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Biomedical subjects

R E Kane

Publications and source records attributed to R E Kane.

At least 37 records · Page 2Linked to original sources
PubMed1989

Glucose intolerance with low-, medium-, and high-carbohydrate formulas during nighttime enteral feedings in cystic fibrosis patients.

Ten young adult cystic fibrosis (CF) patients over 16 years of age (average 21.4 years) began nighttime enteral feedings as a method of nutritional rehabilitation to regain and maintain body weight. Patients received nighttime feedings of 1,000 kcal/M2 of a low- (Pulmocare), medium- (Ensure Plus), or high-carbohydrate (Vivonex) formula for at least 2 nights each with pancreatic enzyme therapy. Five of ten young adult CF patients developed nocturnal hyperglycemia (serum glucose greater than 300 mg/dl) and glucosuria (1-3% glucose) with varying degrees of polyuria during enteral feedings. No patient developed ketonuria despite serum glucoses at times greater than 600 mg %. There was no difference between the hyperglycemic and normoglycemic groups in median age, percent of ideal body weight, NIH score, Brasfield scores, pulmonary function tests, or family history of diabetes. All normoglycemic and four of five hyperglycemic patients had normal fasting blood sugars. The percent hemoglobin A1c was greater in the glucose intolerant group than the normoglycemic patients (11.2 +/- 0.8% vs. 6.8 +/- 1.1%, mean +/- SE, p less than 0.005). Twelve to 15 units of NPH insulin prior to initiation of feedings provided adequate therapy in most hyperglycemic patients. There was no apparent difference in the elevation of early morning serum glucoses with the low- medium- and high-carbohydrate formulas. We concluded that hyperglycemia requiring insulin therapy was common in young adult CF patients using nighttime enteral feedings. A hemoglobin A1c appeared to be a useful screening test before initiating such therapy.

Adult↗
PubMed1989

Initial results of a program in liver transplantation.

St. Louis University established a liver transplant program in early 1988. The authors report on the program's first 10 months in operation, emphasizing the careful planning and cooperation the medical center must undertake to ensure the program's success.

Female↗
PubMed1989

Perinatal cimetidine exposure has no apparent effect on hepatic drug oxidative or conjugative activity in adult male rat offspring.

UNLABELLED: Perinatal exposure of male rat pups to cimetidine has been reported to 'feminize' gonadal and sexual function and to reduce serum testosterone in adult male offspring. This study examined whether perinatal cimetidine exposure altered the androgen 'imprinting' of sex differences in mature male hepatic biotransformation capacities. During the perinatal period, dams were infused with cimetidine (18 mg/kg/day) through Alzet osmotic pumps placed subcutaneously beginning at 10 days of gestation. Pump function was confirmed by weekly high-performance liquid chromatographic analysis of maternal urine for unchanged cimetidine. Male pups were culled at birth with continued exposure to cimetidine in breast milk until weaning. At about 100 days of age, in vitro and in vivo drug oxidative and conjugative activities were measured in mature males. Early cimetidine exposure did not alter hepatic oxidative (cytochrome P-450 content or monooxygenase activity) or conjugative (UDP-glucuronosyltransferase activity towards testosterone, morphine, 1-naphthol, estrone, or sulfotransferase activity towards acetaminophen or glycolithocholate) capacities in mature males. Two sulfotransferase isoenzyme activities (acetaminophen sulfotransferase 2 and bile salt sulfotransferase I) previously shown to be regulated by gonadal hormones were also unchanged. Serum testosterone was unaffected by perinatal cimetidine exposure. Moreover, there were no effects of perinatal cimetidine exposure on in vivo pharmacokinetics or metabolic fate of acetaminophen. CONCLUSION: Perinatal exposure of male pups to doses of cimetidine similar to those used in humans did not appear to affect the imprinting of sex differences on in vitro hepatic drug metabolism or elimination kinetics of acetaminophen.

Acetaminophen↗
PubMed1988

Cost savings and economic considerations using home intravenous antibiotic therapy for cystic fibrosis patients.

