Structure and Biosynthesis of Basement Membranes

Kefalides, Nicholas A.

doi:10.1016/b978-0-12-363706-2.50008-8

Cited by 494 publications

(210 citation statements)

References 80 publications

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“…Sialyl residues have been found in all three layers of the capillary wall. They have been detected in isolated glomerular basement membranes (GBM) (8)(9)(10) and in association with the cell membranes of both the endothelium (11)(12) and epithelium (4)(5)(6)(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.…”

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confidence: 99%

“…Heparan sulfate has been found, however, in association with the cell surfaces of various different cell types (34), including vascular endothelia (35). The question arises as to why GAG have not been detected heretofore in the GBM either by biochemical assays (8)(9)(10) or by histochemical staining procedures (4-7, 11-12). As far as the negative biochemical results are concerned, the explanation may lie in the fact that previous analyses for uronic acid (8,9) or sulfate groups (8) have been done on isolated GBM prepared by sonication, which, according to our experience, disrupts the anionic sites or, if prolonged, removes them entirely.…”

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“…The question arises as to why GAG have not been detected heretofore in the GBM either by biochemical assays (8)(9)(10) or by histochemical staining procedures (4-7, 11-12). As far as the negative biochemical results are concerned, the explanation may lie in the fact that previous analyses for uronic acid (8,9) or sulfate groups (8) have been done on isolated GBM prepared by sonication, which, according to our experience, disrupts the anionic sites or, if prolonged, removes them entirely. Previous histochemical studies had the disadvantage that they were done on fixed sections (4)(5)(6)(7)(11)(12) incubated in basic dyes (with and without prior enzyme digestion).…”

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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.

495

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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Presence of heparan sulfate in the glomerular basement membrane

Kanwar

Farquhar

1979

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

495

191

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“…Biochemical analyses have established that basement membranes possess a highly cross-linked form of collagen (5), rendering basement membranes completely insoluble under physiological conditions. Although most biochemical studies of basement membranes have dealt with the structure and synthesis of collagen, noncollagenous matrix glycoproteins have also been found in some basement membranes (6).…”

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Identification, localization, and role of fibronectin in cultured bovine endothelial cells.

Birdwell¹,

Gospodarowicz²,

Nicolson³

1978

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

235

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We have examined bovine aortic endothelial cell cultures for the presence of fibronectin, a high molecular weight cell-surface glycoprotein. Sparse cultures contain fibronectin only on dorsal cell surfaces at regions of cell-cell contact, as detected by immunofluorescence. In contrast, when the endothelial cells reached confluence as a highly contactinhibited monolayer, fibronectin was detected in an extracellular matrix underneath the cell monolayer but not on top of the monolayer. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis of isolated extracellular matrix revealed that a predominant component of the matrix is a protein of approximately 2.3 X 105 molecular weight,.which has been identified as fibronectin.The vascular endothelium exists as a monolayer of highly flattened and contact-inhibited cells; because of their location at the interface between blood and tissue, endothelial cells are the chief elements involved in the permeability of blood vessels (1, 2). Although the side of the vascular endothelium exposed to the bloodstream is nonthrombogenic, the subendothelial matrix on which the cells rest is very thrombogenic (3,4). Thus, a disruption of the vascular endothelium can expose the underlying basement membrane, resulting.in the aggregation of platelets and thrombus formation. Therefore, factors that are involved in the attachment of endothelial cells to the basement membrane are very important for the proper functioning of the vascular endothelium.Biochemical analyses have established that basement membranes possess a highly cross-linked form of collagen (5), rendering basement membranes completely insoluble under physiological conditions. Although most biochemical studies of basement membranes have dealt with the structure and synthesis of collagen, noncollagenous matrix glycoproteins have also been found in some basement membranes (6). Recent studies indicate that one of these glycoproteins may be identical to fibronectin (7), a major cell-surface glycoprotein that is immunologically identical to cold-insoluble globulin (8), a plasma protein which is presumably the plasma form of fibronectin that is shed from cells into the blood. Fibronectin appears to be similar, if not identical, to the large external transformationsensitive (LETS) protein, which exists on the surface of certain untransformed cells, but not on the surface of transformed cells (9)(10)(11) (21), and we also show that fibronectin is a major component of the extracellular matrix produced by ABAE cells. METHODSCell Culture. The cloning, culturing, and characterization of ABAE cells have been described (21). ABAE cells are identified as endothelial cells on the basis of their morphology and ultrastructure and on their ability to synthesize Factor VIII (antihemophilic factor antigen), a marker for endothelial cells (22). These cells are routinely maintained in fibroblast growth factor (23).Electron Microscopy. Cells were prepared for electron microscopy by described methods (24), and then examined in a Hitachi S-500 ...

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“…carbohydrate moiety has been located at neuromuscular junctions (Sanes and Cheney, 1982a1, but the carbohydrate-rich al(1V) and a2(IV) chains (Kefalides, 1973) are often weakly expressed there. Hence, if this carbohydrate is part of collagen type IV, it is more likely associated with the a3(IV) and a4(IV) chains.…”

Section: Muscle Spindlesmentioning

confidence: 99%

Basal lamina development in chicken muscle spindles

Maier

Mayne

1995

Developmental Dynamics

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The development of basal laminas was examined in immunohistochemical sections of chicken leg muscle spindles from embryonic day (E) 13 to 8 weeks postnatal. Fragments of basal laminas as seen with immunostaining for isoforms of laminin were already observed in E6 muscles. When clusters of intrafusal myotubes were first recognized at E13-14, they were surrounded by basal laminas which were incomplete both in terms of coverage and molecular composition. More mature basal lamina tubes individually enclosed young myofibers at E18. After afferents made contact with myotubes, synaptic portions of basal laminas at myosensory junctions reacted strongly with antibodies against s-laminin and chondroitin sulfate proteoglycan, while extrasynaptic portions were negative or reacted only weakly. At synaptic basal laminas of neuromuscular junctions heparin sulfate proteoglycan and s-laminin became prominent after E16. Contrary to the early presence of basal lamina proteins around intrafusal fibers, initial deposition of basal lamina proteins in the outer spindle capsule was not recognized until E17-18, and significant amounts were not detected until postnatal week 1. Unlike intrafusal basal laminas, capsular basal laminas developed no distinct specialized regions; however, molecular compositions of intrafusal and capsular basal laminas were similar. 0 1995 Wiley-Liss, Inc.

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Structure and Biosynthesis of Basement Membranes

Cited by 494 publications

References 80 publications

Presence of heparan sulfate in the glomerular basement membrane

Presence of heparan sulfate in the glomerular basement membrane

Identification, localization, and role of fibronectin in cultured bovine endothelial cells.

Basal lamina development in chicken muscle spindles

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