Cross-linking of fibronectin to sulfated proteoglycans at the cell surface

Perkins, Margaret; Ji, Tae H.; Hynest, Richard O.

doi:10.1016/0092-8674(79)90109-0

Cited by 222 publications

(78 citation statements)

References 26 publications

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“…In addition, the binding of fibronectin to collagen is enhanced by glycosaminoglycans, and the complexes formed by these interactions are insoluble (36)(37)(38). Also, fibronectin crosslinks to sulfated proteoglycans on cell surfaces (39) and thrombospondin interacts with fibronectin (40). It is thus likely that thrombospondin may interact with these components on the cell surface or extracellular matrix.…”

Section: Discussionmentioning

confidence: 99%

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

Jaffe¹,

Ruggiero²,

Leung³

et al. 1983

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

253

125

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Thrombospondin, a major glycoprotein released from a granules of thrombin-stimulated platelets, is a disulfidebonded trimer of 160-kilodalton subunits. Cultured human foreskin and fetal lung fibroblasts secreted thrombospondin (determined by enzyme-linked immunosorbent assay) into the culture medium in a time-dependent manner (15.7 and 5.8 Thrombospondin is a major platelet a granule glycoprotein that is secreted and then partially bound to platelet membranes when human platelets aggregate in response to thrombin (1)(2)(3)(4)(5)(6)(7)(8). Thrombospondin is a 450-kilodalton (kDal) protein and is composed of three large disulfide-linked subunits (9, 10). During platelet aggregation, thrombin-stimulated platelets develop a membrane-bound lectin-like activity (11-13), which originates from a granules and appears to play a role in mediating platelet aggregation by binding to a specific receptor on other platelets (14,15 3.7 X 10'°Bq). The radioactive postculture medium was removed, centrifuged at 8,000 x g for 2 min to remove cells and debris, and frozen at -35°C. The radioactive cell layers were washed twice, removed with a rubber policeman, pelleted by centrifugation, dissolved by boiling for 5 min in 2% NaDodSO4 containing protease inhibitors as described (20), and frozen until analyzed.In experiments in which the accumulation of thrombospondin antigen was measured by enzyme-linked immunosorbent assay (ELISA), fibroblasts were cultured in minimal essential medium containing 20% rabbit serum in 2-cm2 wells of multiwell plates. When the cells were confluent, the cells were washed, and the medium was replaced with 1 ml of fresh minimal essential medium containing 20% rabbit serum. At various times after the medium change, the postculture medium was removed, centrifuged at 8,000 X g for 2 min, and frozen until assayed. 998The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Section: Discussionmentioning

confidence: 99%

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

Jaffe¹,

Ruggiero²,

Leung³

et al. 1983

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

253

125

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“…tured mass of proteoglycans similar to the type II collagen network in native cartilage matrix . Cross-linking studies of Perkins et al (23) indicated an interaction between sulfated proteoglycans and fibronectin on the cell surface of fibroblasts .…”

Section: Discussionmentioning

confidence: 99%

Extracellular matrix formation by chondrocytes in monolayer culture.

Dessau¹,

Vertel²,

Mark³

et al. 1981

The Journal of Cell Biology

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In previous studies were have reported on the secretion and extracellular deposition of type II collagen and fibronectin (Dessau et al., 1978, J. Cell Biol., 79:342-355) and chondroitin sulfate proteoglycan (CSPG) (Vertel and Dorfman, 1979, Proc. Natl. Acad. Sci. U. S. A. 76:1261-1264) in chondrocyte cultures. This study describes a combined effort to compare sequence and pattern of secretion and deposition of all three macromolecules in the same chondrocyte culture experiment. By immunofluorescence labeling experiments, we demonstrate that type II collagen, fibronectin, and CSPG reappear on the cell surface after enzymatic release of chondrocytes from embryonic chick cartilage but develop different patterns in the pericellular matrix. When chondrocytes spread on the culture dish, CSPG is deposited in the extracellular space as an amorphous mass and fibronectin forms fine, intercellular strands, whereas type II collagen disappears from the chondrocyte surface and remains absent from the extracellular space in early cultures. Only after cells in the center of chondrocyte colonies shape reassume spherical shape does the immunofluorescence reveal type II collagen in the refractile matrix characteristic of differentiated cartilage. By immunofluorescence double staining of the newly formed cartilage matrix, we demonstrate that CSPG spreads farther out into the extracellular space that type II collagen. Fibronectin finally disappears from the cartilage matrix.

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“…Dulbecco's modified Eagle's medium (DME), Roswell Park Memorial Institute (RPMI)-1640, Dulbecco's phosphate-buffered saline (DBPS), penicillin/ streptomycin sulfate, and trypsin-EDTA were purchased from Flow Laboratories (McLean, VA). lodo-1- 14 C-acetic acid ( H-cholesterol (40 to 60 Ci/mmol), 4-14 C-cholesterol (50 to 60 mCi/mmol), iodine-125 (17 Ci/mg, carrier-free), and Aquasol were obtained from New England Nuclear (Boston, MA). Gelatin-Sepharose 4B, DEAE-Sephacel, heparinSepharose CL-6B, and Sephadex G-200 (Superfine) were obtained from Pharmacia Fine Chemicals (Piscataway, NJ).…”

Section: Methodsmentioning

confidence: 99%

“…1 Following Cm, 14 C-Cm-Fn was applied to a heparin-Sepharose column equilibrated with 50 mM Tris acetate (pH 7.0) containing 1.0 mM PMSF and 0.02% sodium azide. Unbound, labeled Fn was washed from the column and discarded.…”

Section: Isolation Of Plasma Flbronectlnmentioning

confidence: 99%

Fibronectin stimulates macrophage uptake of low density lipoprotein-heparin-collagen complexes.

Falcone

Salisbury

1988

Arteriosclerosis

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In this study, we Investigated whether fibronectin will enhance macrophage uptake of participate complexes of low density llpoprotelns (LDL), heparln, and fibrlllar collagen and whether flbronectln's opsonlc effect could be modulated by the heparln component In these model matrices. We Isolated a heparln fraction (Hep Fn ) based on Its affinity to fibronectin. Hep,= n appeared more charged than unfractionated heparln, as evidenced by enhanced electrophoretlc mobility and ability to effect a cathodlc shift in the electrophoretlc migration of fibronectin.

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Cross-linking of fibronectin to sulfated proteoglycans at the cell surface

Cited by 222 publications

References 26 publications

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.

Extracellular matrix formation by chondrocytes in monolayer culture.

Fibronectin stimulates macrophage uptake of low density lipoprotein-heparin-collagen complexes.

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