Glycosaminoglycan Synthesis by Embryonic Inductors: Neural Tube, Notochord, and Lens

Hay, Elizabeth D.; Meier, Stephen

doi:10.1083/jcb.62.3.889

Cited by 194 publications

(72 citation statements)

References 17 publications

(26 reference statements)

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“…The finding that the sites are destroyed by Pronase together with the fact that GAG do not normally occur extracellularly as free polymers (31,32) At the time of the original description of the anionic sites in the GBM it was pointed out (13) that these sites could consist of the carboxyl groups of the collagenous or noncollagenous peptides, sialyl groups of glycoproteins, or sulfated groups of GAG. The first two had been found in isolated GBM, whereas the latter had not been detected, but the presence of GAG has been recorded in basement membranes in other locations (28)(29)(30). In later experiments in which the sites were stained with ruthenium red, it was noted (16) that the GBM sites and their interconnecting filaments bear a striking resemblance to proteoglycan particles found in other connective tissue matrices (33) or in association with other basement membranes (28)(29)(30).…”

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confidence: 91%

“…The first two had been found in isolated GBM, whereas the latter had not been detected, but the presence of GAG has been recorded in basement membranes in other locations (28)(29)(30). In later experiments in which the sites were stained with ruthenium red, it was noted (16) that the GBM sites and their interconnecting filaments bear a striking resemblance to proteoglycan particles found in other connective tissue matrices (33) or in association with other basement membranes (28)(29)(30).…”

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confidence: 91%

“…2a) or testicular and leech hyaluronidase (not shown) at concentrations 4-5 times higher than those used in the past to degrade GAG in the extracellular matrices of several fixed tissues (28)(29)(30). Bladder fluid collected after perfusion with these three enzymes degraded the appropriate GAG substrate, indicating that these enzymes passed through the filter and were active during transit across the glomerular capillary.…”

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confidence: 99%

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Presence of heparan sulfate in the glomerular basement membrane

Kanwar

Farquhar

1979

Proc. Natl. Acad. Sci. U.S.A.

494

191

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The glomerular basement membrane was subjected to digestion with specific enzymes to determine the chemical nature (sialoglycoproteins, collagenous peptides, or glycosaminoglycans) of the anionic sites previously demonstrated in the laminae rarae. Enzyme digestion was carried out both in situ and in vitro. Kidneys were perfused in situ with enzyme solutions followed by perfusion with fixative containing the cationic dye, ruthenium red, to detect the anionic sites. Glomerular basement membranes were isolated by detergent treatment of glomeruli and incubated with enzyme solutions, followed by incubation with cationized ferritin (pI 7.3-7.5 Physiologic studies have established that the glomerular capillaries function as a size-and charge-selective barrier in the production of the glomerular filtrate and in the retention of plasma proteins in the circulation (1-3). By inference it has been assumed (1-3) that charge selectivity is due to the presence in the glomerulus of fixed negative charges, but their precise nature and location in the capillary wall have not been established. Since macromolecular compounds carrying sialic acid residues have been-up to recently-the only known polyanions present in the glomerulus, they have been considered the most likely candidates responsible for the charge barrier (1, 2, 4-7). Sialyl residues have been found in all three layers of the capillary wall. They have been detected in isolated glomerular basement membranes (GBM) (8-10) and in association with the cell membranes of both the endothelium (11-12) and epithelium (4-7, 11), where they are part of the sialic acid-rich, cell-surface coats. A colloidal iron-stainable, cell-coat material is particularly concentrated on the epithelium. Accordingly, it has been repeatedly suggested (1, 2, 4-7) that this "epithelial polyanion" is responsible for establishing the charge-selective properties of the glomerular filter, and, concomitantly, that its loss leads to proteinuria since loss of epithelial cell-coat staining occurs in several renal diseases (1, 2, 5). Materials. Ruthenium red was purchased from Ventron Corp. (Danvers, MA); horse-spleen ferritin (2X crystallized, cadmium free) from Calbiochem; and chondroitin sulfates (types A, B, and C) and heparin (grade I) from Sigma. Chondroitinase ABC (Proteus vulgaris) was obtained from Miles; testicular hyaluronidase from Sigma; leech hyaluronidase from Biotrics, Inc. (Boston, MA); neuraminidase (Clostridium perfringens, NEUA) from Worthington; collagenase form III (Cl. histolyticum) from Advance Biofactures (Lynbrook, NY); and Pronase (Streptomyces griseus, grade B) from Calbiochem. Crude heparinase and purified heparitinase (Flavobacterium heparinium) were the generous gift of Alfred Linker (17).* Neuraminidase and heparitinase were tested by the Azocoll assay (18) and were free of proteolytic activity. Cationized ferritin was prepared as described previously (16).Perfusion Experiments. The left kidney was exposed and perfused as described (16). Initially, the kidney was flush...

