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Artículos de revistas sobre el tema "Glycosaminoglycans Metabolism"

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Publicado: 4 de junio de 2021
Última modificación: 30 de enero de 2023

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1

Viola, Manuela, Timothy E. L. Douglas, Laura Alaniz, and Barbara Bartolini. "Glycosaminoglycans Metabolism." Biochemistry Research International 2012 (2012): 1–2. http://dx.doi.org/10.1155/2012/245792.

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2

Mironov, S. P., A. M. Gerasimov, L. N. Furtseva, A. G. Tikhomirov, D. O. Vasiliev, and R. V. Merkurieva. "Oxyprolinuria and Glycosaminoglycansuria in Achilles Tendon Ruptures." N.N. Priorov Journal of Traumatology and Orthopedics 5, no. 2 (June 15, 1998): 51–53. http://dx.doi.org/10.17816/vto104492.

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In 17 athlets and ballet dancers with Achilles tendon ruptures oxyprolinuria and urine content of hexuronic acid were studied. Considerable increase of collagen and glycosaminoglycans decay products was detected. The results of differential spectrophotometry showed that urine glycosaminoglycanes presented by proteoglycans. It was assumed that Achilles tendon ruptures could be caused by excessive mechanical load and/or lack of the connective tissue metabolism. The authors consider that further study of oxyprolinuria as well as enzyme-substrate systems of glycosaminoglycans are perspective for the detection of trauma risk group.
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3

Koźma, Ewa M., Kornelia Kuźnik-Trocha, Katarzyna Winsz-Szczotka, Grzegorz Wisowski, Paweł Olczyk, Katarzyna Komosińska-Vassev, Mariusz Kasperczyk, and Krystyna Olczyk. "Significant Remodeling Affects the Circulating Glycosaminoglycan Profile in Adult Patients with both Severe and Mild Forms of Acute Pancreatitis." Journal of Clinical Medicine 9, no. 5 (May 1, 2020): 1308. http://dx.doi.org/10.3390/jcm9051308.

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Acute pancreatitis (AP) manifests itself either as a mild, self-limiting inflammation or a severe, systemic inflammatory process that is associated with various complications and a high mortality rate. It is unknown whether these two forms of the disease can differ in the profile of circulating glycosaminoglycans, which are molecules with huge biological reactivity due to a high density of negative electric charge. Plasma glycosaminoglycans were characterized/quantified in 23 healthy controls, 32 patients with mild AP, and 15 individuals with severe disease using electrophoresis with enzymatic identification (chondroitin sulfate and heparan sulfate) or an ELISA-based test (hyaluronan). Moreover, the correlations between the glycosaminoglycan levels and clinical parameters were evaluated. Both forms of AP showed similar remodeling of the plasma profile of the sulfated glycosaminoglycans. In contrast, only in the patients with mild AP was the level of circulating hyaluronan significantly decreased as compared to the healthy controls. Both forms of AP are associated with systemic changes in the metabolism of glycosaminoglycans. However, the alterations in hyaluronan metabolism may contribute to the disease evolution. The circulating hyaluronan may have some clinical value to predict the severity of AP and to evaluate the clinical status of patients with severe AP.
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4

Wolf, Hanna, Andrea Graßmann, Romina Bester, André Hossinger, Christoph Möhl, Lydia Paulsen, Martin H. Groschup, Hermann Schätzl, and Ina Vorberg. "Modulation of Glycosaminoglycans Affects PrPScMetabolism but Does Not Block PrPScUptake." Journal of Virology 89, no. 19 (July 22, 2015): 9853–64. http://dx.doi.org/10.1128/jvi.01276-15.

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ABSTRACTMammalian prions are unconventional infectious agents composed primarily of the misfolded aggregated host prion protein PrP, termed PrPSc. Prions propagate by the recruitment and conformational conversion of cellular prion protein into abnormal prion aggregates on the cell surface or along the endocytic pathway. Cellular glycosaminoglycans have been implicated as the first attachment sites for prions and cofactors for cellular prion replication. Glycosaminoglycan mimetics and obstruction of glycosaminoglycan sulfation affect prion replication, but the inhibitory effects on different strains and different stages of the cell infection have not been thoroughly addressed. We examined the effects of a glycosaminoglycan mimetic and undersulfation on cellular prion protein metabolism, prion uptake, and the establishment of productive infections in L929 cells by two mouse-adapted prion strains. Surprisingly, both treatments reduced endogenous sulfated glycosaminoglycans but had divergent effects on cellular PrP levels. Chemical or genetic manipulation of glycosaminoglycans did not prevent PrPScuptake, arguing against their roles as essential prion attachment sites. However, both treatments effectively antagonizedde novoprion infection independently of the prion strain and reduced PrPScformation in chronically infected cells. Our results demonstrate that sulfated glycosaminoglycans are dispensable for prion internalization but play a pivotal role in persistently maintained PrPScformation independent of the prion strain.IMPORTANCERecently, glycosaminoglycans (GAGs) became the focus of neurodegenerative disease research as general attachment sites for cell invasion by pathogenic protein aggregates. GAGs influence amyloid formationin vitro. GAGs are also found in intra- and extracellular amyloid deposits. In light of the essential role GAGs play in proteinopathies, understanding the effects of GAGs on protein aggregation and aggregate dissemination is crucial for therapeutic intervention. Here, we show that GAGs are dispensable for prion uptake but play essential roles in downstream infection processes. GAG mimetics also affect cellular GAG levels and localization and thus might affect prion propagation by depleting intracellular cofactor pools.
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5

Kittlick, P. D. "Inflammation, glycolytic metabolism, and glycosaminoglycans." Experimental pathology 30, no. 1 (January 1986): 1–19. http://dx.doi.org/10.1016/s0232-1513(86)80051-2.

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6

Bower, L., C. Warren, and G. Manley. "Human Serum and Urine Glycosaminoglycans in Health and in Patients with Chronic Renal Failure." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 29, no. 2 (March 1992): 190–95. http://dx.doi.org/10.1177/000456329202900212.

