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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The increased protein degradation associated with diabetes appears to be different in many respects from protein catabolism in normal, well-nourished cells. In all normal eukaryotic cells examined, degradation of cytosolic proteins exhibits several striking features. Large proteins tend to be degraded more rapidly than small proteins, acidic proteins tend to be degraded more rapidly than neutral or basic proteins, and glycoproteins are degraded more rapidly than non-glycoproteins. Furthermore, a general correlation exists between protein half-life in vivo and susceptibility to proteolytic attack in vitro. In streptozotocin-diabetic rats the relationships between degradative rate and protein size, net charge, and carbohydrate content are absent or markedly reduced among cytosolic proteins of the liver. However, the correlation between protein half-life and susceptibility to proteinase in vitro is unaltered. Therefore, the enhanced protein degradation in diabetes shows little or no selectivity towards large, acidic, glycoproteins but does show specificity for proteins than tend to be sensitive to proteinases. Similar studies using other tissues from diabetic rats are reported and general characteristics of the enhanced liver protein catabolism in starvation and hyperthyroidism are briefly discussed. The biochemical reasons for the increased protein catabolism in diabetes are unclear although several possible explanations are presented. The enhanced breakdown is probably not due to cellular proteins becoming more proteinase sensitive in diabetes since experiments with a variety of endoproteinases including pronase, chymotrypsin, pepsin, and lysosomal cathepsins have failed to demonstrate more rapid digestion of liver proteins from diabetic animals.
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PMID:Protein degradation in metabolic and nutritional disorders. 39 94

Insulin, a mitogen for cultured chick embryo fibroblasts (Temin, H.M. (1968) Cancer 3, 771-787), has been employed to characterize the effects of mitogen/cell membrane interactions as it relates to growth. The specific binding of 125I-insulin to substratum-attached cells is time- and temperature dependent and is optimum at a pH of 7.0. Fetal calf and chicken sera, somatomedin "A/C mixed," and desalanine or native porcine insulin compete with 125I-insulin for membrane-binding sites. Proinsulin, although competing less effectively than native insulin for binding, is more effective than desoctapeptide insulin. Unrelated polypeptide hormones do not compete for 125I-insulin binding. The lowest concentration of insulin at which specific binding is detected is 0.1 nM. Scatchard plot analysis of the binding data indicates that there are two types of binding sites in confluent cultures of fibroblasts: one of high affinity (K1 = 2 to 6 X 10(8) M-1) and low capacity, the other of low affinity (K2 = 0.8 to 3.0 X 10(7) M-1) and high capacity. Approximately 1.9 and 7.1 X 10(3) molecules of insulin are bound at each site, respectively. A 10-min incubation at 24 degrees of the fibroblasts with 10 mug/ml of trypsin causes a 2-fold stimulation of specific 125I-insulin binding and a similar 2-fold increase in insulin-stimulated 2-deoxy-D-glucose uptake and thymidine incorporation. Neuraminidase treatment also produces a 37% increase in specific 125I-insulin binding but treatment with alpha-chymotrypsin or phospholipase C are without significant effect. The results of this and additional experiments support the hypothesis that trypsin treatment of chick embryo fibroblasts leads to an unmasking of 125I-insulin binding sites. Serum starvation of fibroblasts for 12 or 24 h produces a 2.5- to 5-fold increase in specific 125I-insulin binding. This increase is the result of an increase in the number of hormone-binding sites from 9 X 10(3) to 6 X 10(4) per cell which are predominantly of the low affinity type. There is no change in the affinity constants. The presence of camptothecin, or cordycepin, or cycloheximide in the incubation medium completely blocks the increase in number of 125I-insulin-binding sites resulting from serum starvation. The addition of native insulin to the medium of serum-starved cultures also blocks this increase. The magnitude of insulin-stimulated 2-deoxy-D-glucose uptake and thymidine incorporation correlates with the levels of occupancy of the low affinity 125I-insulin-binding sites in untreated fibroblasts. In fibroblasts cultured in the absence of serum, the marked increase in insulin-stimulated 2-deoxy-D-glucose uptake and thymidine incorporation parallels the increase in number of mitogen receptors. The concentration of insulin that produces a half-maximum stimulation of thymidine incorporation is calculated to be 5 X 10(-8) M. At this concentration of insulin, 42% of the receptor sites are occupied.
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PMID:Mitogen receptors in chick embryo fibroblasts. Kinetics, specificity, unmasking, and synthesis of 125I-insulin binding sites. 98 22

