acid-phosphatase and Starvation

Aquatic animals are frequently suffered from starvation due to restricted food availability or deprivation. It is currently known that gut microbiota assists host in nutrient acquisition. Thus, exploring the gut microbiota responses would improve our understanding on physiological adaptation to starvation. To achieve this, we investigated how the gut microbiota and shrimp digestion and immune activities were affected under starvation stress. The results showed that the measured digestion activities in starved shrimp were significantly lower than in normal cohorts; while the measured immune activities exhibited an opposite trend. A structural equation modeling (SEM) revealed that changes in the gut bacterial community were directly related to digestive and immune enzyme activities, which in turn markedly affected shrimp growth traits. Notably, several gut bacterial indicators that characterized the shrimp nutrient status were identified, with more abundant opportunistic pathogens in starved shrimp, although there were no statistical differences in the overall diversity and the structures of gut bacterial communities between starved and normal shrimp. Starved shrimp exhibited less connected and cooperative interspecies interaction as compared with normal cohorts. Additionally, the functional pathways involved in carbohydrate and protein digestion, glycan biosynthesis, lipid and enzyme metabolism remarkably decreased in starved shrimp. These attenuations could increase the susceptibility of starved shrimp to pathogens infection. In summary, this study provides novel insights into the interplay among shrimp digestion, immune activities and gut microbiota in response to starvation stress.

Topics: Acid Phosphatase; Amylases; Animals; Bacteria; Digestion; Gastrointestinal Microbiome; Hepatopancreas; Lipase; Muramidase; Penaeidae; Pepsin A; RNA, Ribosomal, 16S; Starvation; Stomach; Stress, Physiological; Superoxide Dismutase

Starvation, in particular amino acid deprivation, induces autophagy in trophocytes (adipocytes), the major component of the fat body cell types, in the larvae of Drosophila melanogaster. However, the fat body of cockroach has two additional cell types: urocytes depositing uric acid in urate vacuoles as a nitrogen resource and mycetocytes harboring an endosymbiont, Blattabacterium cuenoti, which can synthesize amino acids from the metabolites of the stored uric acid. These cells might complement the roles of autophagy in recycling amino acids in the fat body or other organs of cockroaches under starvation. We investigate the presence of autophagy in tissues such as the fat body and midgut of the American cockroach, Periplaneta americana, under starvation by immunoblotting with antibody against Atg8, a ubiquitin-like protein required for the formation of autophagosomes and by electron microscopy. Corresponding changes in acid phosphatase activity were also investigated as representing lysosome activity. Starvation increased the level of an autophagic marker, Atg8-II, in both the tissues, extensively stimulating the formation of autophagic compartments in trophocytes of the fat body and columnar cells of the midgut for over 2 weeks. Acid phosphatase showed no significant increase in the fat body of the starved cockroaches but was higher in the midgut of the continuously fed animals. Thus, a distinct autophagic mechanism operates in these tissues under starvation of 2 weeks and longer. The late induction of autophagy implies exhaustion of the stored uric acid in the fat body. High activity of acid phosphatase in the midgut of the fed cockroaches might represent enhanced assimilation and not an autophagy-related function.

Topics: Acid Phosphatase; Adaptor Proteins, Signal Transducing; Adipocytes; Amino Acid Sequence; Amino Acids; Animals; Autophagy; Base Sequence; Cloning, Molecular; Fat Body; Lysosomes; Microfilament Proteins; Molecular Sequence Data; Nerve Tissue Proteins; Periplaneta; Sequence Alignment; Starvation; Uric Acid

Digestive enzymatic activity and growth performance on tropical gar (Atractosteus tropicus) larvae fed Artemia nauplii (LF), frozen adult Artemia (AB), an artificial diet (AF) with 46% protein and 16% lipids and a starvation group (SG) from first feeding (5 days after hatching-5 DAH) to 34 DAH were studied. All larvae under starvation (SG) died at 15 DAH. By the end of the experimental period, morphological variables (total length, wet weight and specific growth rate) were significant in larvae fed AF compared to LF and AB. All enzymes studied in the experiment were present since the start of exogenous feeding (including pepsin) and the enzymatic activity varied with the diets. Low levels of enzymatic activity were observed until the 29 DAH; however, after this moment, there was a significant increase (eightfold), particularly for the AF treatment. In vitro protein digestibility tests performed with enzymatic extracts showed that artificial diets with 52% protein and 14% lipids were better digested by larvae before 30 DAH, while diets with 45% protein and 11% lipids were better digested after this age. Taking into account the better growth performance, higher enzymatic activity and better protein digestibility obtained, artificial diets can be used since the start of exogenous feeding on tropical gar larvae, as in other lepisosteids.

