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PubMed1991

Anionic site and immunogold quantitation of heparan sulfate proteoglycans in glomerular basement membranes of puromycin aminonucleoside nephrotic rats.

Renal glomerular basement membranes (GBMs) exhibit a charge-selective barrier, consisting of heparan sulfate proteoglycan (HSPG) that restricts the passage of anionic molecules into the urine. Previous efforts to localize the HSPG core protein within various layers of the GBM have been contradictory. Furthermore, attempts to correlate proteinuria in several disease states with a decrease in anionic sites of HSPG core protein have yielded conflicting results. When antibodies to HSPG from the EHS tumor matrix [anti-(EHS) HSPG] and GBMs [anti-(GBM) HSPG] were used together with immunogold to label renal tissues from puromycin aminonucleoside nephrotic (PAN) rats, immunolabeling results indicated that a portion of the protein core recognized by anti-(EHS) HSPG was significantly reduced, while immunolabeling with anti-(GBM) HSPG was only slightly reduced in early PAN. Anionic sites (stained with the cationic probe, polyethyleneimine) within the lamina rara externa of the GBM remained unaltered throughout the course of PAN.

Animals↗
PubMed2002

Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins.

We previously reported that mouse orthologue of puromycin insensitive leucyl-specific aminopeptidase (mPILSAP) played an important role in angiogenesis by regulating the proliferation and migration of endothelial cells (ECs) (Miyashita et al., 2002. Blood 99:3241-3249). Here, we examined the mechanism as to how mPILSAP regulates the migration of ECs. Cell adhesion through integrins plays a crucial role in cell migration, and ECs use at least type-1 collagen receptor integrin alpha2beta1, fibronectin receptor alpha5beta1, and vitronectin receptors alphavbeta3 and alphavbeta5. mPILSAP antisense oligodeoxynucleotide (AS-ODN) or leucinethiol (LT), a leucyl-aminopeptidase inhibitor, did not affect the attachment but did significantly inhibit the spreading of cells of the murine endothelial cell line MSS31 when they were plated on vitronectin-, fibronectin-, or type-1 collagen, although they did not affect the expression of integrin alpha2, alpha5, alphav, beta1, beta3, and beta5 subunits on the cell surface. AS-ODN and LT also inhibited the tyrosine phosphorylation of FAK when cells were plated on vitronectin, fibronectin, or type-1 collagen. This inhibition of cell spreading and of tyrosine phosphorylation of FAK could be negated by Mg(2+). These results suggest that mPILSAP is involved in the activation of endothelial integrins.

Androstadienes↗
PubMed1980

Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides.

Four major acidic polypeptides, with molecular weights of 88, 72, 71, and 23 thousand, and minor polypeptides with molecular weights of 110, 50, 38, and 30 thousand rapidly accumulated in cultured chick embryo (CE) cells which were exposed for three hours to the arginine analogue canavanine. P110, P88, P71,72, and P23 had unique peptide maps. Evidence of a 27,000 dalton precursor to P23 was obtained. The analogue-stimulated proteins were not related to another set of inducible avian polypeptides known as the glucose-regulated proteins. In mammalian cells, the rate of accumulation of several polypeptides, which were similar in size to the avian proteins, sharply increased after canavanine treatment. Proteins with the same electrophoretic mobilities, isoelectric points, and peptide maps as the analogue-stimulated proteins were expressed at low levels in untreated cultures. To determine the time courses of the canavanine-mediated increases in protein accumulation and the recovery of protein metabolism after analogue treatment, radioactively labeled proteins were extracted from CE cells and analyzed on SDS-polyacrylamide gels. In cultures exposed to canavanine, the rates of accumulation of P88 and P71,72 increased from basal to new plateau levels in about 1.5 hours, while P23 required about 2.5 hours. When added with the analogue, actinomycin D and cordycepin blocked the increases in protein accumulation. These inhibitors also blocked the rapid decline in the rates of accumulation of the enhanced proteins which occurred after removal of canavanine. Studies of the matabolic stability of the enhanced proteins indicated that the changes in their accumulation were caused by alterations in their rates of synthesis. Thus, the analogue-mediated response fulfilled several of the criteria for inducible eucaryotic gene expression. The amino acid analogue p-fluorophenylalanine and the chain-terminating analogue of amino acyl-tRNA puromycin stimulated the synthesis of the same set of proteins induced by canavanine. The enhanced synthesis of these proteins appeared to be a cellular response to either the presence or catabolism of abnormal proteins and puromycyl peptides.