We previously found a trypsin-like proteinase which momentarily appears immediately before DNA synthesis in the cell cycle of Escherichia coli synchronized by phosphate starvation and which is closely related to the initiation of DNA replication (Kato, M., Irisawa, T., Morimoto, Y. and Muramatu, M., unpublished results). The proteinase was named proteinase In. It was purified approximately 2880-fold with a recovery of 15%. The isolated enzyme appeared homogeneous by gel filtration and electrophoresis. Its molecular mass was estimated by analytical gel filtration and SDS/PAGE as approximately 66 kDa. The isoelectric point of proteinase In is 4.9 and its optimal pH is approximately 9. Although protein In hydrolyzes fluorogenic substrate for trypsin, its hydrolytic activity seems markedly affected by amino-acid sequence lying towards the N-terminal from the P1 (lysine, arginine) residue. The proteinase does not hydrolyze N2-benzoyl-D,L-arginine-4-nitronanilide and fluorogenic substrates for chymotrypsin and elastase. The proteinase activity is inhibited by leupeptin, antipain and 4-nitrophenyl 4-guanidinobenzoate, but the effects of tosyl-L-lysine chloromethane, diisopropylfluorophosphate, benzamidine and pentamidine isethionate on the proteinase activity are weak or not inhibitory. Its activity is strongly affected in the presence of NaCl and KCl, and at a concentration of 1.5 M, these increase the activity 14-fold and 13-fold, respectively, above that without salt. Proteinase In was strongly inhibited by various esters of trans-4-guanidinomethylcyclohexanecarboxylic acid, and their inhibitory effects were roughly correlated with those on growth of E. coli. Proteinase activity was found in the cytoplasmic fraction.
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PMID:Purification and characterization of proteinase In, a trypsin-like proteinase, in Escherichia coli. 133 54

The effects of alimentary whey proteins given, as whole proteins (WP), controlled trypsin and chymotrypsin hydrolysate oligopeptides (WPH), or a free amino acid mixture (AAM), on growth, nitrogen retention, and steatorrhea were assessed in 24 Wistar rats (250 to 300 g) after 72 hr of starvation and 24 to 96 hr of realimentation and in 24 controls. The three diets had the same caloric, nitrogen, vitamin, and mineral contents. Rats had free access to the liquid diets. Only rats which ate the whole diet (90 cal) were included in the study. No differences in steatorrhea and fecal nitrogen were observed. The absorption rate was over 95% on the three diets. In contrast, weight gain was statistically better on WPH (+9% after 96 hr of realimentation) than on WP (+5%) or AAM (+2%). This was associated with a statistically higher nitrogen retention at all time periods studied, which was a result of a significant lower nitrogen urinary excretion. Similar results were obtained in controls. This better growth was a result of a better protein synthesis and lower ureagenesis.
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PMID:Effect of whey proteins, their oligopeptide hydrolysates and free amino acid mixtures on growth and nitrogen retention in fed and starved rats. 277 42

Treatment of the rat pancreatic acinar cell line AR4-2J with the calcium ionophore A23187 selectively increases, within a few hours, the steady-state level of trypsin mRNA. Addition of the tumor-promoting phorbol ester phorbol 12-myristate 13-acetate potentiates the calcium-induced increase. The mRNA level of the other tested exocrine pancreatic genes decreases. These results were confirmed by DNA transfection experiments, using the 5' flanking region of the trypsin and chymotrypsin genes linked to the coding sequence of the chloramphenicol acetyltransferase (CAT) gene. In calcium-induced cells transfected with the trypsin constructs, an increase in CAT activity was observed, whereas the chymotrypsin constructs revealed a decreased CAT activity. Glucose starvation of AR4-2J cells similarly elicited a selective increase in trypsin mRNA. This selective regulation of trypsin may reflect its role as the key activator of the other zymogen species.
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PMID:Selective regulation of trypsin gene expression by calcium and by glucose starvation in a rat exocrine pancreas cell line. 308 79

Development of the cellular slime mould Dictyostelium discoideum strain NC4, in the presence of alpha-chymotrypsin (3 mg/ml) is reversibly arrested at the tight aggregate stage (10/12 h). Pronase has a similar effect, but trypsin only retards normal development by about five hours. Normally developing cells are susceptible to alpha-chymotrypsin if they are transferred into its presence at any time up to the tight aggregate stage (10-12 h). Transfer after this stage does not affect the appearance of fruiting body structures in the normal time (24 h). Electron microscopy showed the ultrastructure of alpha-chymotrypsin-blocked aggregates after starvation for 24 h to be consistent with a block at 10-12 h of normal development. Poorly developed prespore vacuoles, having thin incomplete walls and a paucity of electron-dense material, are present in some cells. No angular vacuolated cells characteristic of stalk cells are visible. Fruiting bodies formed in the presence of a alpha-chymotrypsin, either as minority structures when the enzyme is added before 10-12 h of normal development, or as the majority structures on later enzyme addition, were found to be abnormal. Normal stalks were formed but the spores were immature. Prespore vacuoles were present, though disrupted, and the cells were not encapsulated by spore walls. The electronegativity of intact slime mould amoebae was significantly reduced, and material containing L-[6-3H]-fucose and [1-14C]leucine was removed from the cell surface on alpha-chymotrypsin treatment. Few plasma membrane proteins were affected, however, and staining of polyacrylamide gels for glycopeptides using Con A-peroxide binding also showed little change.
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PMID:The effect of chymotrypsin on the development of Dictyostelium discoideum. 743 Sep 29

