Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The aim of this study was to evaluate the differential localisation of glycoconjugates of bovine hyaline cartilage matrix by lectin histochemistry, to compare the results of lectin histochemistry with those that can be obtained in the same tissue with PAS and alcian blue. Frozen and paraffin sections were stained with HE, PAS and alcian blue (pH 1.8). Alcian blue staining was carried out also after 1 and 24 hour digestion with bovine testicular hyaluronidase. Peroxidase conjugated WGA, PNA and RS lectins were tested on all sections before and after 1 hour digestion with bovine testicular hyaluronidase. The results show that all the lectins used in this study react with sugars linked to proteoglycans of territorial matrix, the reaction being increased in territorial, and induced in interterritorial matrix by 1 hour hyaluronidase digestion. Alcian blue at pH 1.8 and PAS were complementary, the former staining territorial, and the latter interterritorial matrix. After 1 hour hyaluronidase digestion, alcian blue stained also the interterritorial matrix. These results suggest that lectins react with low molecular weight proteoglycans and that short hyaluronidase digestion causes depolymerization of high molecular weight proteoglycans without loss of their glucidic components, allowing: a) penetration of alcian blue molecules into the macromolecular proteoglycan network; b) an increase of sugar residuals available for lectin histochemistry. Lectin histochemistry can be useful for differential localisation of glycoconjugates in bovine cartilage, especially if associated with short hyaluronidase digestion and conventional histochemical techniques.
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PMID:Lectin binding properties of bovine resting cartilage. 754 42

Glycoconjugate modifications were analysed in the zona pellucida during development of oocytes in dog and cat using conventional histochemical staining methods with or without previous carbohydrate digestion. A series of lectins combined with desulphation and sialic acid degradation were applied. No differences were observed between dog and cat follicles using conventional histochemical staining methods. In both species, the zona pellucida and follicular fluid/intercellular matrix strongly reacted with PAS and high iron diamine stain (HID) and reacted moderately with low iron diamine stain (LID). Treatment with testicular hyaluronidase, chondroitinase ABC, chondroitinase AC and chondroitinase B treatment diminished HID and LID positivity of follicular fluid and intercellular matrix. Lectins that gave the most intense staining of the zona pellucida of both species were SBA, PNA, RCA-I, GSA-IB4 and WGA, indicating the presence of beta-D-GalNAc, D-Gal and GlcNAc residues. Sulpho- and asulpho-carbohydrates were identified in terminal and/or subterminal positions linked to sialic acid residues. In conclusion, the results indicate that glycosaminoglycans are not present in the zona pellucida of both species. Differences were observed in carbohydrate residues and in their spatial distribution, depending on species and developmental stage of the follicles. The similarity in lectin affinity between ooplasm and zona pellucida of oocytes present in follicles at different stages of development confirm the involvement of oocytes in zona pellucida production.
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PMID:Glycohistochemical investigation of canine and feline zonae pellucidae of preantral and antral oocytes. 1033 57