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PubMed1979

Water-soluble lipoproteins from yolk granules in sea urchin eggs. II. Chemical composition.

The chemical composition of yolk lipoproteins (YLP-1, 2, and 3) was determined. YLP-1, 2, and 3 were quite similar as regards the chemical composition of lipids, proteins, and carbohydrate moieties. Each lipoprotein has an average dry weight composition of lipids (55--72%) and apo-lipoproteins (28--45%) containing protein, hexose, hexosamine, and sialic acid. In each lipoprotein, triacylglycerol is a major lipid component (70--83%), followed by phospholipid (8--16%), cholesterol (free and esterified, 8--10%), and free fatty acid (3--4%). Phosphatidylcholine and phosphatidylserine account for 68--74% and 16--24% of the phospholipids, respectively. The fatty acid compositions of total lipids from each lipoprotein are quite similar, with a high degree of unsaturation (63--65%). The carbohydrate content of apolipoprotiens from each lipoprotein is remarkably high (27--31% of apo-lipoproteins) and their composition is very simple: mannose and glucosamine are major constituents in the polysaccharide moiety of each lipoprotein and sialic acid is all in the N-glycolyl form. The amino acid compositions of apo-lipoproteins are quite similar in YLP-1, 2, and 3, with high contents of aspartic acid, glutamic acid, threonine, serine, and leucine. Furthermore, a small amount of glycolipids is present in the yolk lipoproteins. They were separated into six components on TLC. All of them are resorcinol-positive, indicating the presence of sialoglycolipids.

Amino Acids↗
PubMed1979

Purification and immunochemical properties of human low molecular weight kininogen.

A low molecular weight (LMW) kininogen was isolated from pooled human serum by chromatography on DEAE-Sephadex A-50, CM-Sephadex C-50, Sephadex G-150, and Sephadex G-100. It was shown to be homogeneous by ultracentrifugation, polyacrylamide gel electrophoresis, and immunoelectrophoresis. The sedimentation coefficient, S020,W, of purified LMW kininogen was 3.85 s, and its molecular weight was determined to be 78,000 by Sephadex G-100 gel-filtration. The LMW kininogen contained 79.3% protein, 8.0% hexose, 3.9% hexosamine, and 4.9% sialic acid. In order to determine the immunochemical properties of LMW kininogen, specific antiserum was prepared in rabbits. The antigenic determinant of LMW kininogen was not related to the sialic acid and kinin moieties in the kininogen molecule, but could not be distinguished from that of high molecular weight (HMW) kininogen. In the quantitative single radial immunodiffusion test, a sialic acid-free LMW kininogen reacted to a greater extent with the antiserum than the native LMW kininogen. The kininogen level in human serum was estimated by single radial immunodiffusion. The antiserum cross-reacted with monkey serum, but not with sera from dogs, rats, and mice, horses, pigs, guinea pigs, oxen, and rabbits.

Chromatography, Affinity↗
PubMed1980

Blood group type glycosphingolipids of human cord blood erythrocytes.

The non-acid glycosphingolipids of cord blood erythrocytes, pooled from blood groups O and A respectively, were characterized by mass spectrometry in combination with immunologic and thin-layer chromatographic analyses. The glycosphingolipid pattern was compared to that of adult erythrocytes. Just as for adult blood, the major glycosphingolipid species were lactosylceramide and globotetraosylceramide (globoside). The triglycosylceramide fraction was quantitatively smaller in cord red blood cells and was also enriched in a triglycosylceramide with a terminal hexosamine, as conclusively shown by mass spectrometry. The amount of blood group A and H active glycosphingolipids appeared to be less in cord blood cells compared to adult cells was glycolipids with longer, probably branched chain structures were not detected. In contrast, increased amounts of penta- and hexaglycosylceramides lacking fucose and possibly being biosynthetic precursor substances to the ordinary blood group A and H glycosphingolipids were found typical for cord blood cells.

ABO Blood-Group System↗
PubMed1980

Isolation and characterization of proteodermatansulfate from rat skin.

