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)

Localization of glucuronic acid-containing glycosaminoglycans in the gerbil utricle was examined, using a hyaluronidase-gold labeling technique with special emphasis on the otoconia. Otoconia and the gelatinous layer of the otoconial membrane were strongly labeled by hyaluronidase-gold. The secretory granules in supporting cells were also strongly labeled, suggesting that the organic matrix of otoconia is secreted from the supporting cells. Otoconia seem to lose labeling while they degenerated. The degenerating otoconia were observed to be absorbed into dark cells. Glucuronic acid-containing glycosaminoglycans occur in otoconia. These glycosaminoglycans may play a crucial role in the formation and degeneration of otoconia.
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PMID:Glucuronic acid-containing glycosaminoglycans occur in otoconia: cytochemical evidence by hyaluronidase-gold labeling. 142 47

Sulfated galactosaminoglycans of mature bovine periodontal ligament were separated into four fractions by ethanol precipitation. Fractions I and II were dermatan sulfates with high contents of L-iduronate, but only small amounts of this hexuronic acid were present in fractions III and IV. Effects of digestion with testicular hyaluronidase or a periodate-alkali treatment showed that most if not all of the glycans in fractions I, II and III were hybrid chains containing both L-iduronate and D-glucuronate. The composition of fraction IV was less certain, but the chains strongly resembled fraction III hybrids in electrophoretic characteristics, not chondroitin sulfate. The total amount of the D-glucuronate-rich fractions III and IV in the ligament was similar to that of I plus II. In contrast, almost all of the sulfated galactosaminoglycans of mature skin were rich in L-iduronate. The more varied composition of the ligament glycosaminoglycans may be related to the mixed population of cells in this tissue.
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PMID:Sulfated galactosaminoglycans of bovine periodontal ligament. Evidence for the presence of two major types of hybrids but no chondroitin sulfate. 629 47

Hyaluronan is a megadalton glycosaminoglycan composed of repeating units of D-N-acetylglucosamine-beta-D-Glucuronic acid. It is known to form a highly hydrated pericellular coat around chondrocytes, fibrosarcoma, and smooth muscle cells. Using environmental scanning electron microscopy we detected fully hydrated hyaluronan pericellular coats around rat chondrocytes (RCJ-P) and epithelial cells (A6). Hyaluronan mediates early adhesion of both chondrocytes and A6 cells to glass surfaces. We show that chondrocytes in suspension establish early "soft contacts" with the substrate through a thick, hyaluronidase-sensitive coat (4.4 +/- 0.7 microm). Freshly-attached cells drift under shear stress, leaving hyaluronan "footprints" on the surface. This suggests that chondrocytes are surrounded by a multilayer of entangled hyaluronan molecules. In contrast, A6 cells have a 2.2 +/- 0.4- microm-thick hyaluronidase-sensitive coat, do not drift under shear stress, and remain firmly anchored to the surface. We consider the possibility that in A6 cells single hyaluronan molecules, spanning the whole thickness of the pericellular coat, mediate these tight contacts.
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PMID:Organization and adhesive properties of the hyaluronan pericellular coat of chondrocytes and epithelial cells. 1294 12

The microenvironment provides a functional substratum supporting tumour growth. Hyaluronan (HA) is a major component of this structure. While the role of HA in malignancy is well-defined, the mechanisms driving its biosynthesis in cancer are poorly understood. We show that the eukaryotic translation initiation factor eIF4E, an oncoprotein, drives HA biosynthesis. eIF4E stimulates production of enzymes that synthesize the building blocks of HA, UDP-Glucuronic acid and UDP-N-Acetyl-Glucosamine, as well as hyaluronic acid synthase which forms the disaccharide chain. Strikingly, eIF4E inhibition alone repressed HA levels as effectively as directly targeting HA with hyaluronidase. Unusually, HA was retained on the surface of high-eIF4E cells, rather than being extruded into the extracellular space. Surface-associated HA was required for eIF4E's oncogenic activities suggesting that eIF4E potentiates an oncogenic HA program. These studies provide unique insights into the mechanisms driving HA production and demonstrate that an oncoprotein can co-opt HA biosynthesis to drive malignancy.
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PMID:The eukaryotic translation initiation factor eIF4E harnesses hyaluronan production to drive its malignant activity. 2911 78