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At least 217 records · Page 12Linked to original sources
PubMed1990

Enalapril and low protein reverse chronic puromycin aminonucleoside nephropathy.

The effects of dietary protein and converting enzyme inhibition (CEI) on chronic puromycin aminonucleoside nephropathy (PAN) were studied. PAN was induced with seven SQ injections of puromycin aminonucleoside 20 mg/kg over 10 weeks in male Sprague-Dawley rats. The rats were divided into a 22.5% protein diet group (Gr 1), a 6% protein diet group (Gr 2), and an enalapril-treated group on 22.5% protein diet (Gr 3). Group 4 animals served as age-matched controls. Both diets were isocaloric and had the same phosphorus content. Rats from groups 1, 2, and 4 were sacrificed at 12, 18 and 24 weeks. Five rats of group 3 were sacrificed at 12 weeks, and the others were divided in subgroups 3A (diet changed to 6% protein) and 3B (no changes); half of each subgroup was sacrificed at 18 and 24 weeks, respectively. Group 2 had significantly less proteinuria than group 1 at all times. Group 3 had the same proteinuria as group 1 until 12 weeks and then began to decrease. In group 3A proteinuria decreased to group 2 levels, while in group 3B the decrease was slower but still prominent. Early lesions of focal and segmental glomerular sclerosis/hyalinosis (FSH) were present in groups 1, 2, 3 at 12 weeks (16 +/- 1.2%, 15 +/- 1.3%, 7 +/- 1.3%, respectively, versus 1.3 +/- 0.4% in controls), but by 18 weeks a reversal in FSH was seen in groups 2 and 3A/B (3 +/- 1.6%, 2 +/- 0.4%, and 3 +/- 0.9%, respectively, vs. 14 +/- 1.5% in group 1).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1964

EFFECTS OF PUROMYCIN ON THE NUCLEOPROTEINS OF THE HELA CELL.

The effects of several concentrations of puromycin on the nucleoproteins of HeLa cells grown in monolayers were studied by cytochemical and biochemical techniques. The earliest change at all concentrations of puromycin was a decrease in a granular form of ribonucleoprotein (RNP) that is demonstrable in the normal HeLa cell by the toluidine blue-molybdate (TBM) stain. The other types of RNP revealed by the TBM method were unaltered although the cell volume decreased markedly. Treatment with high concentrations of the antimetabolite resulted in pre-prophase inhibition of mitotic division and led to production of inclusions containing RNP in the cytoplasm; lower concentrations resulted in metaphase arrest. Biochemical analyses confirmed the cytochemical observations and indicated that synthesis of RNA and protein was inhibited to the same extent.

Cell Nucleus↗
PubMed1964

INTESTINAL PHOSPHATASE ACTIVITY: ACCELERATION OF INCREASE BY PUROMYCIN AND ACTINOMYCIN.

Alkaline phosphatase activity of the mouse duodenum normally increases 20-fold between 13 and 20 days. Activity at 15 days is raised two to three times above normal by administering actinomycin D, puromycin, or the aminonucleoside of puromycin at 13 or 14 days. Phosphatase activity in the jejunum and kidney are not similarly affected.

Alkaline Phosphatase↗
PubMed1964

STREPTOMYCINOID ANTIBIOTICS: SYNERGISM BY PUROMYCIN.

Puromycin synergizes the lethal action of streptomycin and related antibiotics. This is interpreted to mean that puromycin action uncovers a sensitive site (or sites) on the 30S ribosome. The streptomycinoid antibiotics can then associate more readily with the ribosome and inhibit further synthesis of valid protein.

Anti-Bacterial Agents↗
PubMed1987

Failure of angiotensin converting enzyme inhibition to affect the course of chronic puromycin aminonucleoside nephropathy.

