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PubMed1992

A microcomputer program for determining turnover rates during non-steady state conditions: application to monoamine turnover.

A program to calculate the turnover rate of monoaminergic neurotransmitters was written for use on microcomputers. The program is based on non-steady state models, i.e., measuring the rate of change of levels of neurotransmitters or their metabolites after pharmacological inhibition of synthetic or degradative enzymes. Methods have been developed to estimate monoamine turnover by measuring the rate of decrease of catecholamine levels after treatment with alpha-methyl-p-tyrosine (AMPT), a tyrosine hydroxylase inhibitor, or the increase in serotonin levels after pargyline, an inhibitor of monoamine oxidase. This program is suitable for examining either linear increases or exponential decreases in monoamine levels. The program has been tested in our laboratory for the determination of serotonin, dopamine or norepinephrine turnover after hormonal or pharmacological manipulations. The program is readily adaptable for calculation of the turnover rate of other biological molecules under non-steady state conditions.

Biogenic Monoamines↗

PubMed1970

Turnover of mammalian phospholipids. Rates of turnover and metabolic heterogeneity in cultured human lymphocytes and in tissues of healthy, starved and vitamin A-deficient rats.

1. Choline- and inositol-labelled phospholipids of human cultured lymphocytes turn over in a biphasic manner; phytohaemagglutinin activation stimulates turnover. 2. Choline-labelled phospholipids of rat liver and kidney, but not of blood, turn over in vivo as fast as those of duodenum, ileum or colon. Turnover in the intestinal tissues is greater in fed than in starved or vitamin A-deficient rats. In each case phosphatidylcholine turns over relatively faster than sphingomyelin or lyso-phosphatidylcholine. 3. It is concluded that phospholipid turnover of the type described is a common feature of viable cells, and that metabolically favourable conditions increase, rather than decrease, turnover.

Animals↗

PubMed1989

Turnover of Ia-peptide complexes is facilitated in viable antigen-presenting cells: biosynthetic turnover of Ia vs. peptide exchange.

Macrophages and B cells process antigens to produce antigenic peptides that associate with class II major histocompatibility complex molecules (e.g., Ia molecules); these Ia-peptide complexes are recognized by CD4+ T lymphocytes. Processing of the antigen hen egg white lysozyme was inhibited by cycloheximide in peritoneal exudate cells (PECs, largely macrophages), but not in TA3 B-lymphoma cells. The uptake and metabolism of hen egg white lysozyme was largely intact in cycloheximide-treated PECs, implicating a blockade in other steps in the formation of Ia-peptide complexes. Turnover of Ia-peptide complexes was markedly enhanced in viable antigen-presenting cells (TA3 and PEC) as compared to such complexes studied on fixed cells or in isolated preparations of Ia and peptide. In B cells the half-life of Ia-peptide complexes was much shorter than the half-life of the Ia molecules, implying turnover of Ia-peptide complexes by dissociatin and peptide exchange. In PECs, the dissociation of Ia-peptide complexes was more limited; the enhanced Ia-peptide turnover in viable PECs reflected in part biosynthetic turnover of Ia molecules. Specific mechanisms may exist in TA3 cells to facilitate exchange of peptides bound to Ia, allowing recycling of Ia to present another antigenic peptide; such Ia recycling would explain the ability of these cells to process and present antigen in the absence of Ia synthesis.

Animals↗

PubMed2000

Measurement of water turnover using deuterium dilution: impact of periodically varying turnover rates on precision and accuracy.

Water metabolism may be non-invasively investigated using deuterium elimination from the body. Evaluation of elimination constants (kD) and pool sizes (N) becomes complicated when turnover rates vary periodically--a realistic scenario in free-living subjects. Unfortunately, phase and frequency of periodic variations are not a priori known and can therefore not be used for a sampling protocol. This study investigates the impact of periodical flux variations on the measurement of water turnover. For two models of periodic variation with identical apparent kD, data sets of tracer concentrations in body water were generated for two-hour intervals using a monoexponential decay equation. Data were analyzed using the two- and the multi-point method increasing observation periods stepwise. Apparent values for kD, N and water turnover (R(H2O)) were compared with values originally used in the model. Periodically varying turnover rates introduce considerable errors for kD and R(H2O) when the two-point method is used. The multi-point method gives a more robust estimate of R(H2O) already after short observation periods, however, due to slope-intercept correlations, still tends to overestimate R(H2O). Errors are more pronounced the more uneven flux rates are distributed. Stepwise analysis of tracer enrichments using the multi-point approach identifies periodical variation of flux rates.

