Gene/Protein Disease Symptom Drug Enzyme Compound
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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)

A cytochemical study was performed on the lamprey ventral aorta with special reference to disulfide and sulfhydryl groups of microfibrils, using the high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) method combined with several other types of treatment. The HID-TCH-SP staining observed was classified into three categories: 1) weak staining in the periphery of collagen fibrils, 2) moderate staining in the boundaries of collagen fibrils, microfibrils and smooth muscle cells, and 3) intense staining of microfibrils. The first and second categories of staining were considered to represent chondroitin and/or heparan sulfate because of sensitivity of the staining to chondroitinase ABC (ChABC) and its specific localization. By contrast, the third category of staining was considered to represent disulfide and sulfhydryl groups of microfibrillar glycoprotein, because it was disclosed only after Oxone oxidation or thiosulfation and was not removed by ChABC digestion. Although this staining reactivity was not apparently altered by SH blockade prior to oxidation or thiosulfation, it was markedly diminished or completely inhibited by S-S reduction followed by SH blockade. These results indicate that lamprey aortic microfibrils contain more S-S groups than SH groups.
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PMID:Cytochemical detection of disulfide and sulfhydryl groups in lamprey aortic microfibrils. 169 75

We investigated the ultrastructural distribution and histochemical properties of sulfated glycoconjugates, which could be preserved by glutaraldehyde fixation, in secretory ameloblasts and developing enamel matrix, by use of the high iron diamine thiocarbohydrazide silver proteinate (HID-TCH-SP) staining and enzymatic digestion methods. Large type HID-TCH-SP stain deposits, approximately 10 nm in diameter, were detected on the interdigitating cell membrane of Tomes' process, inside some secretory granules, on the lateral cell membrane of stratum intermedium, in the basement membranes associated with outer enamel epithelium and endothelial cells of capillary, within the so-called hole region, and in the enamel matrix near future enamel-cement junction. A few large type stain deposits were, however, randomly distributed over the whole layer of enamel matrix. Small type stain deposits smaller than 5 nm in diameter were localized within some secretory granules and Golgi vesicles of ameloblasts and on the surface layer of developing enamel matrix. While the large type HID-TCH-SP stain deposits associated with the basement membranes and on the lateral cell membrane of stratum intermedium were susceptible to heparitinase, the others resisted enzymatic digestion not only by heparitinase but also by testicular hyaluronidase and chondroitinase ABC, indicating that they represent sulfated glycoconjugates other than heparan sulfate, chondroitin sulfate A, dermatan sulfate, or chondroitin sulfate C. On the other hand, HID-TCH-SP stain deposits within the secretory granules of odontoblasts and in the predentine matrix were susceptible to testicular hyaluronidase. Thus, it was confirmed that the composition of sulfated glycoconjugates secreted into the developing enamel matrix differs essentially from that of sulfated glycoconjugates associated with dentinogenesis.
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PMID:Sulfated glycoconjugates in rat incisor secretory ameloblasts and developing enamel matrix. 246 60