The effects of the angiotensin converting enzyme (ACE) inhibitor enalapril on the proteinuria and degree of focal glomerular sclerosis hyalinosis (FSH) in chronic puromycin aminonucleoside nephropathy (PAN) were examined. Chronic PAN was induced in male Sprague-Dawley rats by seven subcutaneous injections of puromycin aminonucleoside (20 mg/kg) over 10 weeks (Groups I and II). Group II rats also received enalapril 10 mg/kg/day in the drinking water throughout the study (12 weeks). Group III rats served as age-matched controls. Proteinuria was similar in Groups I and II (35.5 +/- 9.7 versus 29.1 +/- 4.1 mg protein/mg creatinine, mean +/- SEM, P greater than 0.05). Serum creatinine remained unchanged in Group I, but rose from 0.7 +/- 0.04 to 1.2 +/- 0.1 mg/dl (mean +/- SEM, P less than 0.05) in Group II. FSH was 13.8% in Group I, 12.9% in Group II (P greater than 0.05), and 0.6% in Group III. There was no significant difference in glomerular lipid content and in immunofluorescence for rat albumin, fibrinogen, IgM, IgG, and C3 between Groups I and II. ACE activity was inhibited by 94% in serum, 83% in lungs, and 92% in kidneys; and blood pressure response to. Angiotensin I challenge was decreased by 50% in rats similarly treated with enalapril versus controls. In summary, proteinuria and glomerular sclerosis in this model are not affected by ACE inhibition.

Angiotensin I↗
PubMed1984

Alterations in proteoglycan metabolism in the nephrotic syndrome induced by the aminonucleoside of puromycin.

The synthesis of intact proteoglycans and their glycosaminoglycan (GAG) side chains by isolated rat glomeruli in vitro were studied both at the onset (5 days) and at the point of maximal proteinuria (7 days) of the nephrotic syndrome induced with the aminonucleoside of puromycin. Glomeruli from nephrotic animals incorporated 1.5-fold and 3.0-fold more 35SO4 label into GAG than glomeruli from control animals at 5 and 7 days, respectively, with heparan-35SO4 GAG being responsible for the majority of the increment. Both nephrotic and control incubations contained 60% of the label in the incubation medium, 40% in the glomerular fractions, and less than 1% in the glomerular basement membrane. Glomerular basement membrane from nephrotic rats had no change in their total heparan-35SO4 GAG content. The majority of intact proteoglycan(s) from the glomerular matrix and from the incubation medium of nephrotic and control animals was found in the most buoyantly dense fraction of CsCl gradients (fraction 1). 35S-labeled material isolated from glomeruli of nephrotic animals showed a consistent shift toward lower density gradient fractions, indicating a decrease in their overall carbohydrate to protein ratio. Diethylaminoethyl chromatography of fraction 1 proteoglycan showed a single biphasic peak with the nephrotic rat having an increase in the proportion contributed by the earlier component of the peak. Fraction 1 proteoglycan(s) from the nephrotic experiment was found to have a smaller average hydrodynamic size by Sepharose CL-2B chromatography without a significant change in the corresponding 35S-GAG chain sizes (molecular weight 14,000) by Sepharose CL-6B chromatography. 35S-macromolecules from glomeruli of nephrotic and control rats that appeared in the middle of the CsCl gradients (fraction 3) had similar Sepharose CL-2B elution volumes, whereas the corresponding 35S-GAG chains from incubations of glomeruli from nephrotic animals were smaller. Increased synthesis of heparan sulfate proteoglycan by glomeruli from puromycin aminonucleoside-induced nephrotic rats may be compensatory to loss of another component of the glomerular filtration barrier or may result from abnormal interaction of proteoglycan(s) from nephrotic animals with other glomerular matrix constituents.

Animals↗
PubMed1984

Inhibition of glomerular visceral epithelial cell endocytosis during nephrosis induced by puromycin aminonucleoside.

