Perspectives. Clinton unveils Medicare cuts; health groups hold their fire.
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Biomedical subjects
Publications and source records attributed to C Kent.
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We describe herein the expression and purification of milligram quantities of rat liver CTP:phosphocholine cytidylyltransferase in recombinant baculovirus-infected insect cells. The enzyme was purified by incorporating modifications to a previously published procedure (P. A. Weinhold and D. A. Feldman, 1992, in "Methods in Enzymology" (E. A. Dennis and D. E. Vance, Eds.), Vol. 209, pp. 248-258, Academic Press, San Diego, CA). Like cytidylyltransferase purified from rat liver, the purified recombinant cytidylyltransferase has the same molecular weight (42 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and reacts to antibodies generated against the N and C termini of rat liver cytidylyltransferase. In addition, like the purified rat liver enzyme, the recombinant cytidylyltransferase is activated by lipids. We also expressed rat liver cytidylyltransferase as a fusion protein with glutathione-S-transferase and with a thrombin cleavage site between the two enzymes for rapid isolation of cytidylyltransferase. Thrombin cleavage was, however, incomplete and prolonged exposure to thrombin resulted in the degradation of cytidylyltransferase itself.
A 3-year-old boy with a radiographic finding of an isolated invaginated Meckel's diverticulum is presented. The abnormality simulates a polypoid filling defect in the distal small bowel on barium examination. This particular manifestation of Meckel's diverticulum is very rare and has been reported only once previously. This article re-emphasizes the need to think about this possibility when a polypoid filling defect is seen in the distal small bowel. At the time laparotomy was performed, the abnormality had progressed into a triple intussusception, a rare surgical finding.
The rat adrenal medulla is immature at birth, composed of phaeochromoblasts and undifferentiated chromaffin cells, but by 7 d postnatally morphologically distinct adrenaline-storing (A) and noradrenaline-storing (NA) cells can be distinguished in the adult proportions of approximately 80-85% A and 15-20% NA cells. Glucocorticoid hormones are known to play an important role in the initial expression and maintenance of phenylethanolamine N-methyl transferase (PNMT), the enzyme characteristic of A cells. The purpose of the study was to investigate the effects of glucocorticoids on the establishment of the A and NA cell phenotype in vivo during the first postnatal week. Neonatal rats were treated from postnatal d 1 to 7 either with ACTH to increase circulating levels of glucocorticoids or with aminoglutethimide to reduce blood glucocorticoids. On postnatal d 7 the volume fractions of A and NA cells in the adrenal medulla were estimated and the amounts of stored adrenaline and noradrenaline determined by HPLC and compared with untreated controls. Adrenaline levels were increased following ACTH treatment and there was an apparent decrease after aminoglutethimide which was not statistically significant. There was cytological evidence of the effects of ACTH and aminoglutethimide on the adrenal cortex but no resultant effect on medullary cell morphology. A cells remained predominant with NA cells making up approximately 15% of chromaffin cells, suggesting that any effects of altered glucocorticoid levels were confined to a modulation of adrenaline synthesis by a morphologically unchanged chromaffin cell population.(ABSTRACT TRUNCATED AT 250 WORDS)
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Protein gene product (PGP9.5) has been detected by means of immunocytochemistry in the rat fetus in intra- and extra-adrenal chromaffin cells (E12.5), pancreatic islet cells (E12.5), anterior pituitary cells (E14.5), carotid body chief cells (E15.5), thyroid C cells (E17.5) and respiratory neuroendocrine bodies (E15.5). It was expressed early in ontogenesis coincidental with other known morphological and biochemical signs of differentiation.