PubMed Health⌕ Search

Biomedical subjects

W J Bruin

Publications and source records attributed to W J Bruin.

4 recordsLinked to original sources

Acute inhibition of mineralization and stimulation of bone resorption mediated by hypophosphatemia.

Using rats previously labeled with 45Ca, the effects of a severely phosphate deficient diet on calcium mobilization from bone into serum were examined in both intact and thyroparathyroidectomized (TPTX) RATS. With the TPTX animals, increased calcium mobilization from bone was evident 12 hr after the rats had been placed on the low phosphorus diet. At that time period, both TPTX and intact rats had become severely hypophosphatemic. However, in intact rats, calcium mobilization was not observed until 48 hr had elapsed. Both intact and TPTX hypophosphatemic rats developed hypercalcemia. To determine if inhibition of calcium deposition into bone contributed to this change, the course of 45Ca movement from blood into bone was followed in an experiment where rats received a single injection of the isotope at the time the low phosphorus diet was given. The animals on the low phosphorus diet showed a significantly lower bone specific activity and a higher serum specific activity compared to the control group, indicating calcium deposition into bone was inhibited. We conclude that the acute response to hypophosphatemia, resulting from the low phosphorus dietary regimen, was an increase in bone resorption and an inhibition of bone mineralization. The increase in bone resorption occurred more rapidly in TPTX rats than in the intact animals.

Animals↗

Glycolate pathway in green algae.

By three criteria, the glycolate pathway of metabolism is present in unicellular green algae. Exogenous glycolate-1-(14)C was assimilated and metabolized to glycine-1-(14)C and serine-1-(14)C. During photosynthetic (14)CO(2) fixation the distributions of (14)C in glycolate and glycine were similar enough to suggest a product-precursor relationship. Five enzymes associated with the glycolate pathway were present in algae grown on air. These were P-glycolate phosphatase, glycolate dehydrogenase (glycolate:dichloroindophenol oxidoreductase), l-glutamate:glyoxylate aminotransferase, serine hydroxymethylase, and glycerate dehydrogenase. Properties of glycerate dehydrogenase and the aminotransferase were similar to those from leaf peroxisomes. The specific activity of glycolate dehydrogenase and serine hydroxymethylase in algae was 1/5 to 1/10 that of the other enzymes, and both these enzymes appear ratelimiting for the glycolate pathway.Labeling patterns for products of the glycolate pathway during (14)CO(2) fixation are not the same as those obtained with higher plants. In higher plants glycolate, glycine, and serine are uniformly labeled at shortest time periods. In algae, serine was predominately carboxyl-labeled, similarly to 3-phosphoglycerate. This result, plus the lower specific activity of serine hydroxymethylase, indicates that the glycine-serine interconversin in algae is slower than in plants. Initially (2 to 4 seconds) glycolate and glycine were more C-2 labeled. They rapidly became uniformly labeled, with glycine becoming uniformly labeled first. In the presence of isonicotinylhydrazide, labeled glycolate and glycine accumulated, and only a trace of serine-(14)C was detected. Then glycolate and glycine were initially carboxyl-labeled, and glycolate became uniformly labeled almost immediately and before glycine. These results suggest rapid metabolism of glycolate and glycine, in addition to the glycolate pathway.

Journal Article↗