Puromycin aminonucleoside (PA), injected intravenously into rats in a single dose, causes proteinuria and ultrastructural pathology reminiscent of human lipoid nephrosis (puromycin aminonucleoside nephrosis (PAN]. Glomerular epithelial cell (GEC) endocytosis was studied in this model and in rats with protein-overload proteinuria using ultrastructural morphometry. Disappearance curves were constructed for protamine-heparin aggregates (PHA), which localized in the subepithelial region of the glomerular basal lamina following intravenous injection of protamine followed by heparin. Five groups were studied: (a) preproteinuric PAN, 4 days after PA (mean 4.5 +/- 1.5 mg of urinary protein/24 hours); (b) proteinuric PAN, 10 days after PA (mean 128 +/- 9.6 mg/24 hours); (c) recovery from PAN (mean 12.5 +/- 1.5 mg/24 hours); (d) protein-overload proteinuria, induced by injecting albumin intraperitoneally (mean 211 +/- 15.9 mg/24 hours); and (e) saline-injected controls (mean 1.2 +/- 0.2 mg/24 hours). Only the proteinuric PAN animals (group 2) had altered GEC endocytosis with a PHA half-disappearance time different from the group 5 saline controls (143.2 versus 72.6 minutes, p less than 0.05). The half-disappearance times in groups 1, 3, and 4 were 74.6, 80.7 and 86.5 minutes, respectively. Altered GEC function was further characterized by comparing PHA disappearance with the abundance of albumin-filled vacuoles in the GEC. Prolongation of PHA disappearance in group 2 correlated with the virtual absence of vacuoles; they were abundant in nonproteinuric phases of PAN and in animals with overload proteinuria. We conclude (a) GEC endocytosis is reduced only during the proteinuric phase of PAN, (b) GEC endocytosis is active during the preproteinuric phase of PAN and is a factor that may account for the absence of protein in the urine despite abnormal GBM permeability, (c) decreased GEC endocytosis during proteinuric PAN reflects abnormal cell metabolism due to PA and is not simply a consequence of albuminuria, as overload proteinuria did not produce diminished PHA or albumin uptake.

Animals↗
PubMed1987

Induction of heat shock proteins in Chinese hamster ovary cells and development of thermotolerance by intermediate concentrations of puromycin.

During 4 hr after puromycin (PUR: 20 micrograms/ml) treatment, the synthesis of three major heat shock protein families (HSPs: Mr = 110,000, 87,000, and 70,000) was enhanced 1.5-fold relative to that of untreated cells, as studied by one-dimensional gel electrophoresis. The increase of unique HSPs, if studied with two-dimensional gels, would probably be much greater. In parallel, thermotolerance was observed at 10(-3) isosurvival as a thermotolerance ratio (TTR) of either 2 or greater than 5 after heating at either 45.5 degrees C or 43 degrees C, respectively. However, thermotolerance was induced by only intermediate concentrations (3-30 micrograms/ml) of puromycin that inhibited protein synthesis by 15-80%; a high concentration of PUR (100 micrograms/ml) that inhibited protein synthesis by 95% did not induce either HSPs or thermotolerance. Also, thermotolerance was never induced by any concentration (0.01-10 micrograms/ml) of cycloheximide that inhibited protein synthesis by 5-94%. Furthermore, after PUR (20 micrograms/ml) treatment, the addition of cycloheximide (CHM: 10 micrograms/ml), at a concentration that reduces protein synthesis by 94%, inhibited both thermotolerance and synthesis of HSP families. Thus, thermotolerance induced by intermediate concentrations of PUR correlated with an increase in newly synthesized HSP families. This thermotolerance phenomenon was compared with another phenomenon termed heat resistance and observed when cells were heated at 43 degrees C in the presence of CHM or PUR immediately after a 2-hr pretreatment with CHM or PUR. Heat protection increased with inhibition of synthesis of both total protein and HSP families. Moreover, this heat protection decayed rapidly as the interval between pretreatment and heating increased to 1-2 hr, and did not have any obvious relationship to the synthesis of HSP families. Therefore, there are two distinctly different pathways for developing thermal resistance. The first is thermotolerance after intermediate concentrations of PUR treatment, and it requires incubation after treatment and apparently the synthesis of HSP families. The second is resistance to heat after CHM or PUR treatment immediately before and during heating at 43 degrees C, and it apparently does not require synthesis of HSP families. This second pathway not requiring the synthesis of HSP families also was observed by the increase in thermotolerance at 45.5 degrees C caused by heating at 43 degrees C after cells were incubated for 2-4 hr following pretreatment with an intermediate concentration of PUR.

Animals↗
PubMed1992

Tunicamycin, puromycin and brefeldin A influence the subcellular distribution of neuropeptides in hypothalamic magnocellular neurones of rat.