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Quantitation of uronic acid precipitable by cetylpyridinium chloride (CPC) and electrophoretic separation of glycosaminoglycans were performed on sera from patients with chronic renal failure and compared to normal controls. Serum CPC-precipitable uronic acid (CpUA) levels in patients with renal failure were significantly higher (mean 13·7 mg/L, range 7·1–23·6 mg/L) than normal controls (mean 9·6 mg/L, range 5·1–13·9 mg/L) due to increased concentrations of low sulphated chondroitin sulphate. A positive correlation between serum CpUA and creatinine was found in renal failure patients. Urine CpUA excretion was raised in renal failure patients compared to normal controls with an increased excretion of chondroitin sulphate (Ch-S) of reduced electrophoretic mobility. Heparan sulphate (HS), a major glycosaminoglycan in normal urine, was absent from the urine of these patients. The possible origin of urine glycosaminoglycans and the role of the kidney in glycosaminoglycan metabolism are discussed.
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7

Kahaly, G., C. Stover, J. Beyer, and E. Otto. "In vitro synthesis of glycosaminoglycans in endocrine ophthalmopathy." Acta Endocrinologica 127, no. 5 (November 1992): 397–402. http://dx.doi.org/10.1530/acta.0.1270397.

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The effects of humoral and cell-mediated immunity on the glycosaminoglycan synthesis of retrobulbar fibroblasts was evaluated in patients with endocrine ophthalmopathy. After incubation with IgG and sera, secreted glycosaminoglycans, radiolabeled with D-6-3H-glucosamine and 35sulfate, were precipitated with cetylpyridinium chloride and ethanol. Hyaluronic acid synthesis of human retrobulbar fibroblasts after incubation with sera and IgG and after co-culture with lymphocytes was assessed by means of a radiometric test. Patients' IgG, compared to controls', accounted for a higher secretory stimulation of porcine retrobulbar fibroblasts (as measured by cetylpyridinium chloride precipitation) after 24 and 48 h. Contrasting with 24 h incubation time, glycosaminoglycan values after 48 h were increased two to threefold. Patients' and controls' sera caused earlier and stronger, yet indistinguishable glycosaminoglycan production. Non-sulfated hyaluronic acid was the preponderant glycosaminoglycan secreted into the media by retrobulbar fibroblasts. As assessed with the radiometric test, incubation with patients' and controls' sera and IgG did not reveal a significant difference in stimulating the hyaluronic synthesis of patients' and controls' retrobulbar fibroblasts. When measuring the hyaluronic acid synthesis of controls' and patients' retrobulbar fibroblasts after co-cultivation of lymphocytes, however, patients' lymphocytes had a marked ability to increase the hyaluronic acid concentration compared to controls' lymphocytes. The hyaluronic acid concentration after incubation of a patient's retrobulbar fibroblasts with autologous lymphocytes was markedly more elevated than the intrinsic hyaluronic acid production of retrobulbar fibroblasts. In conclusion, though a significant in vitro influence of patients' IgG and sera on the glycosaminoglycan release of both porcine and human (patients' as well as controls') retrobulbar fibroblasts could not be observed in this study, the indications of a marked stimulatory influence of lymphocytes on the hyaluronic acid secretion of retrobulbar fibroblasts demand further investigation.
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8

Chang, Chih-Cheng, Tien-Chun Chang, Shine CS Kao, Yea-Fhey Kuo, and Li-Fei Chien. "Pentoxifylline inhibits the proliferation and glycosaminoglycan synthesis of cultured fibroblasts derived from patients with Graves' ophthalmopathy and pretibial myxoedema." Acta Endocrinologica 129, no. 4 (October 1993): 322–27. http://dx.doi.org/10.1530/acta.0.1290322.

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Excessive amounts of glycosaminoglycans accumulate in the extraocular muscles of patients with Graves' ophthalmopathy and in the affected skin of patients with pretibial myxoedema. It is widely accepted that fibroblasts are the sources of glycosaminoglycan synthesis. Pentoxifylline, an analogue of the methylxanthine theobromine, inhibits the proliferation and certain biosynthetic activities of fibroblasts derived from normal human skin and from skin of patients with some fibrotic disorders. Our objective was to determine whether pentoxifylline has similar effects on fibroblasts derived from patients with Graves' ophthalmopathy and pretibial myxoedema and could serve as a candidate for the treatment of these manifestations. Fibroblasts from the extraocular muscles of two patients with Graves' ophthalmopathy and normal extraocular muscles of two subjects with strabismus, as well as the affected skin of two patients with pretibial myxoedema were cultured in vitro in the presence and absence of pentoxifylline to assay its effect on the proliferation of fibroblasts and their production of glycosaminoglycans. In subconfluent fibroblast cultures, pentoxifylline treatment caused a dose-dependent inhibition of serum-driven fibroblast proliferation. In confluent fibroblast cultures both in the presence and absence of serum, exposure to pentoxifylline similarly resulted in a dose-dependent inhibition of glycosaminoglycan synthesis for all these different kinds of fibroblasts. These findings may form the rationale for a clinical trial using pentoxifylline for the treatment of Graves' ophthalmopathy and pretibial myxoedema.
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9

Bondar', I. A., and V. V. Klimontov. "Glycosaminoglycans and diabetic nephropathy." Problems of Endocrinology 50, no. 2 (April 15, 2004): 29–34. http://dx.doi.org/10.14341/probl11392.

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Diabetic nephropathy (DN) is one of the leading places in the structure of mortality of patients with diabetes mellitus (DM) in Russia and abroad. Despite intensive study, the causes and development mechanisms of this complication are not finally clear. Most often, diabetic kidney damage is seen as the result of a complex interaction of metabolic, hemodynamic, genetic and other mechanisms. At the same time, the majority of researchers give the leading role to hyperglycemia and the metabolic disorders triggered by it. The latter include intensification of non-enzymatic glycation processes, activation of protein kinase C and polyol shunt, oxidative and carbonyl stress, hyperlipidemia, an imbalance of transcription factors and cytokines, and collagen metabolic disturbances. The role of these factors in the formation of DN has been reflected in a number of recent reviews.
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10

KAHALY, G., M. SCHULER, A. C. SEWELL, G. BERNHARD, J. BEYER, and U. KRAUSE. "URINARY GLYCOSAMINOGLYCANS IN Graves'OPHTHALMOPATHY." Clinical Endocrinology 33, no. 1 (July 1990): 35–44. http://dx.doi.org/10.1111/j.1365-2265.1990.tb00463.x.

