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Target Concepts:
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Query: EC:3.1.6.4 (
chondroitinase
)
2,039
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
It has been proposed that hyaluronan-binding proteoglycans play an important role as guiding cues during neural crest (NC) cell migration, but their precise function has not been elucidated. In this study, we examine the distribution, structure and putative role of the two major hyaluronan-binding proteoglycans, PG-M/versicans and aggrecan, during the course of avian NC development. PG-M/versicans V0 and V1 are shown to be the prevalent isoforms at initial and advanced phases of NC cell movement, whereas the V2 and V3 transcripts are first detected following gangliogenesis. During NC cell dispersion, mRNAs for PG-M/versicans V0/V1 are transcribed by tissues lining the NC migratory pathways, as well as by tissues delimiting nonpermissive areas. Immunohistochemistry confirm the deposition of the macromolecules in these regions and highlight regional differences in the density of these proteoglycans. PG-M/versicans assembled within the sclerotome rearrange from an initially uniform distribution to a preferentially caudal localization, both at the mRNA and protein level. This reorganization is a direct consequence of the metameric NC cell migration through the rostral portion of the somites. As suggested by previous in situ hybridizations, aggrecan shows a virtually opposite distribution to PG-M/versicans being confined to the perinotochordal ECM and extending dorsolaterally in a segmentally organized manner eventually to the entire spinal cord at axial levels interspacing the ganglia. PG-M/versicans purified from the NC migratory routes are highly polydispersed, have an apparent M(r) of 1,200-2,000 kDa, are primarily substituted with chondroitin-6-sulfates and, upon
chondroitinase
ABC digestion, are found to be composed of core proteins with apparent M(r )of 360-530, 000.
TEM
/rotary shadowing analysis of the isolated PG-M/versicans confirmed that they exhibit the characteristic bi-globular shape, have core proteins with sizes predicted for the V0/V1 isoforms and carry relatively few extended glycosaminoglycan chains. Orthotopical implantation of PG-M/versicans immobilized onto transplantable micromembranes tend to 'attract' moving cells toward them, whereas similar implantations of a notochordal type-aggrecan retain both single and cohorts of moving NC cells in close proximity of the implant and thereby perturb their spatiotemporal migratory pattern. NC cells fail to migrate through three-dimensional collagen type I-aggrecan substrata in vitro, but locomote in a haptotactic manner through collagen type I-PG-M/versican V0 substrata via engagement of HNK-1 antigen-bearing cell surface components. The present data suggest that PG-M/versicans and notochordal aggrecan exert divergent guiding functions during NC cell dispersion, which are mediated by both their core proteins and glycosaminoglycan side chains and may involve 'haptotactic-like' motility phenomena. Whereas aggrecan defines strictly impenetrable embryonic areas, PG-M/versicans are central components of the NC migratory pathways favoring the directed movement of the cells.
...
PMID:Avian neural crest cell migration is diversely regulated by the two major hyaluronan-binding proteoglycans PG-M/versican and aggrecan. 1085 Nov 28
Tendon is composed of type I collagen fibers, interspersed with proteoglycan matrix and cells. Glycosaminoglycans may play a role in maintaining the structural integrity of tendon, preventing excessive shearing between collagen components. This study tests the hypothesis that tendon extension mechanisms can be altered by modifying the composition of noncollagenous matrix. Tendon explants were treated with phosphate buffered saline (PBS) or PBS + 0.5 U ml(-1)
chondroitinase
ABC. Structural changes were examined using
TEM
and biochemical analysis, while strain response was examined using confocal microscopy and gross mechanical characterization. Chondroitinase ABC removed 90% of glycosaminoglycans from the matrix. Results demonstrated significant swelling of fibrils and surrounding matrix when incubated in either solution. In response to applied strain, PBS incubated samples demonstrated significantly less sliding between adjacent fibers than nonincubated, and a 33% reduction in maximum force. By contrast, fascicles incubated in
chondroitinase
ABC demonstrated a similar strain response to nonincubated. Data indicate that collagen-proteoglycan binding characteristics can be influenced by incubation and this, in turn, can influence the preferred extension mechanisms adopted by fascicles. This highlights the importance of maintaining fascicles within their natural environment to prevent structural or mechanical changes prior to subsequent analysis.
...
PMID:The influence of noncollagenous matrix components on the micromechanical environment of tendon fascicles. 1613 17
The aim of this study was to investigate the relationship between proteoglycans (PGs) and collagen fibrils at the early mineralization process of mantle dentin. Ten first molar dental germs of rats were removed and fixed in glutaraldehyde/formaldehyde in cacodylate buffer and post-fixed in osmium tetroxide. The samples were dehydrated and embedded in epoxy resin. Ultrathin sections were contrasted and analyzed in
TEM
before and after treatment with EDTA, chondroitinases AC and ABC. After EDTA treatment, a electrondense substance associated with collagen fibril was removed, and did not stain again. A high magnification of these areas showed globular structures with 15 nm diameter surrounding collagen fibrils. In advanced mineralization areas, collagen fibrils showed a banded pattern and at high magnification the fibrils presented a light 10 nm ring inside and a dark 10 nm ring outside. After
chondroitinase
treatment, the electrondense substance associated with collagen fibrils was removed, showing a banded pattern of clear and dark areas along them. From morphological data, the authors proposed a model of interaction between PGs and collagen fibrils, where glicosaminoglycans chains are inside the fibrils, while the protein core remains outside. That stereochemical arrangement would start the crystal nucleation.
...
PMID:A model of the early mineralization process of mantle dentin. 1699 43