A proteodermatansulfate was extracted from rat skin with 4 M guanidine hydrochloride containing protease inhibitors at 4 degrees C. It was separated from collagen on DEAE-cellulose in 7 M urea and was purified by cesium chloride density gradient centrifugation under associative conditions, DEAE-Sephadex column chromatography and then Sephadex G-200 gel filtration. On SDS-disc electrophoresis, the proteoglycan gave a single band staining for protein and a band of the same mobility staining with periodate-Schiff reagent. The proteoglycan contained 46% protein, and this was bound to dermatansulfate via an O-glycosidic linkage. The proteoglycan also contained 20% uronic acid and 16% hexosamine, but no detectable hydroxyproline. The ratio of galactosamine to glucosamine was 68. The dermatansulfate, the only glycosaminoglycan, had a hybrid structure containing iduronic acid and glucuronic acid as uronic acids. The content of glucuronic acid in uronic acid was much higher than that of pig skin dermatansulfate. The dermatansulfate had a slightly higher mobility on cellulose acetate electrophoresis than those from other sources. Gel chromatography on Sepharose CL-6B showed that the molecular weight of the dermatansulfate was 23,000, while that of the proteoglycan was 36,000. The elution profile of a mixture of the proteoglycan and hyaluronic acid on Sepharose 6B column chromatography was similar to that of the proteoglycan alone.

Animals↗
PubMed1981

Isolation and properties of human kappa-casein.

Human kappa-casein was isolated from human whole casein by gel filtration with Sephadex G-200 and hydroxylapatite chromatography in the presence of sodium dodecyl sulfate (SDS). The kappa-casein was calcium-insensitive and did stabilize human beta-casein and bovine alpha s1-casein against precipitation by calcium ions. Formation of micelles from human beta- and kappa-caseins, and calcium ions was confirmed by electron microscopic observation. On SDS-polyacrylamide gel electrophoresis (SDS-PAGE), a single band was obtained. The formation of para-kappa-caseins by chymosin was confirmed by SDS-PAGE. Two para-kappa-caseins with apparent molecular weights of 13,000 and 11,000 appeared. The molecular weight of intact human kappa-casein was estimated to be approximately 33,000. The human kappa-casein contained about 40% carbohydrate (15% galactose, 3% fucose, 15% hexosamines, and 5% sialic acid) and 0.10% (1 mol/mol) phosphorus. Its amino acid composition was similar to that of bovine kappa-casein except for serine, glutamic acid, and lysine contents.

Amino Acids↗
PubMed1983

Porcine liver succinyltrialanine p-nitroanilide hydrolytic enzyme. Its purification and characterization as a post-proline cleaving enzyme.

Succinyltrialanine p-nitroanilide(STANA)-hydrolytic enzyme was purified 5,200-fold from porcine liver soluble fraction with a yield of 75% by ammonium sulfate fractionation and chromatographies on DEAE-Sephacel, Sephadex G-150, and hydroxylapatite columns. The purified enzyme was homogeneous as judged by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate (SDS). The pI of the enzyme was 4.9 by dis gel electrofocusing and the molecular weight was calculated to be 72,000 by gel filtration on a Sephadex G-150 column and 74,000 by SDS-polyacrylamide gel electrophoresis. Acidic amino acids amounted to 17.2% of the total amino acid residues, and the basic ones, 12.9%. No hexosamine was detected. The STANA-hydrolytic enzyme showed maximal activity at pH 7.4 against succinyltrialanine p-nitroanilide and at pH 6.5 against succinyl-Gly-Pro-4-methylcoumaryl 7-amide (MCA), and was stable between pH 6 and 7 in the presence of dithiothreitol. This enzyme hydrolyzed succinyl-Gly-Pro-Leu-Gly-Pro-MCA, succinyl-Gly-Pro-MCA, succinyl-Ala-Pro-Ala-MCA, and several proline-containing natural peptides in addition to succinyltrialanine p-nitroanilide, but was unable to hydrolyze the substrates of aminopeptidases, dipeptidylaminopeptidase IV, trypsin, and chymotrypsin. Elastatinal and chymostatin were effective inhibitors and their IC50 values were 8.7 micrograms/ml and 18.2 micrograms/ml, respectively. The enzyme was completely inhibited by 10(-7) M p-chloromercuribenzoic acid (pCMB), 10(-7) M p-chloromercuriphenylsulfonic acid (pCMPS), and 10(-4) M diisopropyl phosphofluoridate (DFP), but not by 1 mM E-64, which is known as an inhibitor specific to thiol proteinase. The enzyme was easily inactivated by agitation in a Vortex mixer, and its activity was recovered by the addition of thiol compounds such as dithiothreitol, 2-mercaptoethanol and cysteine. The effects of inhibitors and thiol compounds were substantially identical when the enzyme activity was measured with either succinyltrialanine p-nitroanilide or succinyl-Gly-Pro-MCA as a substrate. These results indicate that the STANA-hydrolytic enzyme in the liver soluble fraction is a post-proline cleaving enzyme [EC 3.4.21.26].