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11

Unnikrishnan, V. S., and P. R. Sudhakaran. "Metabolism of glycosaminoglycans in CCl4-induced liver regeneration." Journal of Biosciences 14, no. 2 (June 1989): 163–72. http://dx.doi.org/10.1007/bf02703168.

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12

Kurup, Ravi Kumar, and Parameswara Achutha Kurup. "Hypothalamic digoxin-mediated model for epileptogenesis." Acta Neuropsychiatrica 15, no. 3 (June 2003): 115–21. http://dx.doi.org/10.1034/j.1601-5215.2003.00020.x.

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Background/aims:This study assessed the changes in the isoprenoid pathway and its metabolites in seizure disorder (ILAE classification – I generalized – idiopathic generalized epilepsy with age-related onset – epilepsy with generalized tonic clonic seizures on awakening) and the metabolic cascade produced by isoprenoid pathway dysregulation.Methods:The following parameters were assessed in seizure disorder: isoprenoid pathway metabolites, tyrosine and tryptophan catabolites, glycoconjugates metabolism and red blood cell (RBC) membrane composition.Results:There was elevation in plasma HMG-CoA reductase activity, serum digoxin and dolichol and a reduction in RBC membrane Na-K+ATPase activity, serum magnesium and ubiquinone levels. Serum tryptophan, serotonin, strychnine, nicotine and quinolinic acid were elevated while tyrosine, dopamine, morphine and norepinephrine were decreased. The total serum glycosaminoglycans and glycosaminoglycan fractions (except dermatan sulfate), the activity of glycosaminoglycans (GAG) degrading enzymes and glycohydrolases, carbohydrate residues of glycoproteins and serum glycolipids were elevated. Total serum cholesterol, LDL cholesterol and free fatty acids were increased while HDL cholesterol and triglycerides were unaltered. The concentration of membrane hexose, fucose, cholesterol and phospholipids in the RBC membrane decreased significantly but the total RBC membrane GAG was unaltered.Conclusions:Epileptogenesis could be due to a dysfunctional isoprenoidal pathway and paroxysmal hypothalamic digoxin hypersecretion.
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13

Morozenko, D. V., R. F. Yeromenko, K. V. Gliebova, O. P. Timoshenko, and A. V. Zakharyev. "Disorders of Proteoglycan and Collagen Metabolism in the Kidneys in Diabetes Mellitus: Clinical and Pathogenetic Mechanisms and Laboratory Markers." Ukraïnsʹkij žurnal medicini, bìologìï ta sportu 5, no. 6 (December 12, 2020): 355–61. http://dx.doi.org/10.26693/jmbs05.06.355.

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The article considers the issue of disorders of connective tissue metabolism in diabetes mellitus. Glycosylation of structural components of connective tissue and glucose toxicity have been found to determine the pathogenesis of late complications of diabetes mellitus. The most common concept of the pathogenesis of diabetes is metabolic, according to which all variants of diabetes mellitus, including blood vessels, their basement membrane, are associated with primary disorders of lipid, glycoprotein, protein and carbohydrate metabolism due to complete or partial insufficiency. It has been found that the formation of interstitial fibrosis in the kidneys of patients with diabetes begins in the preclinical stages of diabetic nephropathy. The leading cause of interstitial fibrogenesis is hyperglycemia; exacerbate proteinuria fibrosis, activation of the renin-angiotensin system, chronic inflammation and the formation of myofibroblasts in the interstitium. According to the results of the study of aspects of early diagnosis of kidney damage in type 1 diabetes mellitus, it was found that the development of diabetic nephrosclerosis is characterized by qualitative and quantitative changes in collagen composition in the glomeruli and interstitium, rebalance between collagen synthesis and breakdown, glycosaminoglycans, increased synthesis of fibrogenic growth factors and oxidative modification of proteins. The formation of diabetic nephropathy in patients with diabetes is also characterized by the accumulation of collagen types IV and VI, the appearance of interstitial collagen types III and I in the glomeruli, as well as the accumulation of collagen of all types in tubulointerstitium. Quantitative and qualitative characteristics of sulfated glycosaminoglycans of urine in human diabetes indicated different degrees of development of diabetic nephropathy. Glycosaminoglycans hyperexcretion was observed in patients with diabetes mellitus without proteinuria. In patients with microalbuminuria, glycosaminoglycans hyperexcretion was even more pronounced. It was also found that in diabetes, the total excretion of sulfated glycosaminoglycans in the urine doubles. Conclusion. Thus, in diabetes mellitus, an important pathogenetic link in the violation of the morpho-functional state of the kidneys is the degradation of collagen and proteoglycans of the basement membranes of the glomeruli, as well as interstitial fibrosis. This is reflected in changes in urinary glycosaminoglycans excretion, in particular heparansulfate and chondroitin sulfate, which may serve as a marker of proteoglycan metabolism disorders in the kidneys. Patients with diabetes also have an increase in the urine of hydroxyproline, which indicates an increase in the intensity of collagen metabolism in patients
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14

TANAKA, Tastuo. "The metabolism of glycosaminoglycans in gingiva of pregnant rat." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 28, no. 2 (1986): 516–30. http://dx.doi.org/10.2329/perio.28.516.

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15

Mayer-Sonnenfeld, Tehila, Marsha Zeigler, Michele Halimi, Yael Dayan, Christian Herzog, Corinne I. Lasmezas, and Ruth Gabizon. "The metabolism of glycosaminoglycans is impaired in prion diseases." Neurobiology of Disease 20, no. 3 (December 2005): 738–43. http://dx.doi.org/10.1016/j.nbd.2005.05.009.

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16

Staprans, I., J. M. Felts, and W. G. Couser. "Glycosaminoglycans and chylomicron metabolism in control and nephrotic rats." Metabolism 36, no. 5 (May 1987): 496–501. http://dx.doi.org/10.1016/0026-0495(87)90050-3.

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17

Steiner, Manfred. "Role of glycosaminoglycans in calcium metabolism of human platelets." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 886, no. 3 (May 1986): 406–10. http://dx.doi.org/10.1016/0167-4889(86)90176-x.

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18

Näntö-Salonen, Kirsti, Hannu Larjava, Maija Aalto, and Tarmo Kivimäki. "Urinary glycosaminoglycans in aspartylglycosaminuria: evidence for disturbed proteoglycan metabolism." Clinica Chimica Acta 146, no. 2-3 (March 1985): 111–18. http://dx.doi.org/10.1016/0009-8981(85)90049-x.