Deuterium↗

PubMedDate not supplied

Turnover rates of muscle proteins in cardiac, skeletal, and smooth muscle: turnover rate related to muscle function.

The turnover rate of muscle proteins was related to the physiological function of the muscle in dogs, fowl, rats, and mice. The turnover rates of mixed muscle proteins were most rapid in cardiac muscle, intermediate in red tonic and mixed fiber-type muscles, and slowest in white twitch skeletal muscle. This same progression in turnover rates also was shown in the subcellular fractions of muscle-sarcoplasmic and myofibrillar proteins-as well as in purified proteins, myosin, and tropomyosin. The RNA concentration of muscle was highly correlated with the protein turnover rate, and the RNA activity, i.e., the translational efficiency of the RNA, was similar in the different muscle types.

Animals↗

PubMed1975

Turnover of the cell wall peptidoglycan of Lactobacillus acidophilus. The presence of a fraction immune to turnover.

Exponentially growing cultures of Lactobacillus acidophilus strain 60AM Gasser were previously shown to lose about one-third of their cell wall peptidoglycan per generation via turnover (Boothby, D., Daneo-Moore, L., Higgins, M. L., Coyette, J., and Shockman, G. D. (1973) J. Biol. Chem. 248, 2161-2169). We now show that 20 to 30% of the [3H]lysine initially present in insoluble peptidoglycan fractions was retained after 4 or more generations of continued exponential growth of cultures in the absence of label. Treatment of peptidoglycan fractions, before and after 6 or 8 generations of chase with lysozyme (EC 3.2.1.17), released soluble products containing [3H]lysine which had electrophoretic mobilities identical with the disaccharide-peptide derivatives obtained from the wall peptidoglycan of this species. Because protein is known to contaminate peptidoglycan residues, the double labeled technique was used to show that one-half or less of the label lysine present after 6 or 8 generations of chase could be attributed to protein contamination. This then left a minimum fraction of 10 to 20% of the peptidoglycan that was immune to turnover. The absence of turnover of peptidoglycan labeled during short pulses has now been quantitated to show that pulses shorter than 12% of a generation (6 to 7 min) did not turn over. This turnover-immune fraction is in reasonably good agreement with the immune fraction of 10 to 20% observed after long periods of chase of extensively labeled peptidoglycan.

Amino Acids↗

PubMed1980

Turnover of proteins in asporogenic Bacillus megaterium. Evidence for a gradual decrease of the turnover rate.

The rate of protein turnover in asporogenic Bacillus megaterium decreases continuously during incubation in a sporulation medium. The capability of equilibration of external amino acids with amino acids in the metabolic pool of non-growing cells was retained for at least 5 h. Leucine, while repressing the synthesis of the exocellular protease, does not significantly influence the course of protein degradation in vivo. Transfer of non-growing cells after 4 h to a fresh sporulation medium does not influence the rate of protein degradation. The gradual decrease of the rate of protein turnover in non-growing cells of the asporogenic variant is thus not an artifact caused by a decreased uptake of amino acids by cells or by conditions under which the protein turnover is determined.

Amino Acids↗

PubMed1984

Luteinizing hormone-releasing hormone increases dopamine turnover in the lateral palisade zone of the median eminence and reduces noradrenaline turnover in the nuc. preopticus medialis of the hypophysectomized male rat.

By means of catecholamine fluorescence histochemistry in combination with quantitative microfluorimetry the effects of luteinizing hormone-releasing hormone (LH-RH) has been studied on the amine levels and turnover in discrete catecholamine (CA) nerve terminal populations in the hypothalamus of the hypophysectomized male rat. LH-RH highly selectively increases dopamine (DA) turnover in the lateral palisade zone of the median eminence and highly selectively reduces noradrenaline turnover in the nucleus preopticus medialis without influencing amine levels in these CA nerve terminal systems. It is suggested that the ultrashort feed-back action of LH-RH involves increased release of DA in the lateral palisade zone leading to activation of the DA receptor inhibiting LH-RH release as well as a reduced noradrenaline release in the nucleus preopticus medialis leading to a reduced excitatory influence on the LH-RH neurons at the soma-dendritic level.