Amino Acids↗
PubMed1987

Effect of cycloheximide or puromycin on induction of thermotolerance by sodium arsenite in Chinese hamster ovary cells: involvement of heat shock proteins.

After sodium arsenite (100 microM) treatment, the synthesis of three major heat shock protein families (HSPs; Mr = 110,000, 87,000, and 70,000), as studied with one-dimensional gels, was enhanced twofold relative to that of unheated cells. The increase of unique HSPs, if studied with two-dimensional gels, would probably be much greater. In parallel, thermotolerance was observed as a 100,000-fold increase in survival from 10(-6) to 10(-1) after 4 hr at 43 degrees C, and as a thermotolerance ratio (TTR) of 2-3 at 10(-3) isosurvival for heating at 45.5 degrees C. Cycloheximide (CHM: 10 micrograms/ml) or puromycin (PUR: 100 micrograms/ml), which inhibited total protein synthesis and HSP synthesis by 95%, completely suppressed the development of thermotolerance when either drug was added after sodium arsenite treatment and removed prior to the subsequent heat treatment. Therefore, thermotolerance induced by arsenite treatment correlated with an increase in newly synthesized HSPs. However, with or without arsenite treatment, CHM or PUR added 2-6 hr before heating and left on during heating caused a 10,000-100,000-fold enhancement of survival when cells were heated at 43 degrees C for 4 hr, even though very little synthesis of heat shock proteins occurred. Moreover, these cells manifesting resistance to heating at 43 degrees C after CHM treatment were much different than those manifesting resistance to 43 degrees C after arsenite treatment. Arsenite-treated cells showed a great deal of thermotolerance (TTR of about 10) when they were heated at 45 degrees C after 5 hr of heating at 43 degrees C, compared with less thermotolerance (TTR of about 2) for the CHM-treated cells heated at 45 degrees C after 5 hr of heating at 43 degrees C. Therefore, there are two different phenomena. The first is thermotolerance after arsenite treatment (observed at 43 degrees C or 45.5 degrees C) that apparently requires synthesis of HSPs. The second is resistance to heat after CHM or PUR treatment before and during heating (observed at 43 degrees C with little resistance at 45.5 degrees C) that apparently does not require synthesis of HSPs. This phenomenon not requiring the synthesis of HSPs also was observed by the large increase in thermotolerance to 45 degrees C caused by heating at 43 degrees C, with or without CHM, after cells were incubated for 6 hr following arsenite pretreatment. For both phenomena, a model based on synthesis and redistribution of HSPs is presented.

Animals↗
PubMed1988

Thermotolerance induced by heat, sodium arsenite, or puromycin: its inhibition and differences between 43 degrees C and 45 degrees C.

When CHO cells were treated either for 10 min at 45-45.5 degrees C or for 1 hr with 100 microM sodium arsenite (ARS) or for 2 hr with 20 micrograms/ml puromycin (PUR-20), they became thermotolerant to a heat treatment at 45-45.5 degrees C administered 4-14 hr later, with thermotolerance ratios at 10(-3) isosurvival of 4-6, 2-3.2, and 1.7, respectively. These treatments caused an increase in synthesis of HSP families (70, 87, and 110 kDa) relative to total protein synthesis. However, for a given amount of thermotolerance, the ARS and PUR-20 treatments induced 4 times more synthesis than the heat treatment. This decreased effectiveness of the ARS treatment may occur because ARS has been reported to stimulate minimal redistribution of HSP-70 to the nucleus and nucleolus. Inhibiting protein synthesis with cycloheximide (CHM, 10 micrograms/ml) or PUR (100 micrograms/ml) after the initial treatments greatly inhibited thermotolerance to 45-45.5 degrees C in all cases. However, for a challenge at 43 degrees C, thermotolerance was inhibited only for the ARS and PUR-20 treatments. CHM did not suppress heat-induced thermotolerance to 43 degrees C, which was the same as heat protection observed when CHM was added before and during heating at 43 degrees C without the initial heat treatment. These differences between the initial treatments and between 43 and 45 degrees C may possibly be explained by reports that show that heat causes more redistribution of HSP-70 to the nucleus and nucleolus than ARS and that redistribution of HSP-70 can occur during heating at 42 degrees C with or without the presence of CHM. Heating cells at 43 degrees C for 5 hr after thermotolerance had developed induced additional thermotolerance, as measured with a challenge at 45 degrees C immediately after heating at 43 degrees C. Compared to the nonthermotolerant cells, thermotolerance ratios were 10 for the ARS treatment and 8.5 for the initial heat treatment. Adding CHM (10 micrograms/ml) or PUR (100 micrograms/ml) to inhibit protein synthesis during heating at 43 degrees C did not greatly reduce this additional thermotolerance. If, however, protein synthesis was inhibited between the initial heat treatment and heating at 43 degrees C, protein synthesis was required during 43 degrees C for the development of additional thermotolerance to 45 degrees C.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1983