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19

Uijtdewilligen, P. J. E., E. M. Versteeg, E. M. A. van de Westerlo, J. van der Vlag, W. F. Daamen, and T. H. van Kuppevelt. "Dynamic Expression of Genes Involved in Proteoglycan/Glycosaminoglycan Metabolism during Skin Development." BioMed Research International 2018 (August 29, 2018): 1–16. http://dx.doi.org/10.1155/2018/9873471.

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Glycosaminoglycans are important for cell signaling and therefore for proper embryonic development and adult homeostasis. Expressions of genes involved in proteoglycan/glycosaminoglycan (GAG) metabolism and of genes coding for growth factors known to bind GAGs were analyzed during skin development by microarray analysis and real time quantitative PCR. GAG related genes were organized in six categories based on their role in GAG homeostasis, viz. (1) production of precursor molecules, (2) production of core proteins, (3) synthesis of the linkage region, (4) polymerization, (5) modification, and (6) degradation of the GAG chain. In all categories highly dynamic up- and downregulations were observed during skin development, including differential expression of GAG modifying isoenzymes, core proteins, and growth factors. In two mice models, one overexpressing heparanase and one lacking C5 epimerase, differential expression of only few genes was observed. Data show that during skin development a highly dynamic and complex expression of GAG-associated genes occurs. This likely reflects quantitative and qualitative changes in GAGs/proteoglycans, including structural fine tuning, which may be correlated with growth factor handling.
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20

Imai, Yumi, Ritsuko Odajima, Yoichi Inoue, and Yoshimasa Shishiba. "Effect of growth factors on hyaluronan and proteoglycan synthesis by retroocular tissue fibroblasts of Graves' ophthalmopathy in culture." Acta Endocrinologica 126, no. 6 (June 1992): 541–52. http://dx.doi.org/10.1530/acta.0.1260541.

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One of the pathological changes seen in Graves' ophthalmopathy is the deposition of glycosaminoglycans such as hyaluronan and proteoglycan in retroocular connective tissue. We analyzed glycosaminoglycans synthesized by retroocular tissue fibroblasts in culture derived from an individual not suffering from thyroid disease and from three patients with Graves' ophthalmopathy. Retroocular tissue fibroblasts synthesized both hyaluronan and proteoglycan, the latter composed mainly of chondroitin sulfate. This contrasts with the proteoglycan synthesized by adult skin fibroblasts which was composed of dermatan sulfate and heparan sulfate proteoglycan. Chondroitin sulfate proteoglycan secreted by retroocular tissue fibroblasts consisted of large and small chondroitin sulfate proteoglycans (CS-PG), their size being determined by the Sepharose CL-6B column. The effects of IGF-1 and PDGF on hyaluronan and proteoglycan synthesis were studied separately and in combination. Both IGF-1 and PDGF increased the synthesis of hyaluronan and proteoglycan in a dose-dependent manner. IGF-1 predominantly stimulated secretion of small CS-PG, while PDGF increased large CS-PG markedly when studied in retroocular tissue fibroblasts. In contrast, IGF-1 stimulated secretion of small proteoglycan while PDGF had little effect on proteoglycan synthesis in skin fibroblasts. Thus, glycosaminoglycan synthesized by retroocular tissue fibroblasts has a unique composition and each component is regulated independently, at least in part.
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21

KAHALY, GEORGE, GREGOR FÖRSTER, and CHRISTIANE HANSEN. "Glycosaminoglycans in Thyroid Eye Disease." Thyroid 8, no. 5 (May 1998): 429–32. http://dx.doi.org/10.1089/thy.1998.8.429.

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22

Vorontsov, A. V., I. I. Dedov, M. V. Shestakova, T. M. Milenkaya, and A. P. Knyazeva. "Glycosaminoglycans in therapy of diabetic nephropathy." Problems of Endocrinology 42, no. 5 (October 15, 1996): 14–18. http://dx.doi.org/10.14341/probl12082.

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Sulodexide, a drug containing glycosaminoglycans, was used in the treatment of patients with type I diabetes. Along with their effects on the blood clotting system, glycosaminoglycans are capable of preventing the mesangial proliferation and hyperproduction of extracellular matrix, as well as thickening of the glomerular basal membrane and impairment of its permeability and charge selection. A reliable antiproteinuric effect of the drug was noted, persisting for 6 weeks after it was discontinued; the excretion of protein with the urine reliably decreased in patients with both, microalbuminuria and proteinuria. Moreover, an antiatherogenic effect (a reliable decrease of serum atherogenicity coefficient) of sulodexide was observed. Assessment of the status of the fundus oculi of diabetics treated with sulodexide demonstrated a positive dynamics during therapy in some of the patients with nonproliferative and preproliferative retinopathy; no deterioration as regards the fundus oculi were noted. Hence, addition of sulodexide to combined therapy of patients with diabetic nephropathy is effective and pathogenetically justified.
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23

Baud'Huin, M., C. Ruiz Velasco, G. Jego, C. Charrier, M. Maillasson, F. Redini, D. Heymann, and L. Duplomb. "Glycosaminoglycans inhibit rankl-induced osteoclastogenesis." Bone 44 (June 2009): S334. http://dx.doi.org/10.1016/j.bone.2009.03.640.

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24

Khan, Shaukat, Carlos J. Alméciga-Díaz, Kazuki Sawamoto, William G. Mackenzie, Mary C. Theroux, Christian Pizarro, Robert W. Mason, Tadao Orii, and Shunji Tomatsu. "Mucopolysaccharidosis IVA and glycosaminoglycans." Molecular Genetics and Metabolism 120, no. 1-2 (January 2017): 78–95. http://dx.doi.org/10.1016/j.ymgme.2016.11.007.

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25

Winsz-Szczotka, Katarzyna, Łukasz Mencner, and Krystyna Olczyk. "Metabolism of glycosaminoglycans in the course of juvenile idiopathic arthritis." Postępy Higieny i Medycyny Doświadczalnej 70 (March 4, 2016): 135–42. http://dx.doi.org/10.5604/17322693.1196355.