Our Cystic Fibrosis (CF) Center made an effort to utilize home intravenous antibiotic therapy (HIVAT) as an alternative to continued hospitalization during a 1-year study. After thorough individual clinical and financial evaluation, 27 of 41 CF patients admitted for treatment, including antibiotic therapy, were selected for HIVAT to complete a 14- to 21-day treatment course (mean 15.1 days). The 27 patients (6-28 years old, mean 16 years) incurred a total of $698,587 in hospital charges and physician fees during 96 admissions. The average charge for 974 inpatient days was $717/day ($7,280 per admission). After an average of 10.2 days of inpatient care, the 27 patients underwent 79 courses of HIVAT for an additional 8 days; 21 additional HIVAT courses in six of these patients were initiated on an outpatient basis between frequent readmissions. The 811 days of HIVAT resulted in $85,027 total charges by two home care companies. The charges per day of HIVAT by one company were almost twice that of the other. The average daily cost of HIVAT was $108/day. If the HIVAT patients had remained hospitalized to complete the course of intravenous antibiotic therapy, the projected inpatient costs would have been $589,271. Therefore, the 811 days of HIVAT over a 1-year period resulted in total estimated direct cost savings of $501,770. The average savings per course of HIVAT was $5,017, or $618/day.(ABSTRACT TRUNCATED AT 250 WORDS)

Adolescent↗
PubMed1988

Sexual differentiation of rat hepatic bile salt sulfotransferase isoenzymes.

The mature female rat has three times the hepatic bile salt sulfotransferase (BSS) activity compared with male rats. This study examined the changes in two hepatic BSS isoenzyme activities during sexual maturation, and the role of estrogen in development of sex differences in BSS activities in mature rats. DEAE-Sephadex A-50 chromatography of hepatic cytosol from prepubescent pups revealed that more than 90% of total BSS activity was due to BSS I activity relative to BSS II, similar to postpubertal females. Sex differences in total BSS activities and the isoenzyme patterns developed after the onset of puberty at 30-35 days of age. BSS I was still the predominant isoenzyme in the adolescent female, similar to the prepubescent pup and mature female. In contrast, BSS I activity declined in adolescent males, which appeared to explain the fall in total BSS activity to only one-third of that of the female by maturity. BSS II activity was similar in both sexes at any age. Estrogen treatment of postpubertal male rats rapidly increased hepatic BSS capacity by enhancing BSS I activity producing an isoenzyme pattern similar to the mature female. This rapid enhancement of BSS I by estrogen was blocked by actinomycin D and puromycin. We concluded that 1) sex differences in BSS activities that develop during adolescence were in part due estrogen-maintaining BSS I activity in females and 2) estrogen regulates the synthesis of BSS I at a translational (or pretranslational) level.

Animals↗
PubMed1987

A 250K-molecular-weight actin-binding protein from actin-based gels formed in sea urchin egg cytoplasmic extract.

The actin-based gel formed at 35 degrees C in the cytoplasmic extract from eggs of a sea urchin, Tripneustes gratilla, contains several high-molecular-weight proteins. Among them, the 250K-molecular-weight protein was isolated and characterized. This protein migrated slightly more slowly than filamin from chicken gizzard upon polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. It reacted only very weakly with antibodies against chicken gizzard filamin or against a high-molecular-weight actin-binding protein from Physarum plasmodia. It did not react with antibodies against chicken erythrocyte alpha-spectrin nor against the 220K protein from the same egg. A chemical crosslinking experiment revealed the presence of dimers in the purified 250K protein preparation. A rotary shadowed specimen of such a preparation showed wavy single-stranded molecules 120-170 nm long, having five to six globular domains, which may represent dimers. The appearance was different from that of spectrin or actin-binding protein from macrophage or chicken gizzard filamin. This protein increased the viscosity of F-actin solution. It bound to F-actin preferably at low KCl concentrations such as 20 mM. The binding ability was not influenced by pH between 6.0 and 7.5, although it was somewhat reduced above pH 8.0. The binding was insensitive to low Ca ion concentrations. Electron microscopy using the negative staining technique supported the idea that this protein crosslinks actin filaments. In addition, a second protein from egg gels, with a reported molecular weight of about 220K (Kane, R.E., J. Cell Biol. 66, 305-315 (1975)), comigrated with human erythrocyte alpha-spectrin on an SDS-gel and reacted with antibodies against chicken erythrocyte alpha-spectrin. This suggests that this protein is a sea urchin egg spectrin. The role of these proteins in the cytoskeleton formation in the sea urchin egg is discussed.