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confidence: 91%

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confidence: 91%

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Presence of heparan sulfate in the glomerular basement membrane

Kanwar

Farquhar

1979

Proc. Natl. Acad. Sci. U.S.A.

494

191

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“…Sulfated GAG's are readily extracted from tissues by the usual fixation and dehydration methods; however, they can be retained in connective tissue when cationic dyes or reagents (such as cetyl pyridinium chloride [29], RR [28], alcian blue [1,47], or safranin O [44]) are added to the fixative. RR has been shown to bind to, to precipitate and to stain GAG's in a variety of connective tissues (15,16,34,48,50), where they occur as proteoglycan particles (20=50 nm in diameter) often closely associated with collagen fibrils (16,34,47,48,50).…”

Section: Nature Of the Anionic Sites In The Gbmmentioning

confidence: 99%

“…cles consisting in part of chondroitin sulfate have been identified (based on RR staining and enzyme digestion) in association with basement membranes in a number of other locations-i.e., the embryonic cornea (48), various other embryonic tissues (15,16) and smooth muscle cells in the aorta (50). Sulfated GAG's are readily extracted from tissues by the usual fixation and dehydration methods; however, they can be retained in connective tissue when cationic dyes or reagents (such as cetyl pyridinium chloride [29], RR [28], alcian blue [1,47], or safranin O [44]) are added to the fixative.…”

Section: Nature Of the Anionic Sites In The Gbmmentioning

confidence: 99%

Anionic sites in the glomerular basement membrane. In vivo and in vitro localization to the laminae rarae by cationic probes.

Kanwar

Farquhar

1979

The Journal of Cell Biology

508

200

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Cationized ferritin (CF) of narrow pI range (7.3-7.5) and the basic dye ruthenium red (RR) have been used as cationic probes to partially characterize anionic sites previously demonstrated in the glomerular basement membrane (GBM). When CF was given i.v. to normal rats and the left kidney was fixed by perfusion 15 min thereafter, clusters of CF molecules were found throughout the lamina rara interna (LRI), lamina rara externa (LRE), and mesangial matrix distributed at regular (-60 nm) intervals. When kidneys were perfused with aldehyde fixative containing RR, small (20 nm) RR-stained particles were seen in the same locations distributed with the same 60 nm repeating pattern, forming a quasiregular, lattice-like arrangement. Fine (-3 nm) filaments connected the sites and extended between them and the membranes of adjoining endothelial and epithelial cells 9 When CF was given i.v. followed by perfusion with RR in situ, both probes localized to the same sites 9 CF remained firmly bound after prolonged perfusion with 0.1-0 9 M KCI or NaCI. It was displaced by perfusion with buffers of high ionic strength (0 9149 M KCI) or pH (<3.0 or >10.0). CF also bound (clustered at -60 nm intervals) to isolated GBM's, and binding was lost when such isolated GBM's were treated with buffers of high ionic strength or pH. These experiments demonstrate the existence of a quasi-regular, lattice-like network of anionic sites in the LRI and LRE and the mesangial matrix 9 The sites are demonstrable in vivo (by CF binding), in fixed kidneys (by RR staining), and in isolated GBM's (by CF binding). The results obtained with CF show that the binding of CF (and probably also RR) to the laminae rarae is electrostatic in nature since it is displaced by treatment with buffers of high ionic strength or pH. With RR the sites resemble in morphology and staining properties the proteoglycan particles found in connective tissue matrices and in association with basement membranes in several other locations 9 KEY WORDS cationized ferritin red proteoglycans 9 ionic interaction isolated GBM's 9 ruthenium Recent studies have shown that the glomerular capillary wall contains fixed negatively charged sites which may be important in maintaining nor- J. CELL BIOLOGY 9The Rockefeller University Press 9

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