Chondroitin sulfate is known to be present in normal and leukemic myeloid cells; however, its definitive subcellular location and association with other glycosaminoglycans (GAGs) has not been demonstrated. We have studied the type and distribution of GAGs in neutrophil granule subpopulations of normal and leukemic myeloid cells using ultrastructural, cytochemical, immunologic, and biochemical methods. At the ultrastructural level, high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) stained sulfated glycoconjugates selectively in immature primary granules of normal promyelocytes and Auer rods and immature granules of leukemic myeloblasts. Staining was weak or absent in mature primary granules, whereas tertiary granules stained moderately. Primary granule staining with HID-TCH-SP was greatly diminished by prior treatment of the specimens with chondroitinase ABC and/or nitrous acid, indicating the presence of chondroitin sulfate and N-sulfated glycosaminoglycan. Immunostaining of myeloid cells with a rabbit antichondroitin 4-sulfate and ferritin-conjugated goat anti-rabbit IgG sequence resulted in staining of most primary granules. Biochemical analysis of GAGs from leukemic myeloblasts containing primary granules and Auer rods, but lacking secondary and tertiary granules, revealed 8 x 10(-17) mole of uronic acid/cell and electrophoretic and sulfaminohexose analysis showed 60%-70% chondroitin sulfate AC of heterogeneous molecular weight, 20%-30% of a GAG that most closely resembled heparan sulfate, and 10% dermatan sulfate. The lack of significant HID-TCH-SP staining of sulfate iin sites other than Auer rods and primary granules in leukemic myeloblasts indicates that these granules contain the chondroitin, dermatan, and heparan sulfate isolated from the same specimen. Similar GAGs are present in primary granules of normal cells as evidenced by their cytochemical and immunostaining properties. Thus, these studies demonstrate a heterogeneous population of GAGs not previously identified and localize these substances to the primary granule of leukemic and normal cells.
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PMID:Glycosaminoglycans in human neutrophils and leukemic myeloblasts: ultrastructural, cytochemical, immunologic, and biochemical characterization. 640 32

This study deals with the ultrastructure of the chondroitin sulphate proteoglycans of the Kurloff body, a large lysosomal organelle that stains metachromatically with Toluidine Blue and which is present in Kurloff cells (a blood cell unique to the guinea pig). Splenic tissues were fixed with 1% cetylpyridinium chloride (CPC) added to 4% paraformaldehyde and examined either after Spicer's high-iron diamine staining for sulphated anionic sites followed by post-fixation with ferrocyanide-osmium tetroxide or after a simple post-fixation with ferrocyanide-osmium tetroxide. CPC-precipitated sulphated sites were preferentially located at the periphery of the Kurloff body but, unexpectedly, were absent in the central matrix. Although their electron opacity was lower, these anionic sites were readily observable in the absence of HID-staining after sole post-fixation by ferrocyanide-reduced osmium. CPC-precipitated sulphated anionic sites were either associated with the myelin figures or constituted unexpected structures. They contained (i) tightly-stacked lamellae, with a very regular 4 nm periodicity, and (ii) groups of 2, 3, 4 short dense lines with a 3-5 nm periodicity. By taking into account the susceptibility of these HID-reactive structures towards chondroitinase ABC, these different sulphated components were assumed to be related to the proteochondroitin-4-sulphate previously characterized as the only major sulphated glycoconjugate of the Kurloff cell. Their colocalization with phospholipidic structures was suggested following observation of sections treated by a chloroform-methanol mixture.
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PMID:Kurloff cell ultrastructure after combined formaldehyde-cetylpyridinium chloride fixation and high-iron diamine staining. 767 81

We examined the presence of sialyl glycoconjugates in specific granules from murine bone marrow eosinophils. Lectin cytochemistry using Maackia amurensis lectin II (MAL II) specific for sialyl alpha-2,3 galactose residues demonstrated positive labeling in both immature and mature specific granules. Pretreatment with Clostridium neuraminidase or keratanase II eliminated the positive labeling of MAL II in the specific granules. High iron diamine-thiocarbohydrazide-silver proteinate physical development (HID-TCH-SP-PD) staining, which is specific for sulfated glycoconjugates, also positively labeled immature specific granules lacking crystalloids but not mature granules with crystalloids. Pretreatment with a combination of chondroitinase ABC and keratanase, or a combination of chondroitinase ABC and keratanase II, eliminated the positive labeling obtained with HID-TCH-SP-PD. These results indicate that the sialyl residues detected by MAL II are expressed as terminal sugar residues of keratan sulfate proteoglycan, which appears to be of the corneal type in view of its sensitivity to keratanase and keratanase II. (J Histochem Cytochem 47:481-488, 1999)
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PMID:Keratan sulfate glycosaminoglycans in murine eosinophil-specific granules. 1008 49