A morphometric, biochemical and histochemical comparison of puromycin aminonucleoside and hyperalbuminaemic induced proteinurias in the female Wistar rat.

Biochemical, immunological, histochemical and electron microscope morphometric techniques were used to monitor the changes in urinary protein composition, albumin clearance and glomerular ultrastructure induced in female Wistar rats following i.p. injection of puromycin aminonucleoside (PAN) or bovine albumin (BSA). BSA injected rats maintained a high degree of selectivity with albumin constituting 90 per cent. of the total protein excreted even when mean protein excretion was in the order of 500 mg/24 hr. A similar degree of selectivity was only evident in PAN nephrotic rats at low levels of proteinuria. Levels of 500 mg/24 hr only 57 per cent. of the total protein was albumin. These differences correlated well with the increased number of glomeruli from PAN nephrotics compared with hyperalbuminaemic rats which, at these high levels of proteinuria, had bare areas of glomerular basement membrane caused by epithelial cell detachment (88 and 7 per cent. respectively). Detailed electron microscope morphometric and immunohistochemical studies showed that there were also important quantitative differences in a number of superficially similar glomerular structural alterations. In PAN nephrotic rats all glomeruli showed very marked epithelial cell foot process loss and reduced staining with colloidal iron. In glomeruli from hyperalbuminaemic rats there was a wide variation in the extent of epithelial cell foot process loss and reduced colloidal iron staining was only demonstrable in those glomeruli which had swollen epithelial containing large numbers of vacuoles and protein droplets. Similarly, while protein droplets were smaller and less numerous in glomeruli from PAN-injected rats, they were present in most glomeruli whereas their distribution was much more variable in glomeruli from BSA-injected rats. All the data collected therefore indicated that there were important differences in the types of proteinuria and glomerular ultrastructural damage present in PAN nephrotic and hyperalbuminaemic rats and suggested that their induction may have involved entirely different mechanisms. Evidence gathered from one experimental model should thus only be used with extreme caution to aid in interpretation of data obtained from the other.

Albuminuria↗
PubMed2000

Early indication of effects of puromycin aminonucleoside using a fluorimetric assay of 2-aminoacridone-derivatized carbohydrates in urine.

This paper describes a novel noninvasive method to study the changes in free carbohydrates excreted in urine as a result of toxicity in the rat induced by the administration of puromycin aminonucleoside (PAN). Urine samples were collected for 24 h prior to dosing and at 8, 24, and 32 h postdosing. For each sample, free carbohydrates were extracted from the urine using a graphitized carbon column and then labeled with 2-aminoacridone (2-AMAC) prior to analysis by hydrophilic interaction liquid chromatography (HILC). Dramatic changes were seen in the profile of the carbohydrates at the 8- and 24-h time points. These changes in carbohydrate profiles may be useful as early indicators of toxicity.

Aminoacridines↗
PubMed1996

The relationship of adhesion molecules and leukocyte infiltration in chronic tubulointerstitial nephritis induced by puromycin aminonucleoside in Wistar rats.