Animals↗

PubMed1982

Protein turnover and proliferation. Turnover kinetics associated with the elevation of 3T3-cell acid-proteinase activity and cessation of net protein gain.

1. At least 95% of the total protein of A31-3T3 cell cultures undergoes turnover. 2. First-order exponential kinetics were used to provide a crude approximation of averaged protein synthesis, Ks, degradation, Kd, and net accumulation, Ka, as cells ceased growth at near-confluent density in unchanged Dulbecco's medium containing 10% serum. The values of the relationship Ka = Ks - Kd were : 5%/h = 6%/h - 1%/h in growing cells, and 0%/h = 3%/h - 3%/h in steady-state resting cells. 3. As determined by comparison of the progress of protein synthesis and net protein accumulation, the time course of increase in protein degradation coincided with the onset of an increase in lysosomal proteinase activity and decrease in thymidine incorporation after approx. 2 days of exponential growth. 4. After acute serum deprivation, rapid increases in protein degradation of less than 1%/h could be superimposed on the prevailing degradation rate in either growing or resting cells. The results indicate that two proteolytic mechanisms can be distinguished on the basis of the kinetics of their alterations. A slow mechanism changes in relation to proliferative status and lysosomal enzyme elevation. A prompt mechanism, previously described by others, changes before changes in cell-cycle distribution or lysosomal proteinase activity. 5. When the serum concentration of growing cultures was decreased to 1% or 0.25%, then cessation of growth was accompanied by a lower steady-state protein turnover rate of 2.0%/h or 1.5%/h respectively. When growth ceased under conditions of overcrowded cultures, or severe nutrient insufficiency, protein turnover did not attain a final steady state, but declined continually into the death of the culture.

Animals↗

PubMed1986

Effect of muscular activity on the turnover rate of actin and myosin heavy and light chains in different types of skeletal muscle. I. Changes in the turnover rate of myosin and actin during and after single-bout physical activity.

During a single-bout of 6-h swimming, myosin heavy chain (HC) and actin in m. gastrocnemius turned over more slowly than they did in the pre-exercise period, whereas the turnover rate of myosin light chain (LC) increased; 48 h after swimming, actin and myosin HC had a significantly higher turnover rate, but the turnover rate of myosin LC remained at the pre-exercise level. Exercise caused a remarkable decrease in the incorporation of the 14C leucine into actin and myosin HC, but an increase in the incorporation into myosin LC. An elevation of the synthesis rate of actin and myosin HC was observed 48 h after exercise. Myofibrillar proteinase activity at alkaline pH reached its maximum level during exercise, but the same was observed for the proteolytic activity at acid pH 6 h and at neutral pH 24 h after exercise.

Actins↗

PubMed2002

L-arginine supplementation in pigs decreases liver protein turnover and increases hindquarter protein turnover both during and after endotoxemia.

BACKGROUND: Accumulating evidence suggests that L-arginine, under conditions of septicemia, not only enhances immune function but also improves protein metabolism. OBJECTIVE: Because the effect of L-arginine administration on the protein metabolism of different organs is unknown, the aim of the study was to elucidate the effects of exogenous supplementation of L-arginine during endotoxemia on the in vivo protein metabolism of individual organs and at the whole-body level. DESIGN: Female pigs were cannulated with catheters in the aorta and the splenic, caval, portal, hepatic, and renal veins, enabling measurements across the hindquarter, portal-drained viscera, liver, and kidneys. Endotoxemia was induced by a 24-h continuous intravenous infusion of endotoxin (3 microg x kg body wt(-1) x h(-1)). At 8 h, an intravenous infusion of L-arginine was started (n = 8). Control pigs (n = 6) received L-alanine. At 24 h, blood was sampled. After cessation of the endotoxin infusion, L-arginine and L-alanine infusions were continued as a supplement in the enterally infused diet. At 48 h, blood samples were obtained during the postendotoxemic and nutritionally supported conditions. Stable isotopes were used to assess protein metabolism and phenylalanine hydroxylation. RESULTS: Both during and after the endotoxin challenge, L-arginine administration enhanced protein synthesis and degradation across the hindquarter and simultaneously reduced protein synthesis and degradation in the liver at equal rates. Protein turnover across the kidneys and portal-drained viscera remained unaffected. After endotoxemia, L-arginine infusion decreased whole-body protein turnover without affecting the net protein balance. CONCLUSION: L-Arginine administration affects protein turnover of the muscle area and the liver oppositely.