In order to isolate glucose-starvation-related cDNAs in maize (Zea mays L.) root tips, a cDNA library was constructed with poly(A)+ mRNA from 24 h starved root tips. After differential screening of the library, we isolated six different cDNAs (named pZSS2 and pZSS7) which were expressed during glucose starvation. Time course analysis revealed that maximum expression of five of these genes occurs 30 h after the onset of the starvation treatment. On the contrary, the expression of mRNAs corresponding to pZSS4 was maximal at an early stage of starvation and then dramatically decreased. The expression of this gene did not seem to be specific for glucose starvation. The pattern of induction of the genes corresponding to pZSS2, pZSS3, pZSS5, pZSS6 and pZSS7 revealed that non-metabolizable sugars such as L-glucose and mannitol induce mRNA transcription similarly to glucose starvation. When D-glucose or any other metabolizable sugar was supplied, the level of transcripts was reduced. Nucleotide sequence analyses of the six cDNAs allowed identification of five of them by comparison with sequence data bases. The protein encoded by clone pZSS2 is analogous to a wound-induced protein from barley. Clones pZSS4 to pZSS7 encode, respectively, a transmembrane protein, a cysteine protease, a metallothionein-like protein and a chymotrypsin/subtilisin-like protease inhibitor. Clone pZSS3 shares no significant homology with any known sequence.
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PMID:Molecular cloning and characterization of six cDNAs expressed during glucose starvation in excised maize (Zea mays L.) root tips. 763 17

Both components of nitrogenase, dinitrogenase and dinitrogenase reductase, are rapidly inactivated by oxygen. To investigate the proteolytic degradation of dinitrogenase reductase irreversibly destroyed by high oxygen concentrations, we carried out in vitro experiments with heterocyst extracts from Anabaena variabilis ATCC 29413. The results indicate a direct dependence of degradation on the applied oxygen concentration. Although the degrees of degradation were similar for both the modified and unmodified subunits of dinitrogenase reductase, there was a significant difference with respect to the cleavage products observed. The pattern of effective protease inhibitors suggests the involvement of serine proteases with chymotrypsin- and trypsin-like specificity. A protective effect was obtained by saturation of the nucleotide binding sites of dinitrogenase reductase with either ATP or ADP. As shown by gel filtration experiments, the adenylates prevented the nitrogenase subunits from extensive noncovalent aggregation, which is usually considered evidence for a denaturing process. The in vitro degradation of dinitrogenase reductase is discussed in connection with previous reports on degradation of nitrogenase in cyanobacteria under oxygen stress and/or starvation.
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PMID:Proteolytic degradation of dinitrogenase reductase from Anabaena variabilis (ATCC 29413) as a consequence of ATP depletion and impact of oxygen. 855 Apr 89

We investigated the effect of starvation as a stimulant of the digestive system on digestive proteinase activities in the white shrimp Penaeus vannamei. The starved organisms were sampled periodically according to the molting stage and compared with a continuously fed group. Molting stage was included as an independent variable. Most analyzed variables, except for trypsin, were more affected by starvation than by molting, indicating that starvation is a stimulant that masks the effect of molting and showing that food or alimentary stress is more conspicuous than physiological ones. We found that starvation is a stimulant that surpasses the effect of molting, and because it affects the activity of digestive proteinases, studies of starving organisms in combination with tools of molecular biology, can be a helpful working model in the understanding of mechanisms of regulation of digestive enzyme activity. In the starved organisms, trypsin and chymotrypsin activities were similar, suggesting dependence of one to the other. Changes in proteolytic activities and the number of protein bands in electrophoresis showed evidence of synthesis regulation in the midgut gland of white shrimp.
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PMID:Influence of molting and starvation on the synthesis of proteolytic enzymes in the midgut gland of the white shrimp Penaeus vannamei. 1243 6

In this study, we synthesized a synthetic serine proteinase inhibitor II gene (sPI-II) that harbored the chymotrypsin and trypsin inhibitor domains of the PI-II gene from Nicotiana alata. In an effort to reduce protease activity in a rice cell suspension culture, we first synthesized sPI-II using overlap PCR and then introduced the gene into a rice calli (Oryza sativa L. cv. Dongin) by particle bombardment-mediated transformation. The sPI-II gene was under the control of a rice alpha-amylase 3D promoter induced by sugar starvation. To verify the integration and expression of the sPI-II gene in the transformed rice cells, we employed genomic DNA PCR amplification and Northern blot analysis, respectively. The relative protease activity of the transformed cell suspension culture was reduced to approximately 23% when compared to the non-transformed culture. This indicates that a transformed suspension culture system expressing a proteinase inhibitor, may be a useful tool to protect against recombinant protein losses resulting from extracellular proteases.
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PMID:Reduced protease activity in transformed rice cell suspension cultures expressing a proteinase inhibitor. 1731 52


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