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Animal Feed; Animals; Artemia; Chymotrypsin; Diet; Dietary Proteins; Digestion; Digestive System; Fish Proteins; Fishes; Larva; Lipase; Pepsin A; Peptide Hydrolases; Starvation; Trypsin

We examined the relationship between the amount of organic solvent-soluble fluorescent pigments (OFP), which are generally regarded as the products of lipid peroxidation, and the content of glutathione in chloroquine-treated mice in order to assess the toxicological significance of the formation of these fluorescent pigments. OFP extracted with chloroform/methanol (2:1, v/v) were quantified spectrophotofluorometrically (excitation, 380 nm; emission, 460 nm). The administration of chloroquine diphosphate (50 mg/kg, i.p.) greatly increased the fluorescent intensity of OFP in the kidneys, but not in the livers, whereas administration of this drug significantly decreased glutathione content in the livers. In contrast, depletion of glutathione, induced either by starvation or by pretreatment with buthionine sulfoximine, a potent inhibitor of glutathione synthesis, markedly augmented the fluorescence intensity of OFP in the livers of mice treated with chloroquine. In the serum of mice treated with chloroquine, the alteration in activity of acid phosphatase and gamma-glutamyl transpeptidase approximately paralleled changes in the formation of fluorescent pigments in the tissues. These findings suggest that glutathione is an important endogenous substance which influences the insult of chloroquine.

Topics: Acid Phosphatase; Animals; Antimetabolites; Buthionine Sulfoximine; Chloroquine; gamma-Glutamyltransferase; Glutathione; Kidney; Liver; Male; Methionine Sulfoximine; Mice; Pigments, Biological; Spectrophotometry; Starvation

A number of lysosomal enzymes are secreted from Tetrahymena pyriformis during growth and during starvation. The secretion is energy-dependent and kinetically different among hydrolases. On the basis of the secretion kinetics under starvation conditions, Tetrahymena hydrolases can be separated into three classes. The first group containing acid phosphatase, beta-glucosidase and alpha-galactosidase, are secreted slowly. Within this group about 4% of the initial cellular activity is released per hour. The second group of enzymes, including alpha-glucosidase, alpha-mannosidase and beta-galactosidase, exhibit moderate secretion (11-15% of the initial cellular activity per hour). The third group, N-acetyl-beta-hexosaminidase, has the highest rate of secretion (22% of the initial cellular activity per hour). N-Acetyl-beta-hexosaminidase shows a continuous increase in overall activity during starvation, which is completely blocked by adding cycloheximide; its secretion is also suppressed. Such involvement of enzyme biosynthesis was not seen in the first and second groups. Furthermore, treatment with weak bases caused inhibited secretion of differing degree among acid phosphatase (group I), alpha-glucosidase (group II) and N-acetyl-beta-hexosaminidase (group III).

Topics: Acid Phosphatase; Age Factors; alpha-Mannosidase; Ammonium Chloride; Animals; Azides; beta-Galactosidase; beta-N-Acetylhexosaminidases; Cell Compartmentation; Chloroquine; Cycloheximide; Extracellular Space; Glucosidases; Lysosomes; Mannosidases; Sodium Azide; Starvation; Tetrahymena pyriformis

Acid phosphatase activity in isolated rat liver parenchymal cells has been investigated with quantitative histochemical means during short-term starvation, which leads to a considerable loss in protein mass in the parenchyma. Animals trained to a meal-feeding regime in which food was available during 1 h only per 24 h (using an automatic food dispensing machine), were sacrificed 6, 12, 18, 24 and 36 h after food had been withheld at the time point (23.00 h) of meal feeding. Acid phosphatase activity was analysed cytophotometrically in isolated hepatocytes incorporated into polyacrylamide gels before the enzyme reaction technique with the post-azo coupling was carried out. No indication could be found for any significant changes in the amount of acid phosphatase activity per individual hepatocyte during the entire period of fasting, as compared with two time points (11.00 and 23.00 h) before the theoretical onset of fasting. It is concluded that the considerable enhancement of protein degradation in the lysosomal apparatus during fasting is not reflected by changes in the cellular acid phosphatase activity.

Topics: Acid Phosphatase; Animals; Histocytochemistry; Kinetics; Liver; Male; Proteins; Rats; Rats, Inbred Strains; Starvation

Acid phosphatase (EC: 3.1.3.2) activity at the hypothalamus and frontal cerebral cortex has been studied in male rats maintained on different dietary regimes. The enzyme activity in the cerebral cortex did not undergo any observable changes in any of the experimental groups. Enzyme activity in the hypothalamus, rose after food deprivation in both acutely and chronically starved rats, while the enzyme activity returned to physiological levels in refed animals. The hypothalamus neuroendocrine role and a possible interregional heterogeneity for acid phosphatase in rat brain might explain the two enzymic activity patterns observed in the present experiment.