Acute-Phase Proteins↗

PubMed1989

Rapid intramolecular turnover of N-linked glycans in plasma membrane glycoproteins. Extension of intramolecular turnover to the core sugars in plasma membrane glycoproteins of hepatoma.

Plasma membrane glycoproteins of rat hepatocytes undergo a rapid terminal deglycosylation in that the terminal sugars of the oligosaccharide side chains are rapidly removed from the otherwise intact glycoproteins [Tauber, R., Park, C.S. & Reutter, W. (1983) Proc. Natl Acad. Sci. USA 80, 4026-4029]. The present paper demonstrates that this rapid intramolecular turnover of plasma membrane glycoproteins is not restricted to peripheral sugars but, in contrast to liver, in hepatoma the core sugars of the oligosaccharide chains are also involved. Intramolecular turnover was measured in Morris hepatoma 7777 in five plasma membrane glycoproteins with Mr of 85,000 (hgp85), 105,000 (hgp105), 115,000 (hgp115), 125,000 (hgp125), 175,000 (hgp175) (hgp = hepatoma glycoprotein) that were isolated and purified to homogeneity by concanavalin-A--Sepharose affinity chromatography and semipreparative SDS gel electrophoresis. Analysis of the carbohydrates of hgp85, hgp105, hgp115 and hgp125 revealed the presence of N-linked oligosaccharides containing L-fucose, D-galactose, D-mannose and N-acetyl-D-glucosamine, but only of trace amounts of N-acetyl-D-galactosamine; hgp175 additionally contained significant amounts of N-acetyl-D-galactosamine, indicating the presence of both N- and O-linked oligosaccharides. As shown by digestion with endoglucosaminidase H, the N-linked oligosaccharides of hgp105, hgp115, hgp125 and hgp175 were of the complex type, whereas hgp85 also contained oligosaccharides of the high-mannose type. Half-lives of the turnover of the oligosacharide chains and of the protein backbone of the five glycoproteins were measured in the plasma membrane in pulse-chase experiments in vivo, using L-[3H]fucose as a marker of terminal sugars, D-[3H]mannose as marker of a core sugar and L-[3H]leucine for labelling the protein backbone. Protein backbones of the five glycoproteins were degraded with individual half-lives ranging over 41-90 h with a mean of 66 h. Compared to the degradation of the polypeptide backbone, both the terminal sugar L-fucose and the core sugar D-mannose turned over with much shorter half-lives averaging about 20 h in the five glycoproteins. The data show that, conversely to liver, within plasma membrane glycoproteins of hepatoma not only peripheral sugars but also core sugars of the oligosaccharides are split off during the life-span of the protein backbone. It may therefore be assumed that this reprocessing of plasma membrane glycoproteins is sensitive to malignant transformation.

Animals↗

PubMed1995

Prevention of bone loss in early nonsurgical and nonosteoporotic high turnover patients with salmon calcitonin: the role of biochemical bone markers in monitoring high turnover patients under calcitonin treatment.

Annual bone loss rate was estimated in a group of randomly selected 150 nonsurgical and nonosteoporotic early postmenopausal women, 42-56 years, with the use of the mathematical equation proposed by Christiansen et al. (OSTEOTREND-R) [1]. Fifty-six women were characterized as high turnover patients (estimated annual bone loss more than 2.7%). These high turnover patients were included in a double-blind, placebo-controlled clinical study. Patients were divided into two groups of 28 women each. The first group of patients received 100 IU of salmon calcitonin intranasally daily for 1 year and the second group intranasal spray of placebo daily. Blood and urine biochemical parameters as well as bone mineral content of the spine and proximal forearm were determined initially and at the end of 6 and 12 months. No other side effects were noted apart from discomfort of nasal mucosa in two patients (one in each group). The group of calcitonin-treated patients showed a dramatic decrease in bone loss rate as estimated with the use of biochemical bone markers at the end of 6 and 12 months (3.7% versus 0.8% and 0.0% at the end of 6 and 12 months, respectively, P < 0.001) whereas in the placebo group, bone loss rate remained unchanged (4.2% versus 4.1% and 4.3% at the end of 6 and 12 months, respectively). The calcitonin-treated patients showed a significant increase in bone mineral content of spine and proximal forearm (P < 0.001 at the end of 6 and 12 months, respectively). On the other hand, a significant decrease in all measurement sites appeared in the placebo group.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗

