Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.6.12 (chondroitinase)
 2,183 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies specific for unsulfated, 4-sulfated, and 6-sulfated disaccharide "stubs" that remain attached to the core protein after chondroitinase ABC digestion of chondroitin/dermatan sulfate proteoglycans have been used to study the localization of chondroitin and the two isomeric chondroitin sulfates in developing rat cerebellum. At 1-2 weeks postnatal, unsulfated chondroitin is present in the granule cell layer, molecular layer, and prospective white matter, but there was no staining of the external granule cell layer other than light staining of Bergmann glia fibers. By 3 weeks postnatal, staining of the molecular layer has disappeared and has diminished in the white matter, whereas in adult cerebellum only the granule cell layer remains stained. The staining pattern of chondroitin 4-sulfate is similar to that for chondroitin at 1-2 weeks postnatal, but in contrast to chondroitin, chondroitin 4-sulfate increases in the molecular layer at 3 weeks, and this becomes the most densely stained region of adult cerebellum. Chondroitin 6-sulfate is present predominantly in the prospective white matter of 1-2 week postnatal cerebellum, although significant staining of the granule cell layer is also seen. By 3 weeks postnatal the granule cell staining of chondroitin 6-sulfate has decreased, and in adult cerebellum staining is seen only in the white matter and to a lesser extent in the granule cell layer. Electron microscopy confirmed the presence of chondroitin sulfate in the cytoplasm of neurons and glia of adult brain.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Immunocytochemical localization of chondroitin and chondroitin 4- and 6-sulfates in developing rat cerebellum. 170 39

Chondroitin 6-sulfate depolymerizing activity was examined in the culture supernatant of Streptococcus intermedius ATCC 27335. 2-Acetamido-2-deoxy-3-O-(beta-D-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose was split from the substrate. The enzyme(s) was not active upon chondroitin 4-sulfate or dermatan sulfate, which indicated that the enzyme responsible for the depolymerization is chondroitinase C.
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PMID:Chondroitinase C activity of Streptococcus intermedius. 249 50

Chondroitin sulfate C has been used to demonstrate an approach of generating a range of unmodified glycosaminoglycan oligosaccharide fragments. This involves cleavage by oxymercuration treatment of the nonreducing terminal 4,5-unsaturated uronic acid (DeltaUA) residues from the fragments produced by enzymatic digestion of chondroitin sulfate with chondroitinase ABC. Carrying out the reaction on the unfractionated digestion mixture produces a range of mono- to tridecasaccharides, the compositions of which were established by liquid secondary ion mass spectrometry (LSIMS) and their chromatographic patterns compared with oligosaccharides in the untreated digest. Ten of the main sequences, tri- to octasaccharides, isolated by HPLC from the treated and untreated digests were fully characterized by a combination of LSIMS and 1H NMR. Of these, 6 are homologs of the series with structures DeltaUA1-[3GalNAc(6S)beta1- 4GlcAbeta1]n-3Gal-NAc(6S) and [GalNAc(6S)beta1-4GlcAbeta1]n- 3GalNAc(6S), where n = 1-3. The other 4 sequences, DeltaUA1-[3Gal-NAc(6S)beta1-4GlcAbeta1]n-3GalNAc(4S) and [GalNAc(6S)beta1-4GlcAbeta1]n-3GalNAc(4S), where n = 1 and 2, contain the alternative 4-sulfated GalNAc at the reducing terminal. These results establish that oligosaccharides generated by oxymercuration treatment retain their integrity and only lack the terminal DeltaUA residue.
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PMID:Generation and structural characterization of a range of unmodified chondroitin sulfate oligosaccharide fragments. 866 May 42

Extrinsic factors appear to contribute to the lack of regeneration in the injured adult spinal cord. It is likely that these extrinsic factors include a group of putative growth inhibitory molecules known as chondroitin sulfate proteoglycans (CSPGs). The aims of this study were to determine: (1) the consequences of spinal cord contusion injury on CSPG expression, (2) if CSPGs can be degraded in vivo by exogenous enzyme application, and (3) the effects of intraspinal transplantation on the expression of CSPGs. Chondroitin 6-sulfate proteoglycan immunoreactivity (CSPG-IR) dramatically increased following spinal cord contusion injury both at and adjacent to the injury site compared to normal controls (no surgical procedure) and laminectomy-only controls by 4 days postinjury. The dramatic increase in CSPG-IR persisted around the lesion and in the dorsal one-half to two-thirds of the spinal cord for at least 40 days postinjury. Glial fibrillary acidic protein (GFAP)-IR patterns were similarly intensified and spatially restricted as CSPG-IR patterns. These results suggest that: (1) CSPGs may contribute to the lack of regeneration following spinal cord injury and (2) astrocytes may contribute to the production of CSPGs. In addition, our results show that CSPGs could be cleaved in vivo with exogenous chondroitinase ABC application. This demonstration of cleavage may the basis for a model to directly assess CSPGs' role in growth inhibition in vivo (studies in progress) and hold potential as a therapeutic approach to enhance growth. Interestingly, the robust, injury-induced CSPG-IR patterns were not altered by intraspinal grafts of fetal spinal cord. The CSPG expression profile in the host spinal cord was similar to time-matched contusion-only animals. This was also true of GFAP-IR patterns. Furthermore, the fetal spinal cord tissue, which was generally CSPG negative at the time of transplantation, developed robust CSPG expression by 30 days posttransplantation. This increase in CSPG expression in the graft was paired with a moderate increase in GFAP-IR. CSPG-IR patterns suggest that these molecules may contribute to the limited regeneration seen following intraspinal transplantation. In addition, it suggests that the growth permissiveness of the graft may change overtime as CSPG expression develops within the graft. These correlations in the injured and transplanted spinal cord support CSPGs' putative growth inhibitory effect in the adult spinal cord.
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PMID:Chondroitin sulfate proteoglycan immunoreactivity increases following spinal cord injury and transplantation. 1063 Jan 90