Topics: Acid Phosphatase; Animals; Cerebral Cortex; Food; Hypothalamus; Male; Rats; Rats, Inbred Strains; Starvation

To determine whether the increased activity of cathepsin D observed during starvation-induced cardiac atrophy results from activation of preexisting enzyme or synthesis of new enzyme, a solid phase double-antibody radioimmunoassay was developed for measurement of immunoreactive cathepsin D in extracts of rabbit myocardium. Cathepsin D activity was significantly increased in the hearts of animals starved for 3, 7, and 14 days (82.6 +/- 0.8, 87.2 +/- 3.8, and 95.3 +/- 3.5 U/g wet wt, respectively) compared to controls (65.5 +/- 1.4 U/g wet wt; P less than 0.001). Immunoreactive cathepsin D was increased to a greater extent (168 +/- 7, 179 +/- 16, 200 +/- 17, and 104 +/- 5 micrograms/g wet wt for 3-, 7-, and 14-day starvation and controls, respectively; P less than 0.001) than that expected on the basis of the observed increase in enzyme activity. Sephadex G100 gel filtration of cardiac lysosomal extracts from starved and control animals revealed no evidence of high or low molecular weight forms of cathepsin D. The results suggest the observed increase in cathepsin D activity during starvation-induced cardiac atrophy is accompanied by an increased synthesis and/or decreased degradation of cathepsin D protein, rather than activation of preexisting enzyme. The lower activity levels observed during starvation possibly result from alterations in the concentrations of endogenous inhibitors or activators of cathepsin D.

Topics: Acid Phosphatase; Animals; Atrophy; Cathepsins; Male; Myocardium; Rabbits; Radioimmunoassay; Ribonucleases; Starvation; Time Factors

Prolonged starvation produces dramatic changes both in the lysosomal properties of the heart and in its energy stores and, therefore, might be expected to alter some of the characteristic cardiac responses to ischemia. To test this possibility we ligated the circumflex coronary artery of rabbits that had been fed normally or starved for 6 days. Ultrastructural evidence of myocytic damage following 30 to 120 minutes of ischemia was much less severe in the starved animals than in the normally fed group. The development of signs of irreversible injury (e.g., osmiophilic densities in mitochondria) was delayed for 1 hour or more by starvation. A similar delay occurred in the biochemical redistribution of cathepsin D activity and in the cytoplasmic release of acid hydrolases from lysosomes and sarcoplasmic reticulum. These results indicate a marked protective effect of starvation against myocardial ischemia. In addition, both in starved and in fed animals, ischemically induced release of lysosomal enzymes was closely linked temporally to the development of subcellular damage.

Topics: Acid Phosphatase; Animals; Cathepsins; Coronary Disease; Histocytochemistry; Lysosomes; Male; Myocardium; Rabbits; Sarcoplasmic Reticulum; Starvation

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Cathepsin B; Cathepsin D; Cathepsins; Food; Histocytochemistry; Lysosomes; Male; Microscopy, Electron; Myocardium; Rabbits; Starvation; Subcellular Fractions; Vacuoles

Starvation-induced alterations in liver lysosomes and their recovery pattern following refeeding were investigated. Fasting of adult rats for five days caused an increase in 'free' activities of acid hydrolyses in liver homogenates and loss in sedimentation of one of the heterogenous populations of lysosomes that could be isolated by differential centrifugation. Isopycnic sucrose gradient centrifugation revealed a decrease in the median and modal equilibration densities of all the forms of lysosomes in response to the dietary deprivation. Further, starvation also evoked a distinct bimodal distribution in a population that was rich in acid phosphatases, beta-galactosidase and N-acetyl-beta-glucosaminidase. Realimentation of starved animals for 10 days was found to restore the enzyme levels and the sedimentation characteristics to normal profiles.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Arylsulfatases; beta-Galactosidase; Cathepsins; Cell Fractionation; Centrifugation, Isopycnic; Diet; Liver; Lysosomes; Male; Rats; Ribonucleases; Starvation

Starvation overnight and starvation for 48 h reduced the weight and the protein content of mucosal scrapings, but only minimally reduced the DNA content of the mucosal scrapings. The activity of sucrase and maltase was reduced by both periods of starvation. The activity of lactase and of acid and alkaline phosphatase, however, was less subject to starvation. There were striking differences in the response to starvation between the proximal, mid and distal third of the small intestine. The importance of the proper reference system was discussed.

Topics: Acid Phosphatase; Alkaline Phosphatase; alpha-Glucosidases; Animals; beta-Galactosidase; Body Weight; Disaccharidases; DNA; Germ-Free Life; Hydrolases; Intestinal Mucosa; Intestine, Small; Male; Organ Size; Proteins; Rats; Starvation; Sucrase; Time Factors

The activity of glycolysis and hexose monophosphate shunt decreases while the activity of some oxydative enzymes and acid phosphatase increases in the anterior pituitary of adult female rats during starvation. The alterations depend on the severity of starvation. The polypeptide hormone production also decreases. A close relationship exists between the metabolic activity of the gland and its endocrine function.