PubMed1976

The actions of parathyroid hormone on bone: relation to bone remodeling and turnover, calcium homeostasis, and metabolic bone disease. Part I of IV parts: mechanisms of calcium transfer between blood and bone and their cellular basis: morphological and kinetic approaches to bone turnover.

The supracellular organization of living bone enables the study of isolated cellular and subcellular systems to be related to the study of the whole organism. Bone is formed by osteoblasts in successive stages, separated in both time and space, of matrix formation and primary mineralization. Osteoblasts are joined by tight junctions and largely cover the osteoid seam which separates them from mineralized bone. Secondary mineralization is not completed for several months and is not regulated by the osteoblast. Bone is resorbed by osteoclasts which simultaneously accomplish mineral dissolution and matrix digestion. Active osteoblasts occupy about 5% of the free bone surface, osteoid seams with less active osteoblasts about 10%, active osteoclasts about 0.5%, and Howship's lacunae at which bone remodeling is either quiescent or arrested about 5%. The remaining 80% of the free bone surface is covered by a leaky envelope of thin flattened cells, termed surface osteocytes. Some osteoblasts become permanently buried in the bone as deep osteocytes, around which a specialized and metabolically active perilacunar bone is formed. This bone is less highly mineralized and can temporarily lose or gain calcium in accordance with homeostatic needs. Deep osteocytes maintain contact with each other and with the surface osteocytes, their cell processes within canaliculi being joined by gap junctions. Remodeling of cortical bone proceeds with the excavation by osteoclasts of a longitudinal tunnel which is refilled by osteoblasts to form a new osteon. The anatomically discrete longitudinally oriented structure consisting of a cutting cone of osteoclasts in front and a closing cone of osteoblasts behind is termed a cortical remodeling unit. The events of centrifugal resorption and centripetal formation which occur in a single cross section is termed a cortical remodeling cycle. Normally each new cycle is slightly out of phase with its predecessor. The quantities which characterize cortical remodeling are the birth rate of new remodeling cycles or activation frequency (mu), and the durations of the resorptive period (sigma r), the quiescent interval (sigma q) and the formation period (sigma f). The average distances traveled by the osteoclast and osteoblast are indicated respectively by the mean cement line diameter and mean wall thickness of completed osteons. These quantities show little interindividual variation. Because of this constancy the magnitude of bone turnover (the bone formation rate) is almost entirely a function of mu, the activation frequency of new remodeling cycles. Variations in the velocity of advance of osteoclasts (the linear resorption rate) or of osteoblasts (the appositional rate) alter inversely both the extent of surface engaged in resorption or formation and the time taken to replace a particular moiety of bone, but in a steady state do not influence the rate of turnover of the skeleton as a whole...

Animals↗

PubMed1997

Continuously combined hormone replacement therapy and bone turnover: the influence of dydrogesterone dose, smoking and initial degree of bone turnover.