We studied the expression of adhesion molecules on infiltrating leukocytes and tubular cells in chronic tubulointerstitial nephritis associated with puromycin aminonucleoside (PA) nephrosis. Rats received injections of PA (2 mg/100 g body wt) weekly for the first 3 weeks and every other week thereafter. Rats were killed at 0, 3, 5, 8, and 12 weeks after the start of injections. From the third to the fifth week, the initial infiltrating cells in interstitial tissue were mainly CD4+ T lymphocytes. At the fifth week, ICAM-1, CD44, and hyaluronate were expressed on infiltrating cells in interstitial tissue. At the eighth week, the number of infiltrating cells reached a peak and consisted of T lymphocytes (CD4, CD8) and macrophages (ED1, MHC class II, CD11b, and CD18). The severity of interstitial infiltration was correlated with the degree of proteinuria and with ICAM-1 expression. Our results suggest that CD4+ T lymphocytes may contribute to the production of initial tubular injury. Expression of ICAM-1 helps mononuclear cells migrate to the interstitium. In addition, expression of CD44 and hyaluronate may play important roles in the chronicity of tubulointerstitial nephritis.

Animals↗
PubMed1997

Heme oxygenase synthesis is induced in cultured lens epithelium by hyperbaric oxygen or puromycin.

We showed previously that treatment of cultured rabbit lens epithelial cells (LECs) with hyperbaric oxygen (HBO) produced DNA strand-breaks, caused reversible inhibition of protein synthesis and induced the synthesis of a 32 kD protein. In the present work, we employed immunostaining procedures to identify the 32 kD protein as heme oxygenase-1 (HO-1). Increased synthesis of the enzyme was observed as early as 12 hr after HBO-treatment, reached a maximum at 18 hr and was not detectable at 36 hr. Exposure of the cells to hemin also increased the synthesis of HO-1. An HBO-induced inhibition of protein synthesis and the subsequent induction of HO-1 was also observed in the capsule-epithelium of cultured rabbit lenses. For both LECs and the cultured lens, only HO-1 and not heme oxygenase-2 was HBO-inducible. Use of the antioxidant dimethylthiourea with HBO-treated lenses or LECs did not alter the observed effects on protein synthesis or the induction of HO-1. In contrast to results obtained with 50 atm O2, a pressure of 25 atm O2 inhibited protein synthesis only slightly and failed to induce synthesis of the 32 kD protein (although, as shown previously, identical exposure of LECs to 25 atm O2 significantly damaged DNA). Inhibition of protein synthesis in LECs and cultured lenses with the use of puromycin also induced synthesis of HO-1. Both hemin (10 micron), a source of iron, and 50 atm O2 produced a three-fold increase in the concentration of ferritin, a natural iron chelator, in LECs two days after exposure; no effects on ferritin levels were observed after 1 or 3 days. The finding that the increase in ferritin concentration occurred in the cells significantly after hemin- or HBO-induced synthesis of heme oxygenase indicates that chelatable iron rather than the heme molecule itself may have been the primary agent responsible for inducing ferritin synthesis. The data suggest that HBO-induced synthesis of HO-1 in the lens epithelium may be the result of an inhibition of protein synthesis, possibly leading to an accumulation of heme, rather than a direct protective response against oxidative stress.

Animals↗
PubMed2001

Puromycin aminonucleoside induces glomerular epithelial cell apoptosis.

Glomerular epithelial cell (GEC) injury has been considered to play an important role in puromycin aminonucleoside (PAN)-induced nephrosis. We studied the effect of PAN on rat as well as human GEC apoptosis. Morphogic evaluation of GEC apoptosis and necrosis was carried out by staining with H-33342 and propidium iodide. GEC apoptosis was further confirmed by DNA fragmentation assay (by both agarose gel electrophoresis and end-labeling). To determine the dose- and time-response effect of PAN, GECs were treated with variable concentrations of PAN (10 to 500 microg/ml) for variable time periods (6 to 48 h). To determine the role of gene synthesis, we studied the effect of actinomycin D (a transcriptional inhibitor) on PAN-induced GEC apoptosis. To determine the role of free radicals, we evaluated the effect of superoxide dismutase (SOD), dimethylthiourea (DMTU), and catalase on PAN-induced GEC apoptosis. PAN induced GEC apoptosis in a dose- and time-dependent manner. PAN at a high concentration (PAN, 100 microg/ml) also induced a moderate degree of GEC necrosis. In DNA fragmentation assays PAN-treated GECs showed the classic ladder pattern. PAN-induced GEC apoptosis was partly attenuated with free radical scavengers, such as SOD, DMTU, and catalase. In addition, actinomycin D attenuated PAN-induced GEC apoptosis. PAN induces GEC apoptosis, which may be mediated through the generation of reactive oxygen species.