Topics: Acid Phosphatase; Animals; Eating; Female; Glucosephosphate Dehydrogenase; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Malate Dehydrogenase; Pituitary Gland, Anterior; Rats; Starvation

Topics: Acid Phosphatase; Animals; Ascitic Fluid; Cathepsins; Glucuronidase; Liver; Lysosomes; Mice; Phagocytosis; Starvation

The ultrastructure of the mid-gut cells of female Nasonia vitripennis is described. The mid-gut consists of a uniform, single-cell epithelium. The cells of different gut regions were analysed using morphometric techniques in order to determine any differences in the components. The structure of the cells is described in the unfed animal, and after varying periods of feeding on host body-fluids. Tissues were sampled after 12 h and 24 h of feeding on host body-fluids and after 24 h feeding/24 h starvation. The cells were found to be complex and contain an organelle component that allows solute-transport and extensive lipid synthesis. A limited cytochemical analysis involving the lysosomal marker enzyme-acid phosphatase--and the respiratory enzyme--cytochrome oxidase was carried out.

Topics: Acid Phosphatase; Animals; Digestive System; Electron Transport Complex IV; Epithelial Cells; Epithelium; Female; Histocytochemistry; Hymenoptera; Microscopy, Electron; Starvation

Topics: Acid Phosphatase; Amylases; Animals; Cathepsins; Isoproterenol; Lysosomes; Male; Parotid Gland; Rats; Starvation

Topics: Acid Phosphatase; Animals; Arylsulfatases; Back; Catalase; Cathepsins; Chickens; Chloroquine; Glucuronidase; Hindlimb; Lysosomes; Male; Muscle Denervation; Muscles; Muscular Diseases; Rats; Ribonucleases; Starvation; Time Factors

The foot epithelium of the slug Agriolimax reticulatus (M) can function as a digestive epithelium and possesses a vacuolar system in which heterophagic and autophagic material is hydrolysed. Using ferritin and peroxidase as markers, the process of endocytosis has been demonstrated at the level of the electron microscopy. The mechanisms involved with the uptake of each marker differed in that ferritin was confined to fairly large vacuoles, while peroxidase was present in smaller pinocytotic vesicles which ultimately fused to form larger vacuoles or multivesicular bodies. Cytochemical tests for acid phosphatase revealed that the latter bodies acquired hydrolytic enzyme to become secondary lysosomes. Acid phosphatase was also localized in the Golgi apparatus of the epithelial cells. In addition to the endocytotic activity, evidence of autophagy was found in the epithelial cells and this process was apparently enhanced during starvation.

Topics: Acid Phosphatase; Animals; Endocytosis; Epithelium; Golgi Apparatus; Lysosomes; Microscopy, Electron; Mollusca; Pinocytosis; Starvation

The effect of 120- and 240-h starvation on rats hepatocytes ultrastructure and particularly the changes of the lysosomes were studied. Eelectronmicroscopically and cytochemically there have been observed diminution of the number of mitochondria and degranulation and vacuolzation of the ER. At the same time Golgi complex was hypertrophied and the number of lysosomes was much increased, mainly those of the autophagic type. Biochemically was shown, that the activity of some acid hydrolases (beta-glucosidase, alpha- and beta-galactosidases, beta-N-acetylglucosaminidase, beta-glucuronidase and arylsulphatases A and B) in the liver of starved rats was markedly expressed. The sedimentation properties of the lysosomes and the lysosomal membrane stability was damaged as well. The data received have been discussed in the light of the reconstructive role of lysosomes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Cerebroside-Sulfatase; Chondro-4-Sulfatase; Galactosidases; Glucose-6-Phosphatase; Glucosidases; Glucuronidase; Liver; Lysosomes; Male; Microsomes, Liver; Mitochondria, Liver; Proteins; Rats; Starvation

Acid phosphatase activity is demonstrated employing p-nitrophenyl phosphate as substrate and lead acetate as coupler. The fine structural localization of the enzyme in starved planarian tissues is described. The method is used to pin-point starvation - induced acid phosphatase activity in relation to autophagy and crinophagy in the gland cells; autophagy, autolysis and cell death in parenchymal and gastrodermal cells and basement membrane lysis. Attention is also payed to the demonstration of muscle lysis. The histochemical implications of the method are discussed.

Topics: 4-Nitrophenylphosphatase; Acid Phosphatase; Animals; Basement Membrane; Histocytochemistry; Microscopy, Electron; Nitrophenols; Phosphoric Monoester Hydrolases; Planarians; Staining and Labeling; Starvation; Turbellaria