Animals↗
PubMed1986

TAME stabilizes the cortex and mitotic apparatus of the sea urchin egg during isolation.

The synthetic substrate p-tosyl-L-arginine methyl ester (TAME) has been included in buffered EGTA media used for the isolation of the mitotic apparatus from clam eggs and also for the isolation of the cortex from sea urchin eggs. In the course of an investigation of the role of actin-fascin and actin-myosin interactions in cytokinesis, the isolation of the sea urchin egg cortex was re-examined and the stability of the cortex to lysis in a buffered EGTA medium near neutrality found to depend directly on the presence of TAME. Lysis of eggs at metaphase in this medium yielded a mixture of cortices and mitotic apparatuses (MA); MA stability under these conditions also required the presence of TAME, although a reduced pH allowed MA isolation in its absence. The action of TAME in stabilizing the actin-based structure of the cortex and the microtubule-based structure of the MA is not duplicated by other proteolysis inhibitors and this compound will also induce actin polymerization and gelation in extracts of the soluble cytoplasmic proteins of the egg under conditions where these are normally inhibited.

Actins↗
PubMed1986

Effect of aging on drug-metabolizing enzymes important in acetaminophen elimination.

The effects of aging on selected drug-metabolizing enzyme activities, the pattern of phenol and bile salt sulfotransferase isoenzymes and the pharmacokinetics of acetaminophen were examined in male Fischer 344 rats at ages 5, 14 and 25 months. Aging decreased sulfotransferase activity toward acetaminophen while activity toward glycolithocholate increased with age. Glucuronosyltransferase activity toward estrone increased with age, while activity toward testosterone, morphine and naphthol remained constant. Glutathione-S-transferase (1-chloro-2,4-dinitrobenzene) activity was also unchanged through the various age groups. Cytochrome P-450 content and monooxygenase activity (p-nitroanisole demethylation) activity decreased with advancing age. Overall, the age-related in vitro changes in enzyme activities approached or equaled values measured in 5-month-old female Fischer 344 rats. Moreover, age-related alterations in total phenol sulfotransferase activity and the isozyme pattern paralleled changes in the in vivo elimination kinetics and metabolic fate of acetaminophen. The fraction of drug excreted as the sulfate conjugate and the partial clearance to acetaminophen sulfate decreased with increasing age. Conversely, the fraction excreted as the glucuronide and the partial clearance to acetaminophen glucuronide increased with increasing age. There was no effect of aging on the total clearance of acetaminophen. The gender-related differences in the pattern of sulfotransferase isozyme activity toward phenolic and bile salt acceptors disappeared with age. Age-related changes in sulfation and perhaps glucuronidation in male rats appear to feminize hepatic biotransformation and may arise due to altered gonadal hormone status.

Acetaminophen↗
PubMed1984

An efficacy trial of doxycycline chemoprophylaxis against leptospirosis.

Because leptospirosis has been an important cause of morbidity in U.S. soldiers training in the Republic of Panama, we conducted a randomized, double-blind, placebo-controlled field trial during the fall of 1982 to determine whether doxycycline was an effective chemoprophylactic agent against this infection. Doxycycline (200 mg) or placebo was administered orally on a weekly basis and at the completion of training to 940 volunteers from two U.S. Army units deployed in Panama for approximately three weeks of jungle training. Twenty cases of leptospirosis occurred in the placebo group (an attack rate of 4.2 per cent), as compared with only one case in the doxycycline group (attack rate, 0.2 per cent, P less than 0.001), yielding an efficacy of 95.0 per cent. This study demonstrated the value of doxycycline as a prophylactic drug against leptospirosis.

Clinical Trials as Topic↗
PubMed1983

Interconversion of structural and contractile actin gels by insertion of myosin during assembly.

