The subcellular distribution of rat liver serine-pyruvate aminotransferase

Rowsell, Kathleen V.; Al-Naama, Lamia M.; Benett, P

doi:10.1042/bj2020483

Biochemical Journal

1982

DOI: 10.1042/bj2020483

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The subcellular distribution of rat liver serine-pyruvate aminotransferase

Kathleen V. Rowsell¹,

Lamia M. Al-Naama²,

P Benett³

Abstract: 1. The subcellular distribution of L-serine-pyruvate aminotransferase activity in rat liver was investigated. About 80% was recovered from cell-free homogenates in a 'total-particles' fraction and the remainder in the cytosol. 2. Subfractionation of the particles by differential sedimentation and on sucrose density gradients showed a distribution for serine-pyruvate aminotransferase activity closely matching that observed for mitochondrial marker enzymes. 3. A study of the solubilization of enzymes from combin… Show more

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Cited by 4 publications

References 23 publications

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Quantitative immunocytochemical studies on differential induction of serine

Yokota¹

1986

Histochemistry

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Differential induction of serine: pyruvate amino-transferase (SPT) in rat liver parenchymal cells by administration of glucagon or di-(2-ethylhexyl)phthalate (DEHP) was studied using post-embedding immunocytochemical techniques and morphometric methods. Two groups of rats were fasted for 5 days and daily received peritoneal injection of glucagon (300 micrograms/100 g) or physiological saline. Another two groups of rats were fed on laboratory chow with or without 2% DEHP for 2 weeks. Livers were perfusion-fixed, cut into tissue sections (50-100 micron), and processed to cytochemistry for catalase, immunocytochemistry for SPT, and conventional procedures for electron microscopy. The morphometric analysis showed that glucagon injection has negligible effect on the volume and numerical density and mean diameter of peroxisomes, whereas volume density of mitochondria was decreased by 25%. By DEHP administration peroxisomes were about 3-fold increased in the volume and numerical density. Mitochondria was increased about 40% in the numerical density, but unchanged in the volume density. Light and electron microscopic immunocytochemistry demonstrated that glucagon injection exclusively enhanced mitochondrial SPT, whereas DEHP administration exclusively induced in peroxisomal SPT. Quantitative analysis showed that by the glucagon injection, the labeling density of mitochondria was increased about 4-fold, but that of peroxisomes was 1.6 times as much as control, while by DEHP administration, the labeling density of peroxisomes was enhanced about 3-fold but that of mitochondria was decreased by 13%. The results clearly indicate that glucagon induces mitochondrial SPT, whereas peroxisome proliferator, DEHP induces peroxisomal SPT.

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Quantitative immunocytochemical studies on differential induction of serine

Yokota¹

1986

Histochemistry

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Enzymes of serine metabolism in normal, developing and neoplastic rat tissues

Snell

1984

Advances in Enzyme Regulation

262

234

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Control of Hepatic Utilization of Serine, Glycine and Threonine in Fed and Starved Rats

Rémésy¹,

Fafournoux²,

Demigné³

1983

The Journal of Nutrition

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Effects of varying protein level on hepatic utilization of serine, threonine and glycine were examined by measurements of metabolic fluxes across the liver. Feeding a high protein (HP) diet markedly enhanced hepatic extraction of serine, threonine and glycine, in parallel to alanine. After 20 hours starvation, activity of alanine aminotransferase and serine dehydratase still reflected the induction of these enzymes in fed rats. Thus, in starved rats previously adapted to HP diets, hepatic uptake of serine, threonine and glycine remained very efficient. With a normal diet, gluconeogenesis from alanine may be very active during starvation, in contrast to serine. The present results suggest that serine, and, to a lesser extent glycine, are very efficient glucogenic substrates with HP diets. The serine aminotransferase pathway might be important in rats fed HP diets, particularly for utilization of serine synthesized from glycine in mitochondria. With HP diets, the drop in hepatic alanine, serine and threonine suggest that transport across the plasma membrane might limit their utilization.

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The subcellular distribution of rat liver serine-pyruvate aminotransferase

Cited by 4 publications

References 23 publications

Quantitative immunocytochemical studies on differential induction of serine

Quantitative immunocytochemical studies on differential induction of serine

Enzymes of serine metabolism in normal, developing and neoplastic rat tissues

Control of Hepatic Utilization of Serine, Glycine and Threonine in Fed and Starved Rats

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