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26

Pinto, D. O. "Biosynthesis and metabolism of sulfated glycosaminoglycans during Drosophila melanogaster development." Glycobiology 14, no. 6 (January 22, 2004): 529–36. http://dx.doi.org/10.1093/glycob/cwh070.

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SCHULER, M., G. KAHALY, A. C. SEWELL, H. SCHMIDT, G. BERNHARD, J. BEYER, and U. KRAUSE. "Urinary glycosaminoglycans in endocrine ophthalmopathy." Acta Endocrinologica 120, no. 3_Suppl (June 1989): S39—S40. http://dx.doi.org/10.1530/acta.0.120s039.

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28

Vyatkin, V. A., E. G. Butolin, and V. G. Ivanov. "Effect of chondroitin sulfate on the type I collagen metabolism in the compact bone in alloxan-induced rats." Kazan medical journal 96, no. 5 (October 15, 2015): 802–6. http://dx.doi.org/10.17750/kmj2015-802.

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Aim. To study the type I collagen metabolism in the compact bone in rats with alloxan-induced diabetes receiving sulfated glycosaminoglycans.
 Methods. The study was performed on 67 white outbred male rats with body weight of 180-220 g. Mortality at diabetes reproduction was 44.8%. To clarify the role of exogenous glycosaminoglycans on bone collagen metabolism at diabetes mellitus, 16 animals with alloxan-induced diabetes received 1 mg/kg of chondroitin sulfate intramuscularly every second day. The second group (21 animals) with alloxan-induced diabetes did not received any chondroitin sulfate. Control group included 10 intact animals who were administered a single injection on 0.5% ml of normal saline. The levels of type I collagen metabolism markers (PINP - aminoterminal propeptide of type I procollagen, a marker of bone formation; β-CrossLaps - β-isomerized carboxy-terminal cross-linking region of type I collagen, a marker of bone resorption) and the amount of total collagen were determined in homogenates of femoral shaft.
 Results. Administration of alloxan to the animals has induced the development of diabetes mellitus. The levels of PINP and β-CrossLaps was significantly higher in alloxan-induced rats which were administered chondroitin sulfate compared to rats with «isolated» alloxan-induced diabetes by 21 (p=0.001) and 28 (p=0.01) days of follow-up, the level of total collagen was higher at 70% at 28 day of the experiment (p=0.0004).
 Conclusion. Effect of sulfated glycosaminoglycans on type I collagen metabolism of the compact bone in animals with «isolated» alloxan-induced diabetes is manifested by intensified catabolic and anabolic processes with a predominance of the latter over the control and alloxan-induced rats at 21 and 28 days of the experiment.
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29

Kahaly, G., Ch Hansen, E. Otto, G. Förster, J. Beyer, and G. Hommel. "Diabetic microangiopathy and urinary glycosaminoglycans." Experimental and Clinical Endocrinology & Diabetes 105, no. 03 (July 14, 2009): 145–51. http://dx.doi.org/10.1055/s-0029-1211743.

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30

Bishop, R. E., and J. J. Torres. "Leptocephalus energetics: metabolism and excretion." Journal of Experimental Biology 202, no. 18 (September 15, 1999): 2485–93. http://dx.doi.org/10.1242/jeb.202.18.2485.

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Leptocephali are the unusual transparent larvae that are typical of eels, bonefish, tarpon and ladyfish. Unlike the larvae of all other fishes, leptocephali may remain in the plankton as larvae for several months before metamorphosing into the juvenile form. During their planktonic phase, leptocephali accumulate energy reserves in the form of glycosaminoglycans, which are then expended to fuel metamorphosis. The leptocephalus developmental strategy is thus fundamentally different from that exhibited in all other fishes in two respects: it is far longer in duration and energy reserves are accumulated. It was anticipated that the unusual character of leptocephalus development would be reflected in the energy budget of the larva. This study describes the allocation of energy to metabolism and excretion, two important elements of the energy budget. Metabolic rates were measured directly in four species of leptocephali, Paraconger caudilimbatus, Ariosoma balearicum, Gymnothorax saxicola and Ophichthus gomesii, using sealed-jar respirometry at sea. Direct measurements of metabolic rates were corroborated by measuring activities of lactate dehydrogenase and citrate synthase, two key enzymes of intermediary metabolism, in addition to that of Na(+)/K(+)-ATPase, a ubiquitous ion pump important in osmotic regulation. Excretion rates were determined by subsampling the sea water used in the respiratory incubations. The entire premetamorphic size range for each species was used in all assays. Mass-specific oxygen consumption rate, excretion rate and all enzyme activities (y) declined precipitously with increasing mass (M) according to the equation y=aM(b), where a is a species-specific constant and −1.74<b<-0.44. In leptocephali, the highly negative slope of the familiar allometric equation describing the relationship between mass-specific metabolic rate and mass, normally between −0.33 and 0, showed that a massive decline in metabolic rate occurs with increasing size. The result suggests that the proportion of actively metabolizing tissue also declines with size, being replaced in large measure by the metabolically inert energy depot, the glycosaminoglycans. Leptocephali can thus grow to a large size with minimal metabolic penalty, which is an unusual and successful developmental strategy.
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31

Silbert, Jeremiah. "Metabolism and Structure-Function Relationships of Connective Tissue Glycosaminoglycans and Proteoglycans." Current Organic Chemistry 8, no. 5 (March 1, 2004): 395–411. http://dx.doi.org/10.2174/1385272043485864.

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32

SHIRAKI, Masafumi, Tatsuo TANAKA, Toshiko HORI, Kiyoshi MIZUNO, Yoshinobu MURAHASHI, Yukio IWAYAMA, and Tie-Zheng TAN. "Autoradiographic studies on the metabolism of gingival glycosaminoglycans in experimental periodontitis." Nihon Shishubyo Gakkai Kaishi (Journal of the Japanese Society of Periodontology) 31, no. 2 (1989): 667–74. http://dx.doi.org/10.2329/perio.31.667.

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33

Lucon, Marcos, Joao Roberto Martins, Katia Ramos Moreira Leite, Roberto Soler, Helena B. Nader, Miguel Srougi, and Homero Bruschini. "Evaluation of the metabolism of glycosaminoglycans in patients with interstitial cystis." International braz j urol 40, no. 1 (January 2014): 72–79. http://dx.doi.org/10.1590/s1677-5538.ibju.2014.01.11.

