Preliminary observations on a glucose-6-phosphate-hydrolyzing enzyme in secretory cells: a light microscopic study

Rosen, Sidney I.

doi:10.1007/bf01004971

Cited by 4 publications

(1 citation statement)

References 11 publications

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“…However, microsomal glucose-6-phosphatase activity has been demonstrated unequivocally to be present in pancreatic islets (Waddell & Burchell, 1988), human foetal adrenal glands (Hume, et al, 1995), and low levels have been found in intestinal and gall-bladder mucosa (Hill et al, 1989;Pears et al, 1992) and in some (but not all) brain astrocytes (Bell et al, 1993, Forsyth et at., 1993. There have also been several reports of glucose-6-phosphate hydrolysis in trachea (Rosen, 1970(Rosen, , 1972Kanamura, 1975) or its absence (Hinsch, 1966), using conventional histochemical methods based on the lead salt method (Chiquoine, 1953;Wachstein & Meisel, 1956). However, non-specific hydrolysis of glucose-6-phosphate, other than that catalysed by glucose-6-phosphatase (Burchell & Waddell, 1991), remains a problem in histochemical assays of enzyme activity.…”

Section: Introductionmentioning

confidence: 94%

The glucose-6-phosphatase enzyme in developing human trachea and oesophagus

Hume

Burchell

1996

Histochem J

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Glucose-6-phosphatase is an endoplasmic reticulum system which is found primarily in liver and kidney. Recently, it has become clear that it is also present in lower amounts in a variety of other tissues. Previous histochemical studies of glucose-6-phosphate hydrolysis in trachea have given equivocal results and only one study on adult oesophagus has shown glucose-6-phosphatase, enzymatic activity but without cellular localization. We have now shown, using microassay techniques, that microsomes isolated from human foetal trachea and oesophagus both contain low levels of specific glucose-6-phosphatase activity (mean = 0.9 and 1.5 nmol min-1 mg-1 microsomal protein, respectively) which are less than 10% of the levels in microsomes of human foetal liver of similar age. In the developing trachea, glucose-6-phosphatase immunoreactivity has been found, using a monospecific antibody to the catalytic subunit of the glucose-6-phosphatase enzyme, to be first present at 10-11 weeks' gestation, and thereafter in foetal life, predominantly present in ciliated cells, with smaller amounts in non-ciliated secretory cells, duct lining cells, and occasional basal cells. The foetal oesophageal epithelium is transiently ciliated from 10 to 11 weeks' gestation, but ciliated cells are gradually replaced by squamous cells from 14 to 16 weeks onwards. Glucose-6-phosphatase immunoreactivity in human foetal oesophagus is predominantly confined to ciliated cells, but non-ciliated luminal cells are also reactive, as are occasional basal cells. Mucus secretory cells in foetal trachea and oesophagus are immunonegative, as is the entire epithelium of both organs in the embryo (up to 56 postovulatory days.

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Section: Introductionmentioning

confidence: 94%

The glucose-6-phosphatase enzyme in developing human trachea and oesophagus

Hume

Burchell

1996

Histochem J

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Glucose 6‐phosphatase activity in pregnant and lactating mammary glands of the mouse

et al. 1986

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Glucose 6-phosphatase activity was studied in the secretory epithelial cell and other cell types composing alveoli of the mammary gland (cytochemical study) and in the whole mammary gland (biochemical study) of pregnant and lactating mice. The reaction product for the enzyme activity was seen in the endoplasmic reticulum and nuclear envelope in secretory epithelial cells from all animals examined (days 7 and 14 of pregnancy, and days 0, 3, 10, and 20 of lactation. The amounts of the reaction product appeared scarce at day 7 of pregnancy, moderate at day 14 of pregnancy and day 0 of lactation, and abundant at days 3 and 10 of lactation. The reaction product, however, became generally scarce at day 20 of lactation. Biochemical activity was relatively low at days 7 and 14 of pregnancy and days 0 and 20 of lactation, while it was high at days 3 and 10 of lactation. The increased activity is probably related to functions of secretory epithelial cells in the lactating gland.

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Cytochemical glucose-6-phosphatase activity in the cells of mouse pancreas and submandibular gland

et al. 1983

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Ultrastructural localization of glucose-6-phosphatase activity was studied in the cells of the pancreas and submandibular gland of the mouse using a incubation medium modified from that of Wachstein & Meisel (1956). In pancreatic acinar cells, the reaction product for the enzyme activity was not found even after 90 min of incubation with three changes of the medium. However, the reaction product was localized in the endoplasmic reticulum and nuclear envelope of all other cell types composing the pancreas and submandibular gland. The reaction product appeared in moderate to abundant amounts in acinar cells and striated duct cells of the submandibular gland, and in the B cells, A and D cells of the pancreatic islet, but it was scarce in other cell types.

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Preliminary observations on a glucose-6-phosphate-hydrolyzing enzyme in secretory cells: a light microscopic study

Cited by 4 publications

References 11 publications

The glucose-6-phosphatase enzyme in developing human trachea and oesophagus

The glucose-6-phosphatase enzyme in developing human trachea and oesophagus

Glucose 6‐phosphatase activity in pregnant and lactating mammary glands of the mouse

Cytochemical glucose-6-phosphatase activity in the cells of mouse pancreas and submandibular gland

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