Amino Acids↗
PubMed1984

Enzymatic determination of free glucuronic acid with glucuronolactone reductase. I. Isolation and purification of glucuronolactone reductase from rat kidney.

Glucuronolactone reductase [EC 1.1.1.20] from rat kidney was purified over 300-fold by ammonium sulfate fractionation, chromatography on DEAE-cellulose and hydroxylapatite columns, and preparative isoelectric focusing. The substrate specificity of the enzyme in the reduction reaction was broad, and hexuronic acid was one of the best substrates among monosaccharides. Km values for D-glucuronic acid, D-glucuronolactone, D-galacturonic acid, and L-iduronic acid were 6, 9, 4, and 6 mM, respectively. An investigation of the activity for aldose led to the finding that triose and tetrose served as good substrates for this enzyme. However, the activity for aldopentose or aldohexose was less than 1% of that for D-glucuronic acid at the same concentration. The enzyme was inactive towards most hexosamines (galactosamine, mannosamine, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylmannosamine, but not glucosamine), meso-inositol, D-fructose, and tetrasaccharides from hyaluronic acid and chondroitin 4-sulfate. Trisaccharides from hyaluronic acid and chondroitin 6-sulfate which possess glucuronic acid at the reducing end were poor substrates for the enzyme and the activity towards these 4-substituted glucuronic acids was less than 3% of that towards non-substituted glucuronic acid.

Animals↗
PubMed1984

Purification and characterization of rat low molecular weight kininogen.

Low molecular weight (LMW) kininogen was isolated from pooled rat plasma by chromatography on DEAE-Sephadex A-50, CM-Sephadex C-50, Blue-Sepharose CL-6B, and Sephadex G-100. It was shown to be homogeneous by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoelectrophoresis. The molecular weight of rat LMW kininogen was determined to be 72,000 by SDS-PAGE. The LMW kininogen contained 83.5% protein, 4.0% hexose, 5.5% hexosamine, and 2.7% sialic acid. Kinin liberated from LMW kininogen by trypsin treatment was identified as an Ile-Ser-bradykinin(T-kinin) by analysis involving ion exchange column chromatography on CM-Sephadex C-25 and high performance liquid chromatography on a reverse-phase column (ODS-120T). LMW kininogen formed kinin with rat submaxillary gland kallikrein, but the kinin liberated was only 14% of the total kinin content, that is, that released by trypsin. In order to determine the immunochemical properties of LMW kininogen, specific antiserum was prepared in rabbits. The antiserum cross-reacted with high molecular weight (HMW) kininogen, but spur formation was observed between the LMW and HMW kininogens. The kininogen level in rat plasma was estimated to be 433 microgram/ml by a quantitative single radial immunodiffusion test.

Animals↗
PubMed1984

Studies on perivitelline fluid of horseshoe crab embryo. II. Purification of agglutinin-binding substance from the perivitelline fluid of Tachypleus gigas embryo.

Three glycoproteins with potent agglutinin-binding activity have been isolated from the perivitelline fluid of Tachypleus gigas, horseshoe crab, embryo. In the native form, these agglutinin-binding substances were highly aggregated. After being dissociated in 10 M urea, these proteins were fractionated by gel-filtration on a Fractogel TSK (Toyopearl) HW-60 in Tris-NaCl-CaCl2 (0.05 M Tris-HCl, pH 7.5, containing 0.5 M NaCl and 0.1 M CaCl2) containing 10 M urea. The proteins thus obtained were designated as ABS-I, -II, and -III in the order of elution and have apparent molecular weights of 25,000 (ABS-II) and 10,000 (ABS-III) as judged by both gel-filtration on Fractogel TSK (Toyopearl) HW-60 in 10 M urea and sodium dodecyl sulfate-gel electrophoresis; the molecular weight of ABS-I could not be estimated in the two systems since it was too high. ABS-I, -II, and -III, of which only ABS-I is water-soluble, inhibit one hemagglutination unit of activity with minimum quantities of 0.5 micrograms/ml, 7.8 micrograms/ml, and 1.0 micrograms/ml, respectively. They were found to be glycoproteins in which 6.6% of the dry weight (ABS-I), 4.2% of the dry weight (ABS-II), and 7.5% of the dry weight (ABS-III) were carbohydrate. The dry weight ratio of hexosamines in these substances is 3:1:2 (ABS-I: ABS-II: ABS-III), and that of sialic acid is also 3:1:2. Amino acid analyses of these proteins indicated that they have high contents of aspartic acid, glutamic acid, and glycine in common.

