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Neuroprotection and Repair after Spinal Cord Injury
Published in Jacques Corcos, Gilles Karsenty, Thomas Kessler, David Ginsberg, Essentials of the Adult Neurogenic Bladder, 2020
In SCI, glial scars are thought to act as a barrier to regeneration and recovery. A glial scar's cellular component is composed predominantly of reactive astrocytes with the surrounding matrix rich in proteoglycans.42 This structure is thought to provide a physical barrier to axonal extension as well as to express proteins such as chondroitin sulfate proteoglycans that inhibit axonal growth.42 Chondroitinase ABC, which removes glycosaminoglycan side chains from these molecules, promotes axonal extension and functional recovery after SCI.43 In addition to being a potentially useful primary treatment in SCI, in limiting the glial scar and in reducing its inhibitory effects, chondroitinase ABC may be key in strategies involving cell transplant. Following cell transplantation, axons that traverse a cell transplant may be inhibited from reentering the CNS distally in part by glial scar.44
Antiproteoglycan Antibodies in Experimental Spondylarthritis
Published in Thomas F. Kresina, Monoclonal Antibodies, Cytokines, and Arthritis, 2020
Tibor T. Giant, Katalin Mikecz, Edit Buzás, Eric Dayer, A. Robin Poole
Progressive polyarthritis develops in Balb/c mice immunized with chondroitinase ABC-digested human fetal cartilage proteoglycan. Autoantibodies from arthritic animals and autoreactive monoclonal antibodies raised to mouse proteoglycan cross-react with these arthritogenic proteoglycans. However, the nature of the immunodominant or arthritogenic (auto)epitope(s) is not known. Epitopes on syngeneic mouse cartilage proteoglycan are sensitive to both protease and alkaline treatment, suggesting that the immunodominant (and perhaps the arthritogenic) region(s) of the proteoglycans are related to the core protein. Since chondroitinase ABC digestion is important to expose this immunodominant region and since isolated glycosaminoglycans and their fragments do not react with autoreactive monoclonal antibodies or autoantibodies from arthritic animals, we postulate that these particular epitopes are located on, or near, the chondroitin sulfate attachment region of core protein. However, it is not clear whether these epitopes on arthritogenic proteoglycans are sterically masked from the immune system by chondroitin sulfate chains or are expressed as “new” determinants after modifying the tertiary structure of the core protein by removal of the highly charged chondroitin sulfate side chains.
Immunohistochemical Characterization of Extracellular Matrix in Tumor Tissues
Published in Róza Ádány, Tumor Matrix Biology, 2017
Antibodies 3B3 and 9A2 react with the 6- and 4-sulfate disaccharide units, respectively, which are generated from the chondroitin sulfate chains by digestion with chondroitinase ABC. The antibodies do not recognize the entire constituency of the chondroitin sulfate-repeating units. Chondroitinase ABC, which is an endo-eliminase, can degrade the chondroitin sulfate chain so as to leave only one disaccharide unit attached to the linkage tetrasaccharide.121 The antibodies probably react to the disaccharide units bound intimately to the linkage tetrasaccharides. Couchman et al.108,109 showed that in addition to chondroitin 4-sulfate, dermatan sulfate was also stained with 9A2 in rat cartilage, dermis, and loose connective tissue after chondroitinase ABC digestion. In a previous study,122 we demonstrated that dermatan sulfate proteoglycan chains were detected in tissue sections treated with chondroitin B-lyase (pH 8.0), followed by staining with antibody 9A2 specific for unsaturated uronic acid coupled to N-acetylgalactosamine 4-sulfate. The distribution of dermatan sulfate thus revealed was confirmed by comparison with that found by monoclonal antibody 6B6, which reacts with small proteoglycans carrying dermatan sulfate side chains. The localization of positive staining in fibrous connective tissues was almost identical with these two procedures.
