on rabbit muscle glycogen synthase. I. Subunit composition. J Biol Chem. 1975 Dec 10;250(23):8943–8950. [PubMed] [Google Scholar]
  4. Tan A. W., Nuttall F. Q. Evidence for the non-identity of proteins having synthase phosphatase, phosphorylase phosphatase and histone phosphatase activity in rat liver. Biochim Biophys Acta. 1978 Jan 12;522(1):139–150. doi: 10.1016/0005-2744(78)90330-3. [DOI] [PubMed] [Google Scholar]

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