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34

Luikart, SD, JL Sackrison, and CV Thomas. "Altered glycosaminoglycan production by HL-60 cells treated with 4- methylumbelliferyl-beta-D-xyloside." Blood 66, no. 4 (October 1, 1985): 866–72. http://dx.doi.org/10.1182/blood.v66.4.866.866.

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Abstract Glycosaminoglycans, mainly chondroitin 4-sulfate, are located in the primary granules of human myeloid cells. These polyanionic carbohydrates are believed to play an important role in leukocyte maturation and function. To study the effect of altered chondroitin sulfate metabolism on human promyelocytic leukemia cells, we have treated HL-60 cells with 4-methylumbelliferyl-beta-D-xyloside. beta-D- Xylosides initiate the synthesis of free chondroitin sulfate chains. Cytochemical studies of treated cells demonstrated a marked increase in cytoplasmic granules stained with cationic dyes. This was confirmed by radiolabeled precursor incorporation studies that demonstrated a 344% increase in 35S-sulfate uptake into glycosaminoglycans associated with the cells and a 39% increase in incorporation into glycosaminoglycans released into the media. Chromatographic analyses of these glycosaminoglycans from treated cells demonstrated that the newly formed chondroitin sulfate chains were not attached to protein core and were of shorter length, but of greater charge density than chondroitin sulfate produced by control cells. Thus, beta-D-xyloside appears to alter the protein linkage, chain length, and sulfation of chondroitin sulfate produced by HL-60 cells, and these changes are morphologically evident. These biochemically altered cells may provide important information concerning the role of these macromolecules in myeloid development.
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35

Luikart, SD, JL Sackrison, and CV Thomas. "Altered glycosaminoglycan production by HL-60 cells treated with 4- methylumbelliferyl-beta-D-xyloside." Blood 66, no. 4 (October 1, 1985): 866–72. http://dx.doi.org/10.1182/blood.v66.4.866.bloodjournal664866.

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Glycosaminoglycans, mainly chondroitin 4-sulfate, are located in the primary granules of human myeloid cells. These polyanionic carbohydrates are believed to play an important role in leukocyte maturation and function. To study the effect of altered chondroitin sulfate metabolism on human promyelocytic leukemia cells, we have treated HL-60 cells with 4-methylumbelliferyl-beta-D-xyloside. beta-D- Xylosides initiate the synthesis of free chondroitin sulfate chains. Cytochemical studies of treated cells demonstrated a marked increase in cytoplasmic granules stained with cationic dyes. This was confirmed by radiolabeled precursor incorporation studies that demonstrated a 344% increase in 35S-sulfate uptake into glycosaminoglycans associated with the cells and a 39% increase in incorporation into glycosaminoglycans released into the media. Chromatographic analyses of these glycosaminoglycans from treated cells demonstrated that the newly formed chondroitin sulfate chains were not attached to protein core and were of shorter length, but of greater charge density than chondroitin sulfate produced by control cells. Thus, beta-D-xyloside appears to alter the protein linkage, chain length, and sulfation of chondroitin sulfate produced by HL-60 cells, and these changes are morphologically evident. These biochemically altered cells may provide important information concerning the role of these macromolecules in myeloid development.
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36

Masuda, H., T. Ozeki, I. Takazono, and Y. Tanaka. "Analyses of glycosaminoglycans in human lung cancer." Biochemical Medicine and Metabolic Biology 37, no. 3 (June 1987): 366–73. http://dx.doi.org/10.1016/0885-4505(87)90050-8.

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37

Masuda, H., T. Ozeki, I. Takazono, and Y. Tanaka. "Composition of glycosaminoglycans in human pancreatic cancer." Biochemical Medicine and Metabolic Biology 41, no. 3 (June 1989): 193–200. http://dx.doi.org/10.1016/0885-4505(89)90026-1.

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38

Ashhurst, D. E., and M. Page. "Collagens and glycosaminoglycans associated with fracture healing." Bone 7, no. 5 (January 1986): 393. http://dx.doi.org/10.1016/8756-3282(86)90279-6.

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39

Gambaro, Giovanni, and Bruno Baggio. "Role of glycosaminoglycans in diabetic nephropathy." Acta Diabetologica 29, no. 3-4 (1992): 149–55. http://dx.doi.org/10.1007/bf00573480.

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40

Maccari, Francesca, Dealba Gheduzzi, and Nicola Volpi. "Anomalous Structure of Urinary Glycosaminoglycans in Patients with Pseudoxanthoma Elasticum." Clinical Chemistry 49, no. 3 (March 1, 2003): 380–88. http://dx.doi.org/10.1373/49.3.380.

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Abstract Background: Pseudoxanthoma elasticum (PXE) is a hereditary connective tissue disease in which proteoglycans have altered properties. We investigated whether altered proteoglycan metabolism occurs in vivo and may be reflected in the urine of PXE individuals by analyzing the excreted polysaccharides. Methods: We measured sulfated glycosaminoglycans in the urine of 10 PXE-affected patients, 12 healthy carriers, and 20 healthy controls by agarose gel electrophoresis. Chondroitin sulfate and heparan sulfate disaccharides were also quantified by treatment with specific lyases and separation of products by chromatography. Results: Total polysaccharides were 34% lower in the urine of PXE-affected patients and 17% lower in healthy carriers than in the control group. Chondroitin sulfate was significantly (P <0.01) decreased, and heparan sulfate was significantly increased. The ratio of chondroitin sulfate to heparan sulfate was 2.7 for PXE-affected patients, 2.3 for healthy carriers, and 10.7 for controls. In PXE-affected individuals and carriers, chondroitin sulfate contained more 4-sulfated disaccharide, less 6-sulfated disaccharide, and decreased nonsulfated disaccharide. Heparan sulfate from PXE-affected individuals and healthy carriers produced significantly less N-sulfated disaccharide and more disaccharide sulfated at the C-6 position with no significant abnormality of the nonsulfated disaccharide percentage and sulfates:disaccharide ratio. Conclusions: The urinary data support the concept that the inherited defect of the ABCC6/MRP6 transporter in PXE alters metabolism of key polysaccharides. Structural analysis of urinary sulfated polyanions may be useful in the diagnosis of PXE.
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41

Hansen, Ch, A. Irmscher, K. Kuhlemann, J. Beyer, and G. Kahaly. "Insulin-Dependent Diabetes Mellitus and Glycosaminoglycans." Hormone and Metabolic Research 27, no. 12 (December 1995): 555–58. http://dx.doi.org/10.1055/s-2007-980024.

