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)

We have asked whether treatment of normal cultured cells with proteases, other hydrolytic enzymes, or serum can convert them into transient phenocopies of transformed cells with respect to the very high rate of hexose transport characteristic of transformed cells. Treatment of density-inhibited cultures of normal chick embryo fibroblasts with trypsin, plasmin, neuraminidase, or hyaluronidase stimulated their rate of 2-deoxyglucose uptake to a level only marginally higher than that seen in normal exponentially growing cultures, and only 35-45% of that seen in transformed cultures. Addition of the hydrolytic enzymes to growing cell cultures had little effect on 2-deoxyglucose uptake. Serum, however, could stimulate 2-deoxyglucose uptake all the way up to the transformed level. Even though the hydrolases and serum differed in their ability to stimulate 2-deoxyglucose uptake, both reagents were capable of stimulating cell division equally well. Evidence is presented suggesting that the hexose transport rate is controlled by serum factors, and that proteolysis can affect the response of the cells of these factors.
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PMID:Hydrolase and serum treatment of normal chick embryo cells: effects on hexose transport. 12 53

Prolonged exposure of rats to cigarette smoke resulted in significant alteration in the metabolism of glycosaminoglycans (GAG) and glycoproteins (GP). The concentration of many GAG fractions generally decreased in the aorta, liver and heart, but increased in the lungs. Concentration of chondroitin sulphates decreased in all the tissues. The activity of many enzymes concerned with the degradation of GAG (hyaluronidase, beta-glucuronidase and cathepsin-D) showed increase in these tissues. The concentration of the carbohydrate components (total hexose fucose and sialic acid) of aorta, heart and liver showed decrease in the rats exposed to cigarette smoke while there was increase in the lungs. The activity of many glycohydrolases generally showed increase in these tissues. Thus, exposure of rats to cigarette smoke for long periods produced changes in the aortic GAG and GP which are similar to those observed in atherosclerosis. On the other hand there was accumulation of many GAG in the lung tissue.
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PMID:Changes in the glycosaminoglycans and glycoproteins in the tissues in rats exposed to cigarette smoke. 206 35

The glycosaminoglycans (GAG), glycoproteins and collagen in bovine aorta and venous tissue have been studied. The concentration of hyaluronic acid and dermatan sulphate was significantly more in the venous tissue while chondroitin sulphates were higher in the aorta. Sequential extraction with phosphate buffered saline (PBS) collagenase, hyaluronidase and urea was also carried out with the two tissues. The GAG extractable by PBS and collagenase digestion were more in the aorta. The total aortic glycoproteins had significantly lower hexose and higher sialic acid. The PBS extractable glycoproteins of the venous tissue had more hexose and fucose. The glycoproteins released by collagenase digestion of the venous tissue had lower sialic acid and higher fucose, while glycoprotein released by hyaluronidase digestion had lower sialic acid and higher hexose and fucose. Urea extractable glycoproteins had lower fucose and sialic acid in the venous tissue. Venous tissue had higher total collagen and acid and salt soluble collagen while insoluble collagen was more in the aorta. The total GAG in the venous tissue had greater anticoagulant activity while the aortic GAG bound significantly more serum lipoproteins.
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PMID:Studies on the macromolecular components of the bovine aortic and venous tissue. 309 9

Hyaluronic acid was the only glysosaminoglycan detected in the pulmonary secretions of healthy adult rats exposed to inhalation to methylene chloride, but not of control animals. The compound migrated as a single spot with the mobility of standard hyaluronic acid on cellulose acetate electrophoresis and disappeared after digestion with testicular hyaluronidase. Its identification was confirmed by finding hexuronate/hexosamine in a molar ratio of approx. 1. Glucosamine represented over 97% of the total hexosamine, the remaining 3% being galactosamine. No hexose or sulfate could be detected. Sodium dodecyl sulfate--polyacrylamide gel electrophoresis showed no protein associated with this glycosaminoglycan. It appears that the secretion of hyaluronic acid into the airways may be the result of pulmonary inflammation induced by the toxic effects of methylene chloride.
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PMID:Hyaluronic acid--an indicator of pulmonary injury? 746 58

Cone snail venoms are considered an untapped reservoir of extremely diverse peptides, named conopeptides, displaying a wide array of pharmacological activities. We report here for the first time, the presence of high molecular weight compounds that participate in the envenomation cocktail used by these marine snails. Using a combination of proteomic and transcriptomic approaches, we identified glycosyl hydrolase proteins, of the hyaluronidase type (Hyal), from the dissected and injectable venoms ("injectable venom" stands for the venom variety obtained by milking of the snails. This is in contrast to the "dissected venom", which was obtained from dissected snails by extraction of the venom glands) of a fish-hunting cone snail, Conus consors (Pionoconus clade). The major Hyal isoform, Conohyal-Cn1, is expressed as a mixture of numerous glycosylated proteins in the 50 kDa molecular mass range, as observed in 2D gel and mass spectrometry analyses. Further proteomic analysis and venom duct mRNA sequencing allowed full sequence determination. Additionally, unambiguous segment location of at least three glycosylation sites could be determined, with glycans corresponding to multiple hexose (Hex) and N-acetylhexosamine (HexNAc) moieties. With respect to other known Hyals, Conohyal-Cn1 clearly belongs to the hydrolase-type of Hyals, with strictly conserved consensus catalytic donor and positioning residues. Potent biological activity of the native Conohyals could be confirmed in degrading hyaluronic acid. A similar Hyal sequence was also found in the venom duct transcriptome of C. adamsonii (Textilia clade), implying a possible widespread recruitment of this enzyme family in fish-hunting cone snail venoms. These results provide the first detailed Hyal sequence characterized from a cone snail venom, and to a larger extent in the Mollusca phylum, thus extending our knowledge on this protein family and its evolutionary selection in marine snail venoms.
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PMID:Recruitment of glycosyl hydrolase proteins in a cone snail venomous arsenal: further insights into biomolecular features of Conus venoms. 2241