Employing a combination of microscopical, biochemical and autoradiographic techniques, the primary effects of starvation on adult polycelis tenuis have been studied. Over a five week period of starvation there is on average a 32% decrease in the size of the organism. This decrease is contributed to by a reduction in mitosis and an increase in cell shrinkage autolysis and death. During starvation (following a sharp rise in RNA synthesis) there is a distinct sequence of events; four peaks of acid phosphatase activity can be resolved. The first is associated with the immediate response of the gastrodermis to feeding; the second (after 6 to 7 days) with increased autophagy and dedifferentiation in the gland cells and with muscle lysis of cells. The third peak (after 14 to 15 days) is contributed to largely by the lysis of cells in the gut and the fourth peak (after 25 to 26 days) is caused by an extensive lysis of the reproductive system. Fine structural changes involving increased intracellular vacuolation, autophagy, crinophagy, atrophy of muscle, increased intercellular space and loss of basement membrane matrix have been related to changes in enzyme pattern. Nerve cells appear unchanged throughout the first five weeks of starvation. Pigment and gland cells loose their characteristic granules, dedifferentiate and become morphologically similar to the undifferentiatied neoblasts. Dedifferentiation and the mechanisms involved in the survival of starvation are discussed.

Topics: Acid Phosphatase; Animals; Autolysis; Cell Differentiation; Cell Survival; Lysosomes; Mitosis; Planarians; RNA; Starvation; Turbellaria

Prolonged starvation is known to induce significant alterations in several cardiac lysosomal enzymes, particularly the acid proteinase cathepsin D. To determine what specific factors might mediate these changes, fetal mouse hearts in organ culture were maintained in media designed to simulate selected hormonal or nutritional substrate changes that accompany starvation. Reduced concentrations of glucose caused an increase in the activity of beta-acetylglucosaminidase but had no effect on cathepsin D or acid phosphatase activites (i.e., effects opposite from those of starvation). Also, high concentrations of free fatty acid, acetoacetate, and beta-OH-butyrate induced an increase in cathepsin D (+18%) and a simultaneous decrease in glucosaminidase (-19%), with little change in acid phosphatase. Furthermore, glucagon had no effect on any of the enzymes, whereas growth hormone caused a small (6%) increase in cathepsin D activity. In addition, insulin deprivation caused significant increases (7-25%) in the activities of all three enzymes. Insulin deprivation and excess ketones, but not the other interventions, increased the proportion of enzyme activity which was nonsedimentable. These results suggest the possibility that lysosomal alterations during starvation may be related in part to prolonged insulin deficiency and exposure to high concentrations of ketones and free fatty acids.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Cathepsins; Creatine Kinase; Fatty Acids, Nonesterified; Female; Fetal Heart; Glucagon; Growth Hormone; Insulin; Ketones; Lysosomes; Mice; Models, Biological; Myocardium; Organ Culture Techniques; Pregnancy; Starvation

The authors studied in rats the effect of starving from 24 to 96 hours after a regimen of single or all-day feeding. They determined in liver homogenate the total activities of beta-N-acetyl glucosaminidase, acid phosphatase and beta-glucuronidase as well as the free activities of the two first-mentioned enzymes. The activity of beta-N-acetyl glucosaminidase was also determined in the blood. It was found that the total activity of beta-N-acetyl glucosaminidase in the liver homogenate increased with the length of starvation. The free and serum activities of the enzymes under investigation showed similar changes. These increases were more marked in rats subjected to a single-feeding regimen before starving. These changes are explained as an expression of the active participation of the lysosomes and their enzymes in the transition to endogenous feeding. The lysosomal membrane was more sensitive in starving animals which had been subjected to a single-feeding regimen.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Feeding Behavior; Glucuronidase; Hexosaminidases; Liver; Lysosomes; Male; Rats; Starvation; Time Factors

Topics: Acid Phosphatase; Animals; Arylsulfatases; Atrophy; Body Weight; Endoplasmic Reticulum; Glucuronidase; Lipid Metabolism; Liver; Liver Glycogen; Lysosomes; Male; Microscopy, Electron; Mitochondria, Liver; Nutrition Disorders; Rats; Starvation; Time Factors

The influence of starving on the activity of enzymes of the rat gastric mucosa was investigated by selected histochemical methods. Beside the conventional methods of enzymatic histochemistry the technique of semipermeable membranes was used in the proof of lysosomal enzymes. Dehydrogenases were proved in aqueous and also in gel media with PMS. During the starvation in the parietal cells a marked increase took place in the activity of acid phosphatase, E-600 resistant esterase, less in beta-glucuronidase. High activity of the lysosomal enzymes in macrophages did not change during starvation. Nor did any changes took place in the activity of alkaline phosphatase in the endothelium of the capillaries. The chief cells in the control and starving animals, in contrast to the human gastric mucosa, did not contain any non-specific esterase. Concerning dehydrogenases, parietal cells with a different activity of these enzymes were observed both in starved and control animals. In the rat gastric mucosa starving induced changes in the activity of the enzymes which mark important organelles of the cells. Thus it is possible to consider the observed histochemical changes as a functional manifestation of morphological damage of cellular structures which are affected during starvation.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Carboxylic Ester Hydrolases; Gastric Mucosa; Glucuronidase; Histocytochemistry; Lysosomes; Oxidoreductases; Rats; Starvation