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42

Ysart, G. E., and R. M. Mason. "Serum factors, growth factors and UDP-sugar metabolism in bovine articular cartilage chondrocytes." Biochemical Journal 303, no. 3 (November 1, 1994): 713–21. http://dx.doi.org/10.1042/bj3030713.

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1. The effect of different batches of fetal bovine serum and of growth factors on [35S]sulphate incorporation into glycosaminoglycans and on UDP-sugar pools in explant cultures of bovine articular cartilage was investigated. 2. [35S]Sulphate incorporation was variably stimulated between 1.2- and 3.5-fold by four different batches of serum. The UDP-glucuronate pool size expanded 4.3-6.5-fold in the presence of serum, even in those cultures in which little stimulation of [35S]sulphate incorporation occurred. The UDP-N-acetylhexosamine and UDP-hexose pools expanded by about 1.5- and 2.0-fold respectively in the presence of serum. UDP-xylose was not detected. 3. Equilibrium-labelling and pulse-chase experiments with D-[1-3H]glucose indicated that the rate of flux through the UDP-sugar pools was unaffected by serum. UDP-hexose, UDP-N-acetylhexosamine and UDP-glucuronate have approximate half-lives (t1/2) of 7, 12 and 3-4 min respectively. At equilibrium, the 3H specific activities of UDP-hexose and UDP-N-acetylhexosamine were very similar but that for the UDP-glucuronate pool was much higher, especially in serum-supplemented cultures. The results suggest that UDP-glucuronate synthesis occurs via a pathway which is independent of the main UDP-hexose pathway. 4. Supplementing cultures with heat-treated serum had no effect on the serum-induced expansion of UDP-sugar pools but stimulation of [35S]sulphate incorporation into glycosaminoglycans was 50% lower than for native serum. Acid-treated serum promoted a 2-fold expansion of the UDP-glucuronate and UDP-N-acetylhexosamine pool over that obtained with native serum but was 20% less effective in stimulating [35S]sulphate incorporation than the latter. Prior dialysis of serum had no effect on its modulatory action on either [35S]sulphate incorporation or on the size of UDP-sugar pools. 5. Insulin-like growth factor 1 (IGF-1), transforming growth factor beta-1 (TGF beta-1), platelet-derived growth factor (PDGF) (BB homodimer) and epidermal growth factor (EGF) all stimulated [35S]sulphate incorporation into glycosaminoglycans as expected. The UDP-glucuronate pool expanded by 1.5- and 2.0-fold in the presence of IGF-1 and TGF beta-1 respectively, and by about 1.8-fold in the presence of PDGF or EGF. None of the factors investigated, or combinations of IGF-1 and TGF beta-1 or IGF-1 and EGF, stimulated expansion of the UDP-glucuronate pool to the same extent as native serum.(ABSTRACT TRUNCATED AT 400 WORDS)
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43

Amendum, Paige, Shaukat Khan, Seiji Yamaguchi, Hironori Kobayashi, Yasuhiko Ago, Yasuyuki Suzuki, Betul Celik, et al. "Glycosaminoglycans as Biomarkers for Mucopolysaccharidoses and Other Disorders." Diagnostics 11, no. 9 (August 28, 2021): 1563. http://dx.doi.org/10.3390/diagnostics11091563.

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Glycosaminoglycans (GAGs) are present in proteoglycans, which play critical physiological roles in various tissues. They are known to be elevated in mucopolysaccharidoses (MPS), a group of rare inherited metabolic diseases in which the lysosomal enzyme required to break down one or more GAG is deficient. In a previous study, we found elevation of GAGs in a subset of patients without MPS. In the current study, we aim to investigate serum GAG levels in patients with conditions beyond MPS. In our investigated samples, the largest group of patients had a clinical diagnosis of viral or non-viral encephalopathy. Clinical diagnoses and conditions also included epilepsy, fatty acid metabolism disorders, respiratory and renal disorders, liver disorders, hypoglycemia, developmental disorders, hyperCKemia, myopathy, acidosis, and vomiting disorders. While there was no conclusive evidence across all ages for any disease, serum GAG levels were elevated in patients with encephalopathy and some patients with other conditions. These preliminary findings suggest that serum GAGs are potential biomarkers in MPS and other disorders. In conclusion, we propose that GAGs elevated in blood can be used as biomarkers in the diagnosis and prognosis of various diseases in childhood; however, further designed experiments with larger sample sizes are required.
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44

Kubaski, Francyne, Harumi Osago, Robert W. Mason, Seiji Yamaguchi, Hironori Kobayashi, Mikako Tsuchiya, Tadao Orii, and Shunji Tomatsu. "Glycosaminoglycans detection methods: Applications of mass spectrometry." Molecular Genetics and Metabolism 120, no. 1-2 (January 2017): 67–77. http://dx.doi.org/10.1016/j.ymgme.2016.09.005.

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45

Karlinsky, J. B., P. J. Bucay, D. E. Ciccolella, and M. P. Crowley. "Effects of intratracheal endotoxin administration on hamster lung glycosaminoglycans." American Journal of Physiology-Lung Cellular and Molecular Physiology 261, no. 2 (August 1, 1991): L148—L155. http://dx.doi.org/10.1152/ajplung.1991.261.2.l148.