Magnocellular neurones in the supraoptic nuclei of normal Long Evans and homozygous Brattleboro rats were examined electron-microscopically after intracisternal injections of tunicamycin, puromycin, or brefeldin A. Moderate (50 micrograms) or high (200 micrograms) doses of tunicamycin caused the formation of electron-dense filamentous accretions in the endoplasmic reticulum (ER) cisterns of vasopressin neurones, but only the high dose of tunicamycin also caused accretions to form in the ER of some oxytocin neurones. Immunogold labelling of ultrathin sections from tunicamycin-treated rats revealed that, in about 5% of vasopressin neurones, the accretions could be immunogold-labelled for vasopressin and its associated neurophysin. However, in the majority of vasopressin neurones, the sections required trypsinisation before immunolabelling of the accretions could be detected. Small accretions in the ER of oxytocin neurones did not label for oxytocin or its neurophysin without prior trypsinisation, whereas larger accretions in other oxytocin cells could be labelled without prior trypsin treatment. Administration of puromycin resulted in the formation of small ER accretions in both vasopressin and oxytocin neurones. These accretions were immunolabelled with antisera, respectively, to vasopressin and oxytocin, but neurophysin-immunoreactivity was in most cases absent and was not revealed by treatment with trypsin, suggesting that neurophysin-immunoreactive epitopes were absent from truncated peptides forming the accretions. Brefeldin A caused dilatation of ER cisterns and disruption of the Golgi apparatus in both oxytocin and vasopressin neurones, but did not cause accretions to form in the ER.

Animals↗
PubMed1988

Effects of glucose starvation and puromycin treatment on lipid-linked oligosaccharide precursors and biosynthetic enzymes in Chinese hamster ovary cells in vivo and in vitro.

Previous studies from several laboratories have demonstrated that glucose-starved Chinese hamster ovary (CHO) cells and other cells in culture switch from synthesis of the normal Glc3Man9GlcNAc2-P-P-Dol to Man5-GlcNAc2-P-P-Dol. In this study we have investigated this phenomenon in CHO cells in vitro and in vivo in order to determine the possible site of this block. Our results demonstrate that enzymatic activities responsible for Man9GlcNA2 synthesis in vitro are normal in glucose-starved cells. In vivo, however, the pool of GDP-[3H]Man is severely depleted, while [3H]mannose incorporation into lipid-linked and protein-bound Man5GlcNAc2 is increased. This result suggests that the available GDP-Man in starved cells is utilized to synthesize Man5GlcNAc2 preferentially, resulting in a reduction of Dol-P-Man and Man6-Man9 GlcNAc2 synthesis in vivo in glucose-starved cells. Conditions which prevent the depletion of GDP-[3H]Man in glucose-starved cells, such as puromycin or cycloheximide treatment, result in normal synthesis of Man9GlcNAc2 by glucose-starved cells. An unexpected finding in the course of this study is that puromycin or cycloheximide treatment of cells, which is known to inhibit lipid-linked oligosaccharide synthesis in glucose-fed cells, has no such inhibitory effect on glucose-starved cells.

Adenosine Triphosphate↗
PubMed1979

Peptidyl-puromycin synthesis by free and membrane-bound ribosomes.

The peptidyl transferase reaction, as measured by the formation of peptidyl-puromycin, was compared for free ribosomes and ribosomes bound to two types of membrane, the endoplasmic reticulum and the outer nuclear membrane. In most respects the reaction catalyzed by the three types of ribosome was similar, demonstrating that interaction of the 60 S ribosomal subunit with the membrane has little effect on the functioning of peptidyl transferase, a 60 S protein. However, both the rate and extent of synthesis of peptidyl puromycin were lower for ribosomes bound to the nuclear membrane than for free or microsome-bound ribosomes. This difference appears to be a direct consequence of the ribosome-membrane interaction, since ribosomes stripped from the nuclear membrane could not be distinguished from the other classes of ribosome.

Acyltransferases↗
PubMed1985

Feminization of the hepatic monooxygenases by growth hormone is mimicked by puromycin and correlates with a decrease in male-type cytochrome P450.

The hepatic monooxygenase system (MFO) was studied in hypophysectomized male rats treated with growth hormone (GH), puromycin, or both. GH significantly decreased the amount of cytochrome P450 and the activity of ethylmorphine demethylase but did not affect aniline hydroxylase or NADPH cytochrome c reductase. Puromycin significantly increased the activity of the reductase but otherwise had effects identical to GH. The agent's effects were additive. By labelling the P450 with [3H]-heme we found that GH decreased the amount of male-type (slow turnover) P450 by 56% but lowered the female-type (fast turnover) by only 10%. The hormone increased the half-life of both types by 56 and 100% respectively. We conclude that GH feminizes the MFO by decreasing the synthesis of male-type cytochrome P450.

