Histamine and Heparin Release from Isolated Rat Mast Cells Exposed to Compound 48/80

Slorach, S. A.

doi:10.1111/j.1748-1716.1971.tb04945.x

Cited by 36 publications

(23 citation statements)

References 14 publications

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“…The extracts from 55, 82, and 200 g of human lung fragments, designated preparations 1, 2, and 3, respectively, were each applied directly to a 2 x 20-cm column of Dowex-1 equilibrated in 1 M NaCl and eluted in stepwise fashion with 1, 3, and 4 M NaCl (2,27). Portions of each fraction were assessed for 3S, protein (28), uronic acid, metachromasia, and anticoagulant activity.…”

Section: Resultsmentioning

confidence: 99%

“…The column was eluted with a logarithmic gradient from 0.1 to 1.0 M LiCl, followed by a second logarithmic gradient from 1.0 to 2.0 M LiCl (30). Fractions of 2 ml each were collected at a flow rate of [25][26][27][28][29][30] metachromasia (Fig. 4) -0.1-1.011 LiCI Grodient---.0-2.0M LiCI Grodient-FRACTION NUMBER FIGURE 4 DEAE-cellulose chromatography of human lung fragment mucopolysaccharides from preparation 3 contained in the 3 M NaCl eluate from Dowex-1 chromatography.…”

Section: Resultsmentioning

confidence: 99%

“…5B) that more than 70% was resistant to degradation by chondroitin ABC lyase, and the remainder appeared in a second peak of glycosaminoglycan degradation products. Chondroitin ABC lyase-resistant material in fractions [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30][31][32][33][34] (Fig. 5B) was pooled, dialyzed, and lyophilized.…”

Section: Resultsmentioning

confidence: 99%

“…During extraction and purification procedures heparin was estimated by change in adsorbance at 510 after formation of a heparin-azure A metachromatic complex with commercial porcine heparin as a standard (18,19). It required [25][26][27][28][29][30] (21).…”

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Isolation and Characterization of Heparin from Human Lung

Metcalfe¹,

Lewis²,

Silbert³

et al. 1979

J. Clin. Invest.

148

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A B S T R A C T Heparin as measured by azure A metachromasia and anticoagulant activity has been extracted with 1 M NaCl from 35S-labeled human lung fragments or dispersed human lung cells enriched for mast cells. The 35S-labeled metachromatic material in the 3 M NaCl eluate from Dowex-1 chromatography of the extract from lung fragments exhibited an average mol wt of 20,000 by Sepharose 4B gel filtration. The 35S-labeled metachromatic material with the charge characteristics of commercial porcine heparin on DEAE cellulose chromatography was entirely heparin by the criteria of resistance to degradation by chondroitin ABC lyase and complete degradation by purified heparinase. Antithrombin affinity chromatography of purified heparin with an anticoagulant activity of 137 U/mg, revealed that the one-third that was bound and eluted had a 273 U/mg sp act, whereas the unbound activity was 31 U/mg. Thus, the previously observed heterogeneity of commercial porcine heparin for binding to human antithrombin was also observed with human heparin. The mast cell-enriched human lung cell preparations yielded [35S]mucopolysaccharides with an average mol wt of 60,000 by Sepharose 4B gel filtration. Approximately

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Isolation and Characterization of Heparin from Human Lung

Metcalfe¹,

Lewis²,

Silbert³

et al. 1979

J. Clin. Invest.

148

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“…There Preparationi of glyco.saminoglycans. Purified rat peritoneal mast cells (RPMC) were frozen and thawed six times and extracted wvith 1 M NaCl; the extract was chromatographed on a Dowex 1-x2 column (10,11). The fractions containing heparin proteoglyean, as assessed by metachromasia (12) and assay of uronic acid content (13), were eluted with 3 M NaCl, dialyzed and lyophilized.…”

Section: Introductionmentioning

confidence: 99%

Structural Determinants of the Capacity of Heparin to Inhibit the Formation of the Human Amplification C3 Convertase

Kazatchkine¹,

Fearon²,

Metcalfe³

et al. 1981

J. Clin. Invest.

152

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A B S T R A C T The ability of heparin glycosaminoglycan to prevent formation ofthe properdin-stabilized amplification C3 convertase is independent of antithrombin binding activity and requires substitution of the amino sugar and a degree of oxygen (0)-sulfation which could be on the uronic acid or the amino sugar. Preparations of heparin glycosaminoglycan isolated by different techniques from different species (rat, human, and porcine) exhibited an equivalent capacity to inhibit generation ofthe amplification C3 convertase. Hyaluronic acid, which is devoid of 0-sulfation, had no inhibitory activity; chondroitin 4-sulfate of rat and whale origins, chondroitin 6-sulfate of rat and shark origins, and dermatan sulfate from porcine skin are 0-sulfated on the galactosamine and had minimal activity. Porcine heparin glycosaminoglycan, isolated on the basis of affinity for antithrombin III, had no greater anticomplementary activity than porcine glycosaminoglycan, which failed to bind antithrombin III and had essentially no anticoagulant activity. Nitrogen (N)-desulfation of porcine heparin reduced anticomplementary activity to the level of the other sulfated mucopolysaccharides, and both N-resulfation and N-acetylation restored the original activities, thereby indicating a requirement for N-substitution, but not N-sulfation. N-resulfation of N-desulfated and 0-desulfated heparin did not restore any activity, thus indicating that 0-sulfation and N-substitution represent independent, critical structural requirements for the anticomplementary activity of heparin glycosaminoglycan.

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