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Biomedical subjects

K M Jones

Publications and source records attributed to K M Jones.

At least 55 records · Page 3Linked to original sources
PubMed1987

Phenytoin absorption from tube feedings.

Phenytoin, administered by suspension into a feeding tube through which continuous enteral feedings are being given, is very poorly absorbed. There appears to be very little information regarding this potentially serious problem in the general medical literature. Commonly used doses of phenytoin (300 to 500 mg/d) may result in almost undetectable serum levels. Therapeutic phenytoin levels may be obtained if a very large dose of the drug is given. Our patient required 1800 mg daily in two divided doses to get a serum phenytoin level of 9 micrograms/mL. Commonly used enteral feedings were being delivered by way of a continuous infusion pump. We found one enteral feeding product that did not severely impair the absorption of phenytoin. The mechanism by which enteral feedings impair phenytoin absorption is unknown.

Cerebral Hemorrhage↗
PubMed1987

Mammary masses in the adolescent female.

Disease of the breast is uncommon in the adolescent female. Of 25,650 surgical specimens examined at The Children's Memorial Hospital in Chicago from 1974 through 1985, only 40 lesions were of adolescent breast origin in females. The ages of the patients ranged from 12 to 22 years. The most common lesion was fibroadenoma (19) followed by gigantomastia and cystosarcoma phyllodes. A malignant lesion is rare in this age group and both instances in this series had predisposing factors (for example, prior regional radiation in childhood). The findings of this study, plus that of the literature reviewed, emphasize conservative treatment with observation followed by simple excision when the patient nears completion of the development of the breast in most instances.

Adenofibroma↗
PubMed1985

Complexes of low-density lipoproteins and arterial proteoglycan aggregates promote cholesteryl ester accumulation in mouse macrophages.

We studied the effect of complexes of low-density lipoproteins (LDL) and different proteoglycan preparations from bovine aorta on LDL degradation and cholesteryl ester accumulation in mouse peritoneal macrophages. Native proteoglycan aggregate containing proteoglycan monomers, hyaluronic acid and link protein was isolated by associative extraction of aortic tissue, while proteoglycan monomer was obtained by dissociative isopycnic centrifugation of the native proteoglycan aggregate. In vitro proteoglycan aggregates were prepared by reaction of the proteoglycan monomer with exogenous hyaluronic acid. 125I-labeled LDL-proteoglycan complexes were formed in the presence of 30 mM Ca2+ and incubated with macrophages. At equivalent uronic acid levels in the proteoglycans the degradation of 125I-labeled LDL contained in the native proteoglycan aggregate complex was 3.7-7.5-fold greater than the degradation of the lipoprotein in the proteoglycan monomer complex. Degradation of 125I-LDL in the in vitro aggregate complex, while higher than that in the monomer complex, was markedly less than that in the native aggregate complex. The larger size and the greater complex-forming ability of the native proteoglycan aggregate might account for the greater capacity of the aggregate to promote LDL degradation in macrophages. The proteoglycan-stimulated degradation of LDL produced a marked increase in cholesteryl ester synthesis and content in macrophages. The LDL-proteoglycan complex was degraded with saturation kinetics, suggesting that these complexes are internalized through high-affinity receptors. Degradation was inhibited by the lysosomotropic agent, chloroquine. Acetyl-LDL, but not native LDL, competitively inhibited the degradation of the 125I-LDL component of the complex. Polyanionic compounds such as polyinosinic acid and fucoidin, while completely blocking the acetyl-LDL-stimulated cholesteryl ester formation, had no effect on the proteoglycan aggregate-stimulated cholesterol esterification. This suggests that LDL-proteoglycan complex and acetyl-LDL are not entering the cells through the same receptor pathway. These results demonstrate that the interaction of LDL with arterial wall proteoglycan aggregates results in marked cholesteryl ester accumulation in macrophages, a process likely to favor foam cell formation. A role for arterial proteoglycans in atherosclerosis is obvious.

Animals↗
PubMed1977

L-serine dehydratase from Arthrobacter globiformis.

1. L-Serine dehydratase (EC 4.2.1.13) was purified 970-fold from glycine-grown Arthrobacter globiformis to a final specific activity of 660micronmol of pyruvate formed/min per mg of protein. 2. The enzyme is specific for L-serine; D-serine, L-threonine and L-cysteine are not attacked. 3. The time-course of pyruvate formation by the purified enzyme, in common with enzyme in crude extracts and throughout the purification, is non-linear. The reaction rate increases progressively for several minutes before becoming constant. The enzyme is activated by preincubation with L-serine and a linear time-course is then obtained. 4. The substrate-saturation curve for L-serine is sigmoid. The value of [S]0.5 varies with protein concentration, from 6.5mM at 23microng/ml to 20mM at 0.23microng/ml. The Hill coefficient remains constant at 2.9.5 The enzyme shows a non-specific requirement for a univalent or bivalent cation. Half-maximal activity is produced by 1.0mM-MgCl2 or by 22.5mM-KCl. 6. L-Cysteine and D-serine act as competitive inhibitors of L-serine dehydratase, with Ki values of 1.2 and 4.9mM respectively. L-Cysteine, at higher concentrations, also causes a slowly developing irreversible inhibition of the enzyme. 7. Inhibition by HgCl2 (5micronM)can be partially reversed in its initial phase by 1mM-L-cysteine, but after 10 min it becomes irreversible. 8. In contrast with the situation in all cell-free preparations, toluene-treated cells of A. globiformis form pyruvate from L-serine at a constant rate from the initiation of the reaction, show a hyperbolic substrate-saturation curve with an apparent Km of 7mM and do not require a cation for activity.

Arthrobacter↗