91 male, albino rats, Wistar strain, with body weight 150 +/- 10 g, subdivided into 2 series were investigated. The 1rst series animals (E) were fed on single daily meals in the course of 20 days, only 2 h in 24 h and after that period were subjected to complete starvation and investigated on the 24th, 48th, 72th and 96th h resp. after the ceasing of food supply. A 2nd animal series (C) serves as a control, which in the course of 20 days, were on a all-round diet and later put in identical conditions of complete starvation and also investigated on the 24th, 48th, 72th and 96th h. The liver histological, histo-enzymatical (AP, BG, AlkP and ATP) and electron microscopic changes followed up, as well as certain physiological, biochemical and morphometric indices. The dynamics of the alterations in complete starvation and the confrontation of the data between the 2 animal series with different preceding nutritional regimes show that: 1) single daily meals leads to real undernourishment; 2) the undernourishment predetermines a more severe course of the following period of complete starvation; 3) 3 phases are established during the complete starvation: adaptive, alterative-restorative and alterative. Each phase bears a definite subcellular characteristics where the lysosomes apparatus plays an essential role.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Blood Glucose; Blood Proteins; Cell Nucleus; Endoplasmic Reticulum; Glucuronidase; Liver; Lysosomes; Male; Mitochondria, Liver; Organ Size; Rats; Starvation

Comparative histochemical investigations of the livers and kidneys of female Sprague-Dawley rats were made: 1. after intoxication with O-pinacolyl-methyl-phosphonylfluoride (Soman), O,O-diethyl-O-p-nitrophenylphosphate (Paraoxon, E 600); 2. after starvation of 24 to 36 h; 3. after hypoxia for 24 h. From the results it is concluded that the fatty degeneration of liver and kidney after PE.-intoxication is caused by intracellular hypoxia. No fatty degeneration of the organs was observed following deprivation of food for 36 h. A decreased level of cholin which might be caused by the intoxication with PE., and which could be the reason for the fatty degeneration was not found. This was indicated by the unaltered evidence of phosphatids in the intoxicated animals.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cytochrome Reductases; Electron Transport Complex IV; Esterases; Fatty Liver; Female; Glucose-6-Phosphatase; Glucosephosphate Dehydrogenase; Glucuronidase; Hydroxybutyrate Dehydrogenase; Hypoxia; Isocitrate Dehydrogenase; Ketoglutarate Dehydrogenase Complex; Kidney; Lipase; Lipid Metabolism; Liver; Malate Dehydrogenase; Organophosphorus Compounds; Paraoxon; Pyruvate Dehydrogenase Complex; Rats; Soman; Starvation; Succinate Dehydrogenase

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Cathepsins; Fluorescent Antibody Technique; Heart Ventricles; Hexosaminidases; Lysosomes; Male; Mice; Myocardium; Rabbits; Starvation; Subcellular Fractions

The gastrodermis of adult Schistosoma mansoni was examined by electron microscopy to determine the effects of starvation and the effects of hycanthone, administered in vitro. Special attention was focused on the relationship of the Golgi complexes with the process of autophagy. In general, autophagy was increased in the gastrodermis when it was exposed to stress conditions such as starvation and hycanthone. Acid phosphatase and thiamine pyrophosphatase activities were used as enzyme markers for the Golgi complexes and lysosomes. During the early stages of starvation, there was a 4-fold increase in the number of Golgi complexes per unit area in the gastrodermis. A progressive increase in the number of secondary lysosomes was evident as starvation time was increased. Hycanthone accelerated the effects of starvation. It was hypothesized that acid hydrolases are passed to the Golgi complexes via ER-derived vesicles. The enzymes are subsequently released as primary lysosomes from the Golgi complex to fuse with cytosegresomes and form secondary lysosomes (cytosomes).

Topics: Acid Phosphatase; Animals; Chromatin; Female; Golgi Apparatus; Histocytochemistry; Hycanthone; Lysosomes; Male; Mice; Microtubules; Schistosoma mansoni; Starvation; Thiamine Pyrophosphatase