Extracts of the soluble cytoplasmic proteins of the sea urchin egg form gels of different composition and properties depending on the temperature used to induce actin polymerization. At temperatures that inactivate myosin, a gel composed of actin, fascin, and a 220,000-mol-wt protein is formed. Fascin binds actin into highly organized units with a characteristic banding pattern, and these actin-fascin units are the structural core of the sea urchin microvilli formed after fertilization and of the urchin coelomocyte filopods. Under milder conditions a more complex myosin-containing gel is formed, which contracts to a small fraction of its original volume within an hour after formation. What has been called "structural" gel can be assembled by combining actin, fascin, and the 220,000-mol-wt protein in 50-100 mM KCl; the aim of the experiments reported here was to determine whether myosin could be included during assembly, thereby interconverting structural and contractile gel. This approach is limited by the aggregation of sea urchin myosin at the low salt concentrations utilized in gel assembly. A method has been devised for the sequential combination of these components under controlled KCl and ATP concentrations that allows the formation of a gel containing dispersed myosin at a final concentration of 60-100 mM KCl. These gels are stable at low (approximately 10 micron) ATP concentrations, but contract to a small volume in the presence of higher (approximately 100 micron) ATP. Contraction can be controlled by forming a stable gel at low ATP and then overlaying it with a solution containing sufficient ATP to induce contraction. This system may provide a useful model for the study of the interrelations between cytoplasmic structure and motility.

Actins↗
PubMed1980

Redistribution of actin and fascin in sea urchin eggs after fertilization.

Following fertilization, the sea urchin egg cortex undergoes a structural change involving the assembly and organization of actin filaments into microvilli. Antifascin localizes this actin cross-linking protein in the microvilli of the fertilized egg cortex but no organized staining is present in the unfertilized cortex. Determination of the actin content of eggs using the DNAase I inhibition assay indicates that actin is about 1.4% of the total protein. Approximately 90% of this actin is soluble in low calcium isotonic extracts of unfertilized eggs while only 60-65% can be recovered in identical extracts of fertilized eggs. Similar measurements for fascin using a radioimmunoassay indicate this molecule represents about 0.3% of the total egg protein, essentially all of which is recovered in low calcium isotonic extracts of unfertilized eggs. After fertilization only 65-70% of this actin cross-linking protein is in the soluble phase. These results demonstrate a markedly different solubility for actin and fascin after fertilization, when the indirect immunofluorescence staining localizes fascin in the microvilli, and are consistent with the idea that fascin organizes newly polymerized actin filaments into the microvillar cores. A consideration of the amounts of actin and fascin incorporated into the cortex after fertilization and the number of microvilli on the egg surface indicates that the measured values are sufficient to account for the observed microvillar elongation.

Actins↗
PubMed1980

Induction of either contractile or structural actin-based gels in sea urchin egg cytoplasmic extract.

The gel formed by warming the 100,000 g supernate of isotonic extracts of sea urchin eggs to 40 degrees C is made up of actin and two additional proteins of mol wt of 58,000 and 220,000. Actin and 58,000 form a characteristic structural unit which has now been identified in the microvilli of the urchin egg and in the filopods of urchin coelomocytes. However, egg extract gels did not contract as those from other cell types do, and the aim of these experiments was to determine the reason for this lack of contraction. Although the extracts are dialyzed to a low ionic strength, myosin is present in soluble form and makes up approximately 1% of the protein of the extract. It becomes insoluble in the presence of high ATP concentrations at 0 degrees C, and the precipitate formed under these conditions consists almost entirely of myosin. This procedure provides a simple method of isolating relatively pure myosin without affecting other extract components and functions. Contraction will follow gelation in these extracts if the temperature and time of incubation used to induce actin polymerization are reduced to minimize myosin inactivation. At the optimal ATP and KCl concentration for contraction, the contracted material has an additional 250,000 component and contains very little 58,000. The conditions found to provide maximum gel yields favor the formation of the actin-58,000-220,000 structural gel, while reduced temperature and increase in KCl concentration results in a contractile gel whose composition is similar to those reported from amoeboid cell types. Both the structural protein cores found in the egg microvilli and a gel contraction related to the amoeboid motion which is seen in later urchin embryonic development can thus be induced in vitro in the same extract.

Actins↗