Bearing Fatigue Life Tests in a Synthetic Traction Lubricant

Culp, D. V.; Stover, J. D.

doi:10.1080/05698197608982800

Cited by 6 publications

(7 citation statements)

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“…FN is known to bind to collagen (8) and to be closely associated with sulfated proteoglycans at the surface of cultured cells (7,30) . Evidence has also been presented which suggests that FN-heparan sulfate complexes are involved in cell-tosubstate adhesion (7) .…”

Section: Discussionmentioning

confidence: 99%

Fibronectin localization in the rat glomerulus.

Courtoy¹,

Kanwar²,

Hynes³

et al. 1980

The Journal of Cell Biology

160

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Fibronectin (FN) has been localized in the rat glomerulus using indirect immunolabeling . It was demonstrated in frozen sections by immunofluorescence, in sections of fixed kidneys by both peroxidase and ferritin-labeled antibodies, and in isolated glomerular basement membranes (GBM) with ferritin-labeled antibodies . Complementary and convergent results were obtained with these approaches . FN was most abundant in the mesangial matrix where it was especially concentrated at the interface between the endothelial and mesangial cells. In the peripheral capillary loop, FN was also detected in the laminae rarae (interna and externa) of the GBM -i.e ., between the endothelial and epithelial cells, respectively, and the GBM. These findings indicate that FN is an important constituent of the glomerulus, and they are compatible with the assumption that, in the glomerulus, as in cultured cells, FN is involved in cell-to-cell (mesangial-mesangial, mesangial-endothelial) and cell-to-substrate (mesangial cellmesangial matrix, epithelium-GBM, endothelium-GBM) attachment .Fibronectin (FN) (22) is a glycoprotein associated with fibrillar elements on the cell surface (11) and in the extracellular matrix (3,14, 33) which is involved in cell-to-cell and cell-to-substrate attachment (36). A similar, immunologically indistinguishable protein known as cold-insoluble globulin (CIG) (37), or plasma fibronectin, is found circulating in the blood .FN appears to be a major connective tissue protein, widely distributed in normal tissues (34). A close alignment or codistribution has been noted between extracellular fibronectin and intracellular actin (15, 33), and the possibility of a transmembrane linkage between the two has been proposed (15). Thus, a complex network' involving actin, FN, and probably other components (e.g., proteoglycans [7, 301) has been envisaged which connects adjacent cells, mediates cell anchorage to the extracellular matrix, and transmits deformation generated by the contractile cells. Because the glomerulus is under a high and variable hydrostatic pressure, it seemed possible that such a network may operate to maintain glomerular integrity and to regulate its blood flow (28). By immunofluorescence, FN has already been localized in the mesangium of newborn (24), adult (5,29, 31, 32,34,38), or diseased glomeruli (25, 31, 32) . By electron microscopy, a prominent fibrillar material is observed in the mesangial matrix (MM) (9), the nature of which is unknown. Some investigators described immunoreactivity for fibronectin (5,29, 31, 32) in the peripheral regions of the capillary loops, whereas others reported that it was absent (25,34,38) . In these regions, an extensive fibrillar network is also ' This network has been referred to as a "fibronexus" (33) .THE JOURNAL OF CELL BIOLOGY " VOLUME 87 DECEMBER 1980 691-696 ©The Rockefeller University Press " 0021-9525/80/12/0691/06 $1 .00 observed in the laminae rarae of the glomerular basement membrane (GBM), which appears to anchor the epithelial and endothelial...

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Section: Discussionmentioning

confidence: 99%

Fibronectin localization in the rat glomerulus.

