Metabolism of Polysaccharides Containing Glucuronic Acid

Silbert, Jeremiah E.

doi:10.1016/b978-0-12-395501-2.50012-8

Cited by 7 publications

(3 citation statements)

References 540 publications

(235 reference statements)

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“…Testicular hyaluronidase is also capable of degrading chondroitin sulphate and dermatan sulphate, so it is unclear why this enzyme has so little effect. One reason may be that the larger fragments (octasaccharides; Silbert, 1966) remaining after hyaluronidase digestion still contribute to the integrity of the barrier.…”

Section: Discussionmentioning

confidence: 99%

Effect of enzyme digestion on the permeability barrier in keratinizing and non-keratinizing epithelia

Squier

1984

Br J Dermatol

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In an attempt to characterize the permeability barrier of the oral mucosa and skin, small pieces of keratinized and non-keratinized oral epithelia and epidermis were digested with specific enzymes. These enzymes were selected for their effect on carbohydrate-protein, or carbohydrate-lipid compounds and phospholipids. The effect of the enzyme treatment was monitored by exposing the digested tissue to horseradish peroxidase. Electron microscopic examination of tissue treated with phospholipases revealed considerable damage to membrane structures but not to the integrity of the permeability barrier. Hyaluronidase and neuraminidase caused less structural damage but did not impair barrier function; this was only seen after treatment with chondroitinase ABC. This enzyme may degrade certain of the polar molecules thought to be necessary to stabilize the neutral lipid bilayers of the intercellular barrier and thus disrupt its barrier properties.

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Section: Discussionmentioning

confidence: 99%

Effect of enzyme digestion on the permeability barrier in keratinizing and non-keratinizing epithelia

Squier

1984

Br J Dermatol

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“…On the other hand it was inactivated by treatment with polysaccharide-splitting enzymes. Whereas testicular hyaluronidase, chondroitinase ABC and AC, and streptococcal hyaluronidase are all capable of degrading more than one species of polysaccharide, including HA, the leech hyaluronidase is known to affect HA only (see Silbert, 1966). The inactivation of CAF by this latter enzyme therefore strongly suggests that HA is essential for the cell-aggregation activity.…”

Section: Figurementioning

confidence: 99%

Aggregation of feline lymphoma cells by hyaluronic acid

Wasteson

Westermark

Lindahl

et al. 1973

Intl Journal of Cancer

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Addition of media from cultured human sarcoma or glioma cells to cultures of suspended feline lymphoma cells [established line FL 74) induced visible aggregationCells in vivo show complex and specific interactions which inter alia keep them arranged in organs and tissues of fixed composition and topography. Such interactions may be reproduced in vitro, where cells will often organize nonrandomly to form aggregates of similar cells with the exclusion of unlike elements (histiotypic aggregation; see e.g. Oppenheimer and Humphreys, 1971;Moscona, 1971). The nature of the aggregating factors is largely unknown.The present report is concerned with a different kind of aggregating phenomenon, expressed by a single cell type (cat lymphoma) in response to a factor produced by a number of non-related cells. The aggregation factor has been identified as hyaluronic acid (HA), suggesting a hitherto unrecognized biological function for this polysaccharide. These results confirm and extend those of Pessac and Defendi (1972), who observed a similar phenomenon in a murine system. MATERIAL AND METHODS Cell lines and culture conditionsThe derivation of the cell lines employed appears in Table I. The lymphoid cell lines were cultivated in Erlenmeyer flasks as non-stirred semi-suspension cultures, with cell aggregates located on the bottom of the flasks. The sarcoma,

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“…Enzymes degrading glycosaminoglycans have been extensively reviewed [7,12,15,22,23,29]. Meyer et al [22] wotdd not accept a subgroup of chondroitinases since all these enzymes would actively degrade hyaluronic acid.…”

Section: Introductionmentioning

confidence: 99%

The Substrate Specificity of the Glycosaminoglycuronoglycan Degrading Enzymes of Human Serum

Ml¹

1971

Enzyme

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A method is described for the assay of glycosaminoglycuronoglycan degrading activity in serum. Normal human serum was shown to have a hy aluronidase active at pH 3.7 on hyaluronic acid, chondroitin-4-sulphate and variably on chondroitin-6-sulphate, but with no activity towards dermatan sulphate. A second enzyme was demonstrated at pH 7.0, actively degrading dermatan sulphate and chondroitin-4-sulphate but with little effect on either chondroitin-6-sulphate or hyaluronic acid.

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Metabolism of Polysaccharides Containing Glucuronic Acid

Cited by 7 publications

References 540 publications

Effect of enzyme digestion on the permeability barrier in keratinizing and non-keratinizing epithelia

Effect of enzyme digestion on the permeability barrier in keratinizing and non-keratinizing epithelia

Aggregation of feline lymphoma cells by hyaluronic acid

The Substrate Specificity of the Glycosaminoglycuronoglycan Degrading Enzymes of Human Serum

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