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Incorporation of [3H]glucosamine and 35S into glycosaminoglycan (GAG) was measured in hamster lung explant cultures at 0, 1, 4, and 24 h after a single endotracheal instillation of Escherichia coli endotoxin. Lung content of GAG was measured in a second group of treated animals over an 8-day period. Albumin was detected after endotoxin treatment in bronchoalveolar lavage fluid at 24 h but was not found in lavage fluid 7 days later or in lavage fluid of saline-treated animals. Over the initial 24 h, increasing amounts of radiolabeled precursor molecules were incorporated into all classes of GAG. Proportionally more radiolabel was incorporated into hyaluronic acid and chondroitin sulfate, and less was incorporated into heparan sulfate. The proportion of radiolabel incorporated into dermatan sulfate did not change. Total lung content of hyaluronate and chondroitin sulfate was elevated at 24 h but was returning to baseline by 8 days. The lung content of dermatan sulfate was increased at 8 days; lung content of heparan sulfate did not change over the 8-day study period. Elevations in the amount of explant heparan sulfate that bound to antithrombin III (AT III) were found at 1 h after both saline and endotoxin treatment. Radiosulfated heparan sulfates were found in blood from hamsters treated with endotoxin 1 h previously; these heparan sulfates did not bind to AT III. However, blood contained heparin-like activity. We conclude that endotoxin differentially alters the metabolism of each class of hamster lung glycosaminoglycans and that metabolic changes begin very rapidly after endotoxin exposure. The relation of pulmonary endothelial injury to the presence of heparin-like activity in blood is not yet clear.
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46

Koźma, E. M., K. Olczyk, A. Głowacki, K. Komosińska, P. Sonecki, T. Najmiec, and M. Jaźwiec. "Glycosaminoglycans of human serum and their alterations in diabetes mellitus." Acta Biochimica Polonica 43, no. 3 (September 30, 1996): 567–74. http://dx.doi.org/10.18388/abp.1996_4492.

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Human serum contains several glycosaminoglycans (GAGs), mainly chondroitin sulphates and significantly less of heparan sulphate + heparin and dermatan sulphate. The non-insulin-dependent diabetes mellitus (with vascular complications) was associated with a significant increase in total serum GAG concentration, mainly of chondroitin sulphates and dermatan sulphate, with a simultaneous decrease in heparan sulphate + heparin level. These alterations were much more evident in patients with poor metabolic control. Hyaluronic acid (undetectable in healthy subjects and in patients with good metabolic control) appeared only in trace amounts in poorly controlled diabetic individuals. The obtained data allow to conclude that the diabetes mellitus-associated disturbances in tissue GAG metabolism lead to significant alterations in serum GAG composition.
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47

Wu, V. Y., B. Wilson, and M. P. Cohen. "Disturbances in Glomerular Basement Membrane Glycosaminoglycans in Experimental Diabetes." Diabetes 36, no. 6 (June 1, 1987): 679–83. http://dx.doi.org/10.2337/diab.36.6.679.

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48

Wu, V. Y., B. Wilson, and M. P. Cohen. "Disturbances in glomerular basement membrane glycosaminoglycans in experimental diabetes." Diabetes 36, no. 6 (June 1, 1987): 679–83. http://dx.doi.org/10.2337/diabetes.36.6.679.

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49

Hill, D. J., A. Logan, M. McGarry та D. De Sousa. "Control of protein and matrix-molecule synthesis in isolated ovine fetal growth-plate chondrocytes by the interactions of basic fibroblast growth factor, insulin-like growth factors-I and -II, insulin and transforming growth factor-β1". Journal of Endocrinology 133, № 3 (червень 1992): 363–73. http://dx.doi.org/10.1677/joe.0.1330363.

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ABSTRACT Chondrogenesis is thought to be controlled by interactions between circulating anabolic hormones and locally produced peptide growth factors, and involves ordered changes in matrix composition which ultimately allow endochondral calcification. We have used a model of isolated ovine fetal growth-plate chondrocytes to examine the actions and interactions of basic fibroblast growth factor (basic FGF), insulin-like growth factors-I and -II (IGF-I and -II), insulin and transforming growth factor-β1 (TGF-β1) on total protein, collagen or non-collagenous protein and sulphated glycosaminoglycan synthesis. These parameters were determined by assessment of the incorporation by monolayer cultures of early passage chondrocytes of [3H]leucine, [14C]proline and [35S]sulphate respectively, followed by partial molecular characterization. Basic FGF enhanced total protein synthesis with a half-maximal effective concentration of 270 ± 60 pmol/l (mean ± s.e.m., four animals) and was sixfold more active on a molar basis than IGF-I or insulin, and 28-fold more active that IGF-II which is the endogenously synthesized IGF. The actions of basic FGF were additive to those of IGF-I or insulin. More detailed analysis of extracellular-matrix component synthesis showed that basic FGF, IGF-I and insulin each caused significant increases in the synthesis of collagen and sulphated glycosaminoglycans. TGF-β1 had no effect on total protein synthesis by chondrocytes when present alone at concentrations of 200 pmol/l or less, but was inhibitory at 400 pmol/l. However, the use of this parameter masked a stimulatory action of 50 or 100 pmol TGF-β1 on sulphated glycosaminoglycan synthesis and a relative shift in the ratio of collagen: non-collagenous protein synthesis in favour of the former. A synergistic interaction existed between TGF-β1 (20–100 pmol/l) and basic FGF which potentiated total protein and collagen synthesis, and their actions on sulphated glycosaminoglycan production were additive. The same concentrations of TGF-β1 inhibited the ability of IGF-I or insulin to stimulate total protein or collagen synthesis, but were additive to their stimulatory effects on sulphated glycosaminoglycan synthesis. The results suggest that matrix-molecule composition and the anabolic status of the epiphyseal growth-plate may be modulated in utero by multiple interactions between peptide growth factors produced locally, such as basic FGF, IGF-II and TGF-β1, and circulating hormones such as insulin and IGF-I. Journal of Endocrinology (1992) 133, 363–373
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50

Kawakami, Yutaka, Hiromi Oku, Kazuharu Nomura, Shigeaki Gorie, and Hiromi Ohta. "Metabolism of a Glycosaminoglycan during Metamorphosis in the Japanese Conger eel,Conger myriaster." Research Letters in Biochemistry 2009 (2009): 1–5. http://dx.doi.org/10.1155/2009/251731.

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Hyaluronan (HA) is a linear polysaccharide of high molecular weight that exists as a component of the extracellular matrix. The larvae (leptocephali) of the Japanese conger eel (Anguilliformes:Conger myriaster) have high levels of hyaluronan (HA) which is thought to help control body water content. We isolated glycosaminoglycans (GAGs) from Japanese conger eel leptocephali and measured the changes in tissue HA content during metamorphosis. HA content decreased during metamorphosis. In contrast, neutral sugar content increased during metamorphosis. We hypothesize that the leptocephali utilize a metabolic pathway that converts HA to glucose during metamorphosis. Glucose may then be metabolized to glycogen and stored in the juvenile life-history stage.
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