Isoflavones improve collagen I and glycosaminoglycans and prevent bone loss in type 1 diabetic rats
Published in Climacteric, 2020
A. A. F. Carbonel, M. C. Vieira, R. S. Simões, P. D. A. Lima, L. F. P. Fuchs, E. R. C. Girão, G. P. Cicivizzo, G. R. S. Sasso, L. O. Carvalho de Moraes, J. M. Soares Junior, E. C. Baracat, M. J. Simões, M. J. B. C. Girão
Five femurs shafts (2 mm) containing trabecular and cortical bone regions were collected from each group. Epiphyses were removed to exclude growth from this analysis. Following this procedure, the femurs were washed for 2 h in phosphate-buffered saline solution containing protease inhibitor. They were decalcified in a 25% solution of formic acid, at pH 2.0, for 3 days, kept in phosphate-buffered saline solution containing protease inhibitor, at a temperature of 4°C for 24 h, and then submitted to overnight proteolysis with papain at 60°C. GAG identification used the standards chondroitin-4-sulfate from whale cartilage, chondroitin-6-sulfate from shark cartilage, dermatan sulfate from bovine intestinal mucosa (Seikagaku Kogyo Co., Tokyo, Japan), and heparan sulfate from bovine lung34. GAG identification was improved using controls that were generated by enzymatic degradation of the sulfated GAGs using flavobacterium heparinum-derived chondroitinases. Dermatan sulfate and chondroitin sulfate were characterized after sample incubation with chondroitinase AC and chondroitinase ABC. The incubation products were submitted to agarose gel electrophoresis, and confirmation of the particular type of GAGs was accomplished by agarose gel band patterns. The same standards were also used for quantitative determination of the samples by 532 nm densitometry. The results were expressed as micrograms of GAGs per milligram of tissue (mean ± standard deviation). All were assayed in triplicate. The detection limit was 1 μg/μl of GAG sulfate.
Trehalose attenuates spinal cord injury through the regulation of oxidative stress, inflammation and GFAP expression in rats
Published in The Journal of Spinal Cord Medicine, 2019
Mahdieh Nazari-Robati, Mahboobe Akbari, Mohammad Khaksari, Moghaddameh Mirzaee
Trehalose, a nonreducing disaccharide, is synthesized by bacteria, yeast, fungi, insects and plants which preserves them against environmental stresses such as heat, freezing, desiccation, dehydration and oxidation.10 Besides these properties, recent reports showed that trehalose suppresses inflammatory response induced by endotoxic shock in vivo and in vitro.11,12 Moreover, trehalose treatment inhibited oxidative stress and inflammation in an experimental subarachnoid hemorrhage.13 Furthermore, trehalose could suppress TNFα production by bone marrow cells in lipopolysaccharide (LPS) injected mice.14 A recent study indicated that a combination of high dose of trehalose and chondroitinase ABC (cABC) administration promotes functional recovery after SCI.15 Furthermore, we showed that trehalose protects cABC against oxidative stress and proteolysis in vitro.16 However, the effect of trehalose on inflammatory response and oxidative stress following SCI has not been reported. Therefore, we designed this study to examine whether trehalose can suppress inflammation and oxidative stress induced in SCI. Additionally, we investigated astrocytes activation and locomotor function following trehalose treatment in an experimental model of SCI.
Concentration of sulfated glycosaminoglycans in the mammary tissue of female rats with the aging and about hormonal influence
Published in Gynecological Endocrinology, 2018
Sueli M. P. S. Torres, Helena B. Nader, Ricardo S. Simões, Edmund C. Baracat, Manuel de J. Simões, Luiz F. P. Fuchs, José Maria Soares-Jr, Regina Célia T. Gomes
CS, DS and HS were identified based on the migration of the compounds compared to known standards of CS (whale cartilage), DS (pig skin) (Seikagaku Kogyo Co., Tokyo, Japan), and HS (bovine pancreas) (Molecular Biology Division, UNIFESP – EPM, São Paulo, Brazil). The results were expressed as sulfated GAG μg/mg of dry tissue powder (Table 1, Figure 2). Due to the similarity of the chemical structures of CS and DS, it was necessary to submit the samples to enzymatic degradation to distinguish between them. Ten samples of purified sulfated GAG from each group were pooled, then 1. It is treated with the chondroitinase ABC lyase (Sigma-Aldrich, St. Louis, MO) acts degrading the CS and DS and 2. It treated with the chondroitinase AC lyase (Sigma-Aldrich, St. Louis, MO) that acts degrading the CS. The characterization of sulfated GAG was performed following the protocol earlier [13]. After the enzymatic degradation and characterization we conclude that: there is no CS in the analyzed samples.