In this study we examined whether the effect of continuously combined hormone replacement therapy (HRT) on bone metabolism is influenced by dydrogesterone dose, smoking and initial degree of bone turnover. In a double-blind randomized study, 123 healthy postmenopausal women (mean age 51.7 years; range 30-61 years) received 17 beta-estradiol, 2 mg orally per day, continuously combined with either 2.5, 5, 10 or 15 mg of dydrogesterone daily. At baseline and at 3 and 6 months of therapy, bone formation was assessed by determining total alkaline phosphatase (TAP), bone-derived alkaline phosphatase (BAP), and the carboxy-terminal propeptide of collagen type I (PICP) in serum; bone resorption was assessed by the calcium/creatinine (Ca/Creat) and hydroxyproline/creatinine (Hp/Creat) ratio in 2-h fasting urine, and the serum carboxy-terminal pyridinolyne cross-linked telopeptide of collagen type I (ICTP). Dydrogesterone dose did not influence the effect of HRT on any of the bone markers. Combining the data of the four treatment groups, the decrease in each marker, compared to baseline values, was significant. However, in non-smokers, compared to smokers, after 6 months of therapy the decline in BAP and TAP was significantly more pronounced and the plasma estradiol level was significantly higher. For each bonemarker at baseline, women in the highest quartile, compared to women in the lowest quartile, showed a significantly stronger decrease in this marker in response to HRT. We conclude that dydrogesterone dose does not modify the effectiveness of replacement therapy. However, smoking and a low bone turnover at baseline may diminish its beneficial effect on bone.

Adult↗

PubMed1976

A new approach to assessing collagen turnover by using a micro-assay. A highly efficient and rapid turnover of collagen in rat periodontal tissues.

Measurement of [3H]proline incorporation into newly synthesized and mature collagen in connective tissues was used to compare rates and efficiency of collagen turnover. The approach minimizes label-recycling problems. By using a micro-assay to determine hydroxyproline specific radioactivities, a highly efficient and rapid collagen turnover in rat periodontal tissues was demonstrated.

Animals↗

PubMed2001

Movement of the iron-sulfur subunit beyond the ef loop of cytochrome b is required for multiple turnovers of the bc1 complex but not for single turnover Qo site catalysis.

Recent kinetics experiments using mutants of the bc(1) complex (ubihydroquinone-cytochrome c oxidoreductase) iron-sulfur subunit with modified hinge regions have revealed the crucial role played by the large scale movement of its [2Fe-2S] cluster domain during the activity of this enzyme. In particular, one of these mutants (+1Ala) with an insertion of one alanine residue in the hinge region is partially deficient in performing this movement. We found that this defect can be overcome by the appearance of a second mutation substituting the leucine at position 286 in the ef loop of cytochrome b with a phenylalanine. Detailed studies of these mutants and their derivatives revealed that the ef loop acts as a barrier that needs to be crossed for multiple turnovers of the enzyme but not for a single turnover ubihydroquinone oxidation site catalysis. These findings indicate that the movement of the iron-sulfur subunit is composed of two discrete parts: a "micro-movement" at the cytochrome b interface, during which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," during which the cluster domain swings away from cytochrome b interface, crosses the ef loop, and reaches a position close to cytochrome c(1) heme, to which it ultimately transfers an electron.

Alanine↗

PubMed1983

Influence of diet on glucose turnover and rates of gluconeogenesis, oxidation and turnover of D-(-)-lactate in the bovine.

D-(-)-Lactate metabolism as influenced by the level of roughage in the diet was examined in eight Hereford heifers (306 kg) fed ad libitum as alfalfa hay diet (R) (2.02 Mcal ME/kg) (ME, metabolizable energy) or a 90% concentrate diet (C) (2.95 Mcal ME/kg) for 18 days. Animals were adjusted to negative pressure hoods (188 liter/minute airflow) and fitted with jugular and urinary catheters. Animals received 32.2 and 71.4 microCi of D-[U-14C]lactate and 435.7 and 233.3 microCi of 2-[3H]glucose for the primer dose and hourly infusion rates, respectively. Blood, expired CO2 and urine samples were taken at 30-minute intervals for 6 hours with CO2 and urine samples taken for an additional 24 and 42 hours, respectively. ME intakes were not different between diets (P greater than 0.05) for the day of infusion. Glucose turnover rates were 143.3 and 154.3 mmol/hour, whereas, D-(-)-lactate turnover was 0.67 and 0.57 mmol/hour for R anc C, respectively. Rates of oxidation and gluconeogenesis were 0.61 and 0.22 mmol/hour for R and 0.55 and 0.16 mmol/hour for C. Recovery of 14C in urine and expired air accounted for 3.73 and 44.3% of the infused dose for R and 2.13 and 43.5% of the infused dose for C. Oxidation was the major route of D-(-)-lactate elimination but the potential for D-(-)-lactate elimination from the bovine under high D-(-)-lactate loads is as yet undetermined.

Animal Nutritional Physiological Phenomena↗