Animals↗
PubMed1999

Effect of albumin administration on L-tryptophan levels in the serum and tissues of rats with puromycin aminonucleoside-induced nephrosis.

We examined the effect of albumin administration on L-tryptophan (Trp) levels in the serum and tissues of rats with puromycin aminonucleoside (PAN)-induced nephrosis. PNA-injected rats showed increased urinary protein and serum non-esterified fatty acids levels and decreased serum albumin level at 8 days after the injection. The nephrotic rats showed a decrease in total serum Trp level and increases in free serum Trp and liver and kidney Trp levels but no change in urinary Trp level. At 5 min after intravenous injection of bovine serum albumin, the nephrotic rats had serum albumin concentration similar to the level of non-nephrotic rats and showed a recovery of decreased total serum Trp with the reduction of increased free serum Trp and liver Trp.

Animals↗
PubMed1975

EDTA-and puromycin-derived duck- and rabbit globin-messenger ribonucleoprotein complexes isolated by oligo (dT)-cellulose chromatography.

Duck- and rabbit globin messenger ribonucleoprotein complexes isolated by oligo(dT) cellulose chromatography reveal an identical protein pattern-two main proteins of molecular weights of 73,000 and 49,000 daltons and minor components-whether the complexes have been liberated from polyribosomes with the EDTA- or the puromycin-high-salt method. In the globin messenger ribonucleoprotein particles of both species predominantly the protein with a molecular weight of 73,000 daltons is attached to poly(A)-containing regions of the messenger RNAs.

Animals↗
PubMed1984

An ultrastructural study of the effect of the steroid in puromycin aminonucleoside nephrosis rats.

In order to investigate the significance of the histological change in glomerular epithelial cells in minimal change nephrotic syndrome in man (MCNS) and to help in clarifing the mechanism of action of a steroid in this disease, methylprednisolone was administered to rats with puromycin aminonucleoside nephrosis (PAN). This is an experimental nephrosis having a close resemblance morphologically and physiologically, to human MCNS. Morphological changes in the glomerulus were observed ultrastructurally. The administration of the steroid to PAN rats showed remarkable changes including, rapid disappearance of proteinuria in PAN rats in a manner similer to that seen in human MCNS, and significantly faster recovery of changes in glomerular epithelial cells when compared with spontaneous recovery. From the present study, it is clear that the steroid is effective in rapidly restoring the normal shape of glomerular epithelial cells in PAN rats. The filtration barrier in the glomerular capillary wall (GCW) is also thought to have recovered and proteinuria is cured. Based on these considerations, it may be suggested that proteinuria in human MCNS is caused by changes in glomerular epithelial cells, and that the clinical treatment of proteinuria in MCNS is effective when glomerular epithelial cells have functionally recovered.

Animals↗
PubMed1995

Increased glomerular and urinary malondialdehyde in puromycin aminonucleoside-induced proteinuria in rats.

Puromycin aminonucleoside (PAN)-induced proteinuria in rats may be mediated by reactive oxygen metabolites (ROM), which are injurious to several cell components including membrane lipids. Increased malondialdehyde (MDA) production is indicative of lipid peroxidation. We examined if MDA content of glomeruli and its urinary excretion were increased in rats administered PAN. Of three groups of 8 Sprague-Dawley rats each, group 1 served a control, group 2 animals received a single intravenous injection of PAN (5 mg/100 g body weight) and group 3 animals PAN with intraperitoneal injections of dimethylthiourea (DMTU), a free radical scavenger of oxidants such as hydroxyl radicals, for 4 days. The rats were sacrificed on day 8 after PAN injection. Increasing proteinuria, starting on day 4, developed in animals in group 2 but not in the others. The glomerular MDA (nmol/mg protein) in group 2 animals was 2.93 +/- 1.91, significantly higher than 0.87 +/- 0.63 and 1.26 +/- 0.76 in groups 1 and 3, respectively. Urinary levels of MDA markedly increased in group 2 rats on day 3 and remained high thereafter, but no such increase occurred in the control animals and those administered PAN with DMTU; the latter was thus protective against PAN toxicity. Our observations support the view that ROM are involved in PAN-induced glomerular injury and that increased urinary MDA excretion can be a marker of ROM-mediated lipid peroxidation.