1. Rates of insulin secretion, glucose utilization, lactate output, incorporation of glucose into glycogen, contents of glucose 6-phosphate, fructose 1,6-diphosphate and ATP, and maximally extractable enzyme activities of hexokinase, high-K(m) glucose-phosphorylating activity (;glucokinase'), glucose 6-phosphatase and unspecific acid phosphatase were measured in isolated pancreatic islets from fed and 48-h-starved mice. 2. In the fed state insulin secretion from isolated islets was increased five- to six-fold when the extracellular glucose concentration was raised from 2.5mm to 16.7mm; 5mm-caffeine potentiated this effect. The secretory response to glucose of islets from mice starved for 48h was diminished at all glucose concentrations from 2.5mm up to approx. 40mm. Very high glucose concentrations (60mm and above) restored the secretory response to that found in the fed state, suggesting that the K(m) value for the overall secretory process had been increased (approx. fourfold) by starvation. Addition of 5mm-caffeine to islets from starved mice also restored the insulin secretory response to 2.5-16.7mm-glucose to normal values. 3. Extractable hexokinase, ;glucokinase', glucose 6-phosphatase and unspecific phosphatase activities were not changed by starvation. 4. Glucose utilization and glycolysis (measured as the rate of formation of (3)H(2)O from [5-(3)H]glucose over a 2h period) was decreased in islets from starved mice at all glucose concentrations up to approx. 55mm. At still higher glucose concentrations up to approx. 100mm, there was no difference between the fed and starved state, suggesting that the K(m) value for the rate-limiting glucose phosphorylation had been increased (approx. twofold) by starvation. Preparation of islets omitting substrates (glucose, pyruvate, fumarate and glutamate) from the medium during collagenase treatment lowered the glucose utilization measured subsequently at 16.7mm-glucose by 38 and 30% in islets from fed and starved mice respectively. Also the 2h lactate output by the islets at 16.7mm extracellular glucose was diminished by starvation. Incorporation of glucose into glycogen was extremely low, but the rate of incorporation was more than doubled by starvation. 5. After incubation for 30min at 16.7mm-glucose the content of glucose 6-phosphate was unchanged by starvation, that of ATP was increased and the concentration of (fructose 1,6-diphosphate plus triose phosphates) was decreased. 6. Possible mechanisms behind t

Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Caffeine; Fructosephosphates; Fumarates; Glucokinase; Glucose; Glucose-6-Phosphatase; Glucosephosphates; Glutamates; Glycogen; Glycolysis; Hexokinase; In Vitro Techniques; Insulin; Insulin Secretion; Islets of Langerhans; Kinetics; Male; Mice; NADP; Pyruvates; Starvation; Tritium

Topics: Acid Phosphatase; Ciliophora; Cytoplasmic Granules; Endoplasmic Reticulum; Histocytochemistry; Lysosomes; Organoids; Ribosomes; Starvation

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Citric Acid Cycle; Digestive System; Epithelial Cells; Epithelium; Glutamate Dehydrogenase; Histocytochemistry; Larva; Lepidoptera; Oxidoreductases; Starvation

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Carbon Disulfide; Cell Membrane; Chemical and Drug Induced Liver Injury; Edema; Endoplasmic Reticulum; Glucose-6-Phosphatase; Histocytochemistry; Liver; Liver Diseases; Male; Mixed Function Oxygenases; Nucleotidases; Phenobarbital; Rats; Starvation; Succinate Dehydrogenase; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bivalvia; Carbohydrate Metabolism; Cytoplasmic Granules; Ecology; Glucose; Glycogen; Hemolymph; Histocytochemistry; Starvation; Temperature; Trematoda

Topics: Acid Phosphatase; Animals; Brain; Cathepsins; Duodenum; Glucuronidase; Ileum; Lung; Male; Radiation Injuries, Experimental; Rats; Starvation

Topics: Acid Phosphatase; Animals; Dehydration; Drug Stability; Enzyme Activation; Esterases; Glucuronidase; Histocytochemistry; Hot Temperature; Hydrogen-Ion Concentration; Intestines; Kinetics; Lysosomes; Oligochaeta; Starvation; Structure-Activity Relationship

Topics: Acid Phosphatase; Alkaline Phosphatase; Aminopeptidases; Animals; Digestive System; Esterases; Fasciola hepatica; Glucosidases; Glucuronidase; Glycogen; Glycosaminoglycans; Hexosaminidases; Histocytochemistry; Inclusion Bodies; Lymnaea; Lysosomes; Starvation; Sulfatases; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Atrophy; Chickens; Esterases; Glucuronidase; Histocytochemistry; Intestine, Small; Leucyl Aminopeptidase; Male; Starvation; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adaptation, Physiological; Animal Nutritional Physiological Phenomena; Animals; Body Weight; Cathepsins; Dietary Carbohydrates; Dietary Fats; Dietary Proteins; Female; Galactosidases; Glucuronidase; Hydrolases; Intestinal Mucosa; Intestine, Small; Lysosomes; Organ Size; Rats; Starvation; Sulfatases; Time Factors

Postnuclear supernates from homogenates of skeletal muscle from rats subjected to starvation, injections of Triton WR-1339, dextran-500, and dextran + corticosterone were fractionated by means of rate and isopycnic zonal centrifugation in sucrose-0.02 M KCl gradients. Zonal fractions were analyzed for protein, RNA, cytochrome oxidase, and up to six acid hydrolases. The results indicate the presence of two groups of lysosome-like particles. One group contributes approximately 95% of the cathepsin D and acid phosphatase activity and 75% of the acid ribonuclease, beta-glucuronidase, and arylsulfatase activity in muscle. It is characterized by a modal equilibrium density of 1.18 that is decreased by starvation, but is not shifted by dextran-500 or Triton WR-1339. The second group has a higher proportion of acid ribonuclease, beta-glucuronidase, and arylsulftase; the equilibrium density can be shifted by dextran-500 and Triton WR-1339. It is suggested that this group of lysosomes is derived from macrophages and other connective tissue cells, whereas the former group represents lysosome-like particles from muscle cells.