Amino Acids↗
PubMed1985

A common linkage saccharide unit between teichoic acids and peptidoglycan in cell walls of Bacillus coagulans.

Teichoic acid-glycopeptide complexes were isolated from lysozyme digests of the cell walls of Bacillus coagulans AHU 1631, AHU 1634, and AHU 1638, and the structure of the teichoic acid moieties and their linkage regions was studied. On treatment with hydrogen fluoride, each of the complexes gave a hexosamine-containing disaccharide, which was identified to be glucosyl(beta 1----4)N-acetylglucosamine, in addition to dephosphorylated repeating units of the teichoic acids, namely, galactosyl(alpha 1----2)glycerol and either galactosyl(alpha 1----2)[glucosyl(alpha 1----1/3)]glycerol (AHU 1638) or galactosyl(alpha 1----2)[glucosyl(beta 1----1/3)]glycerol (AHU 1631 and AHU 1634). From the results of Smith degradation, methylation analysis, and partial acid hydrolysis, the teichoic acids from these strains seem to have the same backbone chains composed of galactosyl(alpha 1----2)glycerol phosphate units joined by phosphodiester bonds at C-6 of the galactose residues. The presence of the disaccharide, glucosyl(beta 1----4)N-acetylglucosamine, in the linkage regions between teichoic acids and peptidoglycan was confirmed by the isolation of a disaccharide-linked glycopeptide fragment from each complex after treatment with mild alkali and of a teichoic acid-linked saccharide from each cell wall preparation after treatment with mild acid. Thus, it is concluded that despite structural differences in the glycosidic branches, the teichoic acids in the cell walls of the three strains are linked to peptidoglycan through a common linkage saccharide, glucosyl (beta 1----4) N-acetylglucosamine.

Bacillus↗
PubMed1996

How does hyperglycaemia predispose to diabetic nephropathy?

Diabetic nephropathy is preceded by 'hyperfiltration' mediated by dilatation of the afferent arterioles to the glomeruli by means of IGF-1, prostaglandins, bradykinin, nitric oxide and atrial natriuretic peptide, together with constriction of the efferent arterioles by local thromboxane A2. Raised glomerular intracapillary pressures might then contribute to glomerulosclerosis, but in any case there is permeability of the vascular endothelium. AGEPs and lipid peroxides can explain this. AGEPs, or simply intermittently high levels of glucose, also account for synthesis of extracellular matrix proteins that lead to thickening of the basement membrane and glomerulosclerosis. Another glucose product, glucosamine-6-phosphate, is formed when there is hexosamine flux along with insulin resistance in tissues, and is implicated in glomerulosclerosis, since it also stimulates TGF-beta transcription. In seeking to explain proteinuria, depletion of heparan sulphates from the endothelial cells and GBM is now established as a principal cause. In addition to a high glucose reducing the synthesis of heparan sulphates, it has now been shown that high glucose may depress the synthesis of heparin sulphate proteoglycan.

Diabetic Nephropathies↗
PubMed1983

Secretion of mucin by explants of rabbit and human cervix in organ culture.

Small explants (2-3 mm3) of endocervix from virgin, estrous rabbits, and from hospitalized patients undergoing hysterectomy for nonneoplastic disease, were placed in organ culture and maintained in serum-free media for 4 days at 35 degrees C in a humid environment of 95% air/5% CO2. Waymouth's MB 752/1 with 10-5 M hydrocortisone succinate, 10-7 M retinyl acetate, and 1 microgram/ml insulin proved to be an excellent medium for maintaining these tissues, as judged by examination with light and scanning electron microscopy after incubation for 5 days. The explants incorporated the radiolabeled glycoprotein precursor, tritiated glucosamine, and secreted labeled mucin glycoproteins in vitro. Mucin released into the culture medium contained sialic acid and hexosamine in a molar ratio of approximately 0.5-0.8:1.0. Although some alterations occur in the morphology of secretory cells and their products after maintenance in culture for several days, the system can be utilized for studying various aspects of the cell biology of cervical mucin secretion.