Animals↗
PubMed1993

Ultrastructural changes in glomerular epithelial cells in acute puromycin aminonucleoside nephrosis: a study by high-resolution scanning electron microscopy.

Ultrastructural changes in the podocytes were studied during the development of, and recovery from, acute puromycin aminonucleoside (PAN) nephrosis using high-resolution scanning electron microscopy (hrSEM) and transmission electron microscopy (TEM). In the process of development of PAN nephrosis, four types of early structural changes were observed before total loss of foot processes: formation of cytoplasmic blebs, masking of filtration clefts, flattening of foot processes, and retraction of foot processes. The masking of filtration clefts visualized by hrSEM corresponded to the multiplication of slit diaphragms and adhesion of foot processes in the TEM findings, and preceded retraction of the foot processes. Changes of podocyte configuration were produced. Recovery from this change of podocyte configuration began as islands of podocyte interdigitation, and was proceeded by expansion of the islands. During recovery, the primary processes were re-established either by retraction or perforation of the thin cytoplasm after the formation of foot processes. We conclude that loss of foot processes begins with the masking of filtration clefts. Recovery from the change in podocyte configuration begins with the formation of new foot processes.

Acute Disease↗
PubMed1987

Effects of puromycin on rat embryos in vitro.

Somite-staged rat embryos were exposed to varying concentrations of puromycin for 48 h in vitro. Medium concentrations below 0.92 microM had no significant effects, while concentrations above 1.84 microM were lethal. Between these extremes, there were concentration dependent increases in the incidence of malformations in a close relationship to growth retardation.

Abnormalities, Drug-Induced↗
PubMed1978

Effect of actinomycin D or puromycin on microsomal testosterone hydroxylase activity enhanced by testosterone in female rat liver.

The injection of testosterone propionate for 4 successive days into female rats resulted in an increase of the in vitro conversion of the hydroxylated testosterones from testosterone by the hepatic microsomal fraction, but no change in the content of microsomal cytochrome P-450 occurred. Actinomycin D or puromycin, which was administered for 4 days with injections of testosterone propionate, prevented the enzyme induction.

Animals↗
PubMed1980

Experimental nephrotic syndrome in the rat induced by puromycin aminonucleoside: hepatic synthesis of lipoproteins and apolipoproteins.

Hepatic synthesis of lipoproteins and apolipoproteins was investigated in male Wistar rats with severe nephrotic syndrome induced by puromycin aminonucleoside by incubating liver slices with a mixture of 14C-amino acids. Labeled lipoproteins were separated by preparative ultracentrifugation from the incubation medium after the addition of carrier plasma. The incorporation of 14C-amino acids into very low density lipoproteins (VLDL) (1.006 g/ml), low density lipoproteins (LDL) (1.006-1.063 g/ml) and high density lipoproteins (HDL) (1.063-1.210 g/ml) was increased in nephrotic liver 6.1-, 5.7- and 5.0-fold, respectively. The measurement of radioactivity associated to apolipoproteins isolated by SDS-PAGE documented an increased incorporation into apolipoprotein E (apoE) of nephrotic VLDL (33.1% vs 20% of the total radioactivity incorporated into VLDL apoproteins) and a markedly increased incorporation into apolipoprotein A-I (apo-A-I) of nephrotic HDL (44.3% vs 16.3% of the total radioactivity incorporated into HDL apoproteins). In nephrotic liver, the total incorporation of amino acids into apolipoproteins (apoVLDL + apoLDL + apoHDL) was increased 12.6 times for apo-A-I, 6,4 times for apoB, 5.0 times for apoE, 4.2 times for apoC + apoA-II and 2.5 times for apoA-IV. We suggest that, in nephrotic liver: (a) the synthesis of VLDL, LDL and HDL is increased, and (b) the total synthesis of apoA-I is selectively increased when compared to that of the other apolipoproteins.

Amino Acids↗