Topics: Acid Phosphatase; Animals; Cathepsins; Cell Fractionation; Centrifugation, Zonal; Corticosterone; Detergents; Dextrans; Dialysis; Electron Transport Complex IV; Glucuronidase; Lysosomes; Methods; Muramidase; Muscle Proteins; Muscles; Phagocytosis; Proteins; Rats; Ribonucleases; RNA; Starvation; Time Factors; Tissue Extracts

Topics: Acid Phosphatase; Animals; Carbon Isotopes; Coenzyme A; Electron Transport Complex IV; Fatty Acids; Glucose-6-Phosphatase; Liver; Lysosomes; Malonates; Microsomes, Liver; Mitochondria, Liver; NAD; NADP; Phosphogluconate Dehydrogenase; Rats; Starvation

Topics: Acid Phosphatase; Adipose Tissue; Alkaline Phosphatase; Animals; Epididymis; Esterases; Glycogen; Histocytochemistry; Male; Mesentery; Nutritional Physiological Phenomena; Rats; Starvation

Topics: Acid Phosphatase; Animals; Azo Compounds; Cell Nucleus; Chelating Agents; Clitoris; Cytoplasm; Endoplasmic Reticulum; Female; Glucuronidase; Golgi Apparatus; Histocytochemistry; Kidney; Lipids; Liver; Lysosomes; Mercury; Mice; Microscopy; Microscopy, Electron; Naphthalenes; Rats; Starvation

Topics: Acid Phosphatase; Adaptation, Physiological; Animals; Body Weight; Cathepsins; Diet; Female; Galactosidases; Glucuronidase; Hydrolases; Kidney; Liver; Lysosomes; Organ Size; Proteins; Rats; Starvation; Sulfatases; Time Factors

Topics: Acid Phosphatase; Adrenal Glands; Adrenocorticotropic Hormone; Alkaline Phosphatase; Animals; Cats; Cattle; Female; Fetus; Guinea Pigs; Histocytochemistry; Horses; Humans; Hypoxia; Male; Mice; Rabbits; Rats; Sex Factors; Sheep; Species Specificity; Starvation

Topics: Acid Phosphatase; Alloxan; Animals; Blood Glucose; Carbon Isotopes; Dactinomycin; Depression, Chemical; Detergents; Diabetes Mellitus, Experimental; Endoplasmic Reticulum; Glucose-6-Phosphatase; In Vitro Techniques; Insulin; Kinetics; Liver; Methods; Microscopy, Electron; Microsomes, Liver; Microtomy; Puromycin; Rats; Starvation; Stimulation, Chemical; Time Factors

Topics: Acid Phosphatase; Animals; Caseins; Diet; Hydrogen-Ion Concentration; Liver; Male; Nitrogen; Peptide Hydrolases; Rats; Starvation; Zea mays

Topics: Acid Phosphatase; Cell Nucleolus; Cell Nucleus; Cytoplasm; Dihydrolipoamide Dehydrogenase; Feeding Behavior; Glycogen; Histocytochemistry; Inclusion Bodies; Insecta; Larva; Lipid Metabolism; Lipids; Methods; Microscopy, Electron; Mitochondria; Mitochondrial Swelling; Mitosis; Nucleoproteins; Oxygen Consumption; RNA; Staining and Labeling; Starvation; Time Factors

Topics: Acid Phosphatase; Animals; Chronic Disease; Estrus; Female; Hemosiderosis; Histocytochemistry; Kidney; Kidney Tubules; Microscopy, Electron; Pregnancy; Rats; Starvation

Topics: Acid Phosphatase; Animals; Diet; Electrons; Histological Techniques; Metabolism; Microscopy; Microscopy, Electron; Pancreas; Pathology; Phosphates; Protein Deficiency; Rabbits; Research; Starvation

Topics: Acid Phosphatase; Clinical Enzyme Tests; Liver; Methylprednisolone; Starvation

Topics: Acid Phosphatase; Alkaline Phosphatase; Electron Transport Complex II; Liver; Liver Glycogen; Rats; Research; Starvation; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Cortisone; Phosphoric Monoester Hydrolases; Rats; Starvation

Topics: Acid Phosphatase; Animals; Hepatocytes; Liver; Mitochondria; Oryzias; Phosphoric Monoester Hydrolases; Polysaccharides; RNA; Starvation

Topics: Acid Phosphatase; Animals; Fishes; Hepatocytes; Liver; Mitochondria; Oryzias; Polysaccharides; RNA; Starvation

Topics: Acid Phosphatase; Animals; Fishes; Hepatocytes; Liver; Mitochondria; Nucleic Acids; Oryzias; Polysaccharides; RNA; Starvation