Aniline Hydroxylase↗
PubMed1977

Dose-response relationships in attenuation of puromycin-induced amnesia by neurohypophyseal peptides.

Intracerebral injections of puromycin one day after training of mice in a Y-maze cause amnesia when the animals are tested 7 days later. This amnesia was shown to be attenuated by various neurohypophyseal hormones, analogs and fragments, administered subcutaneously immediately after training. Dose-response relationships have been obtained for the attenuation of puromycin-induced amnesia in mice by selected neurohypophyseal peptides. All of the compounds tested reduce the amnesia in a dose-related way, suggesting that these peptides may interact with specific receptors to induce their central effect. Among the peptides studied the two most potent--i.e., those that cause substantial retention of memory at the lowest doses--are the neurohypophyseal hormone arginine vasopressin and Z-prolyl-leucyl-glycinamide (Z-MIF).

Amnesia↗
PubMed1993

Dup 753 prevents the development of puromycin aminonucleoside-induced nephrosis.

The appearance of nephrotic syndromes such as proteinuria, hypoalbuminemia, hypercholesterolemia and increase in blood nitrogen urea, induced in rats by injection of puromycin aminonucleoside was markedly inhibited by oral administration of Dup 753 (losartan), a novel angiotensin II receptor antagonist, at a dose of 1 or 2 mg/kg per day. The results suggest a possible involvement of the renin-angiotensin system in the development of puromycin aminonucleoside-induced nephrosis.

Angiotensin II↗
PubMed1992

Reduced puromycin sensitivity of translocated polysomes after the addition of elongation factor 2 and non-hydrolysable GTP analogues.

Treatment of reticulocyte polysomes with elongation factor eEF-2 and GTP led to an increased sensitivity of peptidyl-tRNA for puromycin as a result of the translocation from the ribosomal A-site to the P-site. Upon addition of an excess of the non-hydrolysable GTP analogue, GuoPP[CH2]P, the puromycin sensitivity decreased rapidly. The decrease in sensitivity required high concentrations of eEF-2 with half maximal effect at an eEF-2 concentration of around 1 microM. The data suggest either that peptidyl-tRNA had re-translocated back to the A-site due to the higher affinity of eEF-2 for the pre-translocation than for the post-translocation ribosome, or that the eEF-2-GuoPP[CH2]P complex blocks the peptidyl-transferase activity.

Animals↗
PubMed1989

Low density lipoprotein metabolism in rats with puromycin aminonucleoside-induced nephrotic syndrome.

With puromycin aminonucleoside-induced nephrotic syndrome (NS) in rats, twofold elevated levels of lipoproteins were observed. These levels were not related to proteinuria or to plasma albumin levels. Ultrastructural lesions induced in the kidneys by puromycin aminonucleoside were consistent with NS, while there was little or no hepatic involvement. Apolipoprotein B (apo B) kinetic measurements using homologous 125I-labeled low density lipoproteins (LDL) demonstrated a higher synthetic rate in nephrotic rats relative to controls (6.18 +/- 1.86 micrograms x g-1 x d-1 v 3.94 +/- 0.66 micrograms x g-1 x d-1 respectively, P less than .005), while the fractional catabolic rate was only marginally reduced (1.64 +/- 0.28 pools x day-1 in NS v 1.83 +/- 0.37 pools x day-1 in controls, P less than 0.4). These results indicate that in rats with experimentally induced NS, the expanded apo B-LDL pool results from increased synthesis of this apoprotein while no significant role can be ascribed to alterations in its catabolism. These data are consistent with our preliminary findings in NS in humans.

Animals↗
PubMed1978

ADH and related peptides: effect of pre- or posttraining treatment on puromycin amnesia.

The peptide Z-Pro-Leu-Gly-NH2 attenuated puromycin-induced amnesia in mice when administered 5 days prior to training, while arginine vasopressin, lysine vasopressin and cyclo(Leu-Gly), were effective when given 24 hr before training. The activity of all peptides to inhibit puromycin-induced amnesia decreased as the interval after training and before peptide administration increased, suggesting that the peptides influence memory processes rather than generalized arousal mechanisms.

Animals↗