Animals↗
PubMed1986

Isolation and characterization of three forms of luteinizing hormone from the pituitary gland of the horse.

Three isoforms of equine luteinizing hormone (eLH-A, eLH-B and eLH-C) have been isolated from horse pituitary glands. Separation was achieved on the basis of charge heterogeneity by ion-exchange chromatography. These charge differences were apparent after final purification, as determined by electrophoretic mobility on polyacrylamide disc gels (RF = 0.14, 0.19 and 0.26 for eLH-A, -B and -C, respectively). Apparent size differences were also noted between the isohormones by gel filtration on Sephadex G-100. Ve/Vo ratios for eLH-A, -B and -C were 1.72, 1.54 and 1.47, respectively. All 3 isoforms were found to contain an equivalent amount of hexose (9.0-9.2%). Isohormones eLH-B and eLH-C, however, possess more sialic acid than eLH-A (6.6-6.7%, vs. 4.5%). The eLH-A and eLH-B preparations contain a similar amount of hexosamine, which is slightly lower than the amount of eLH-C (8.8-9.1% vs. 11.2%). No differences were noted between the isohormones by rat Leydig cell LH bioassay, equine testis LH radioreceptor assay (RRA) or calf testis follicle-stimulating hormone (FSH) RRA. Slight, but nonsignificant, variations were noted between preparations in an eLH radioimmunoassay (RIA). Although chemical variations were detected between the eLH isoforms, no significant differences were observed in in vitro biological and immunological activities. The differences detected in sialic acid content raises the possibility that differences in in vivo clearance rates may exist.

Animals↗
PubMed1989

Structural requirements of heparin disaccharides responsible for hemorrhage: reversion of the antihemostatic effect by ATP.

Topically applied heparin and heparan sulfate disaccharides, with the basic structure delta-4,5 uronyl-(1----4)-glucosamine and bearing a sulfate at the C-6 position of the glucosamine residue, are antihemostatics as potent as heparin, producing uncontrollable hemorrhage from small blood vessels. The finding that other sulfated disaccharides with the same sulfate:hexosamine:uronic acid ratios but with the sulfate at a different position (C-2), or with different glycosidic linkage (1----3), were inactive as inhibitors of hemostasis indicates that a specific structure is needed to produce the effect. The inhibitory activity of the normal hemostatic process could be reversed by ATP. Molecular models show that part of the disaccharide inhibitors and ATP hold a similar structural conformation.

Adenosine Triphosphate↗
PubMed2004

Increased O-glycosylation of insulin signaling proteins results in their impaired activation and enhanced susceptibility to apoptosis in pancreatic beta-cells.

Because adverse effects of glucose were attributed to its increased routing through the hexosamine pathway (HBP), we inquired whether HBP activation affects pancreatic beta-cell survival. Exposure of human islets to high glucose resulted in increased apoptosis of beta-cells upon serum deprivation that was reversed by azaserine. Also, glucosamine, a direct precursor of the downstream product of the HBP, increased human beta-cells apoptosis upon serum deprivation, which was reversed by benzyl-2-acetamido-2-deoxy-alpha-d-galactopyranoside (BADGP), an inhibitor of protein O-glycosylation. These results were reproduced in RIN rat beta-cells. Glucosamine treatment resulted in inhibition of tyrosine-phosphorylation of the insulin receptor (IR), IRS-1, and IRS-2, which was associated with increased O-glycosylation. These changes caused impaired activation of the PI 3-kinase/Akt survival signaling that resulted in reduced GSK-3 and FOXO1a inactivation. BADGP reversed the glucosamine-induced reduction in insulin-stimulated phosphorylation of IR, IRS-1, IRS-2, Akt, GSK-3, and FOXO1a. Impaired FOXO1a inactivation sustained expression of the pro-apoptotic protein Bim, without affecting Bad, Bcl-XL, or Bcl-2 expression. These results indicate that hyperglycemia may increase susceptibility to apoptosis of human and rat beta-cell through activation of the HBP. Increased routing of glucose through this metabolic pathway results in impaired activation of the IR/IRSs/PI3-kinase/Akt survival pathway by induction of O-glycosylation of signaling molecules.