Courtoy¹,

Kanwar²,

Hynes³

et al. 1980

The Journal of Cell Biology

160

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“…A large I0 peak appears in the cell profile. When Platt cultures were serum-starved, Io remained in the cell fraction, unlike the serum-starved BI04 cells which contain I0 in their SAM (10).…”

Section: A Teriamentioning

confidence: 89%

“…B104 rat neuroblastoma cells and their behavioral variants ERAI l and ERB9 were grown and subeultured as previously described (10,13). The human neuroblastoma line, Platt, was grown in Dulbccco's modified Eagles medium (DME) with 10% fetal calf serum (FCS), 10 mM HEPES buffer, 250 U/ml peniciUin, 250/~g/ml streptomycin at 37°C in a 10% CO2-humidified air mixture.…”

Section: Ceils and Growth Conditionsmentioning

confidence: 99%

“…2A and Table I). The appearance of Io in the cell fraction but not the SAM fraction of ERB9 cells raised the possibility that the appearance of Io in the SAM of B 104 neurite-positive cells (10) was the result of serum starvation. To test this, serum-sensitive BI04 cells were grown in the chemically defined, serum-free I0 is tabulated as the percentage it comprises of the total polysaccharide containing material in a given sample.…”

Section: Ceils and Growth Conditionsmentioning

confidence: 99%

“…In an earlier study, biochemical analysis of neuroblastoma SAM showed the appearance of a high molecular weight glycoconjugate in SAM from neurite-producing ("differentiated") B 104 rat neuroblastoma cells (10). This material was designated Io in the analysis scheme and has never been observed in glial ceils, muscle cells, or a variety of fibroblastlike cells (11).…”

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confidence: 99%

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Isolation and characterization of a large, neurite-associated glycoconjugate from neuroblastoma cells

Chernoff¹,

Maresh²,

La³

1983

The Journal of Cell Biology

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A high molecular weight glycoconjugate has been isolated from neurite-producing neuronal tumor cells in culture and has been designated as Io based on its elution characteristics in gel filtration chromatography. This molecule cannot be found in a variety of nonneuronal cells. Io is found in the substratum-attached material or cell fraction of neurite-producing neuroblastoma cells, depending upon culture conditions. It is found in the substratum-bound fraction of B104 rat neuroblastoma cells during serum starvation and in the EGTA-detached cell fraction of B104 cells grown in chemically defined N2 medium. It occurs only in the cell fraction of the human neuroblastoma line Platt. Examination of behavioral variants of the 8104 rat line further strengthens the association of Io with neurite production; the constitutive neurite-producing ERB9 variant contains Io while the non-neurite-producing ERA11 variant does not. Io is large, eluting in the void volume of Sepharose-CL2B columns. Radioiodination of intact cells with lactoperoxidase shows 10 to be a cell surface component. Metabolic radiolabeling studies show that it contains a high proportion of polysaccharide to protein, does not contain mannose, and is unsulfated. Alkaline borohydride reduction releases two size classes of large polysaccharide chains. The alkaline reduction results, along with the mannose incorporation studies, show the presence of O-glycosidic linkages and few, if any, N-linkages. Resistance to nitrous acid deamination, insensitivity to glycosaminoglycan lyases, and the absence of sulfation, indicate that 10 does not contain the glycosaminoglycans hyaluronic acid, chondroitin-, dermatan-, or heparan-sulfates. Affinity column chromatography reveals high binding affinity of Io to polyornithine and no binding to gelatin (collagen) or the glycosaminoglycans hyaluronate and heparin. These studies describe a unique high molecular weight glycoconjugate on the surface of neurite-producing neuroblastoma cell lines from two species.Several approaches have been used to examine mechanisms in neuronal cells underlying growth cone adhesion and neurite outgrowth. The effects of physical/chemical properties of the tissue culture substratum on strength of adhesion and rate of neurite outgrowth were initially explored by Letourneau (1). Substrata coated with polycationic polypeptides, especially polyornithine (PORN) and polylysine, were found to optimize growth cone adhesion and neurite outgrowth from embryonic sensory ganglia. A complementary approach has involved a search for factors from cells or their environment that stimulate neuronal differentiation. Studies using embryonic ciliary ganglia have shown the existence of substances in extracts of target tissues (2, 3), conditioned medium from heart cultures (4, 5) and a variety of other tissues (6) that stimulate neurite outgrowth. These substances are active only when bound to PORN-coated substrata (designated PORN-bound neurite-1~4[: /OURN,~L OF CEtL 8fOLOGY-VOtUME 96 MARCH 1983 661-668

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