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Molecular pathology of glucose‐6‐phosphatase 1
Author(s) -
Burchell Ann
Publication year - 1990
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.4.12.2168325
Subject(s) - molecular pathology , glucose 6 phosphatase , pathology , chemistry , medicine , biochemistry , enzyme , gene
It was known in the 1950s that hepatic microsomal glucose‐6‐phosphatase plays an important role in the regulation of blood glucose levels. All attempts since then to purify a single polypeptide with glucose‐6‐phosphatase activity have failed. Until recently, virtually nothing was known about the molecular basis of glucose‐6‐phosphatase or its regulation. Recent studies of the type 1 glycogen storage diseases, which are human genetic deficiencies that result in impaired glucose‐6‐phosphatase activity, have greatly increased our understanding of glucose‐6‐phosphatase. Glucose‐6‐phosphatase has been shown to comprise at least five different polypeptides, the catalytic subunit of glucose‐6‐phosphatase with its active site situated in the lumen of the endoplasmic reticulum; a regulatory Ca 2+ binding protein; and three transport proteins, T 1; T 2 , and T 3 , which respectively allow glucose‐6‐phosphate, phosphate, and glucose to cross the endoplasmic reticulum membrane. Purified glucose‐6‐phosphatase proteins, immunospecific antibodies, and improved assay techniques have led to the diagnosis of a variety of new type 1 glycogen storage diseases. Recent studies of the type 1 glycogen storage diseases have led to a much greater understanding of the role and regulation of each of the glucose‐6‐phosphatase proteins.— B urchell , A. Molecular pathology of glucose‐6‐phosphatase. FASEB J. 4: 2978‐2988; 1990.