Apoptosis↗
PubMed1995

Effects of lansoprazole on gastric ulcer healing and mucin content.

The effect of lansoprazole, a new benzimidazole proton pump inhibitor, on the relationship between ulcer healing and changes in mucin content was studied in gastric ulcer patients. Twenty-one outpatients with active gastric ulcers received lansoprazole 30 mg once daily given in the morning for 8 weeks. The gastric mucin content was examined by HPLC analysis of hexosamines in gastric biopsy specimens obtained from the lesser curvature of the pylorus and the greater curvature of the upper body. The ulcer healing rate for lansoprazole was 85.7% at 8 weeks. The mucin content of both mucosal regions significantly decreased to approximately 70% (pylorus 70.9%; upper body 74.7%) of the value before drug treatment. The results of this study demonstrate that 30 mg lansoprazole once daily is remarkably effective in healing gastric ulcers because of its potent acid suppression. It appears that acid inhibition is the primary factor in initial treatment. However, maintaining an altered gastric mucosal defense mechanism may have implications for the long-term treatment of gastric ulcers.

2-Pyridinylmethylsulfinylbenzimidazoles↗
PubMedDate not supplied

Biological changes in the annulus fibrosus in patients with low-back pain.

The anterior annulus from patients undergoing surgery for low-back pain was compared with the same region removed at autopsy. Collagen, proteoglycan, and water content were measured in different regions across the annulus. Water and proteoglycan contents increased from the outer to the inner annulus, whereas the collagen contents declined. Quantitative differences were found between agematched surgical and autopsy specimens. Discs from most patients showed lowered proteoglycan contents, and a few of these showed high water contents. Loss of collagen in isolated areas of the annulus was demonstrated in some patients. Collagen loss occurred most frequently in the lumbosacral disc, whereas changes in proteoglycan and water were more frequent higher in the lumbar region. No qualitative changes in collagen types were detected immunochemically. In many patients, the levels of proteoglycan which aggregated in vitro were extremely low. Changes in hexosamine molar ratio of disc proteoglycan and in the length of the chondroitin sulfate side chains were observed with aging in this group of patients.

Acetylglucosaminidase↗
PubMed2006

Glucosamine administration during resuscitation improves organ function after trauma hemorrhage.

Stress-induced hyperglycemia is necessary for maximal rates of survival after severe hemorrhage; however, the responsible mechanisms are not clear. One consequence of hyperglycemia is an increase in hexosamine biosynthesis, which leads to increases in levels of O-linked attachment of N-acetyl-glucosamine (O-GlcNAc) on nuclear and cytoplasmic proteins. This modification has been shown to lead to improved survival of isolated cells after stress. In view of this, we hypothesized that glucosamine (GlcNH2), which more selectively increases the levels of O-GlcNAc administration after shock, will have salutary effects on organ function after trauma hemorrhage (TH). Fasted male rats that underwent midline laparotomy were bled to a mean arterial blood pressure of 40 mmHg for 90 min and then resuscitated with Ringer lactate (four times the shed blood volume). Administration of 2.5 mL of 150 mmol L GlcNH2 midway during resuscitation improved cardiac output 2-fold compared with controls that received 2.5 mL of 150 mmol L NaCl. GlcNH2 also improved perfusion of various organs systems, including kidney and brain, and attenuated the TH-induced increase in serum levels of IL-6 (902+/-224 vs. 585+/-103 pg mL) and TNF-alpha (540+/-81 vs. 345+/-110 pg mL) (values are mean+/-SD). GlcNH2 administration resulted in significant increase in protein-associated O-GlcNAc in the heart and brain after TH. Thus, GlcNH2 administered during resuscitation improves recovery from TH, as assessed by cardiac function, organ perfusion, and levels of circulating inflammatory cytokines. This protection correlates with enhanced levels of nucleocytoplasmic protein O-GlcNAcylation and suggests that increased O-GlcNAc could be the mechanism that links stress-induced hyperglycemia to improved outcomes.

Animals↗