Proteoglycans synthesized by embryonic chicken retina in culture: Composition and compartmentalization

Morris, John E.; Yanagishita, Masaki; Hascall, Vincent C.

doi:10.1016/0003-9861(87)90337-7

Cited by 33 publications

(9 citation statements)

References 37 publications

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“…We found that these cells produce HS/heparin secreted into the culturing media. The retina and malignant solid tumors also produce the sulfated GAGs [1,2,22-26]. Although HSs are mostly found as proteoglycans associated with the basal lamina or the plasma membrane, the presence of HSs in the culturing medium might be a result of shedding or release of their extracellular domains from the cell membranes as soluble components.…”

Section: Discussionmentioning

confidence: 99%

Glycosaminoglycans in human retinoblastoma cells: Heparan sulfate, a modulator of the pigment epithelium-derived factor-receptor interactions

2003

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BackgroundPigment epithelium-derived factor (PEDF) has binding affinity for cell-surface receptors in retinoblastoma cells and for glycosaminoglycans. We investigated the effects of glycosaminoglycans on PEDF-receptor interactions.Results125I-PEDF formed complexes with protease-resistant components of medium conditioned by human retinoblastoma Y-79 cells. Using specific glycosaminoglycan degrading enzymes in spectrophotometric assays and PEDF-affinity chromatography, we detected heparin and heparan sulfate-like glycosaminoglycans in the Y-79 conditioned media, which had binding affinity for PEDF. The Y-79 conditioned media significantly enhanced the binding of 125I-PEDF to Y-79 cell-surface receptors. However, enzymatic and chemical depletion of sulfated glycosaminoglycans from the Y-79 cell cultures by heparitinase and chlorate treatments decreased the degree of 125I-PEDF binding to cell-surface receptors.ConclusionsThese data indicate that retinoblastoma cells secrete heparin/heparan sulfate with binding affinity for PEDF, which may be important in efficient cell-surface receptor binding.

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Section: Discussionmentioning

confidence: 99%

Glycosaminoglycans in human retinoblastoma cells: Heparan sulfate, a modulator of the pigment epithelium-derived factor-receptor interactions

2003

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“…The BMPs are also known to interact with extracellular matrices such as heparin, heparan sulfate, and collagens (Reddi, 1995; Ruppert et al, 1996; Zhu et al, 1999), which appear to modulate the biological activities of the BMPs (Ruppert et al, 1996). Some of these extracellular matrix molecules may perform similar functions in the developing retina, which contains heparin, heparan sulfate proteoglycans, and several collagen types (Newsome et al, 1976; Toole, 1982; Morris et al, 1987; Needham et al, 1988; Threlkeld et al, 1989; Linsenmayer et al, 1990; Dhawan and Beebe, 1994; McAdams and McLoon, 1995, Ring et al, 1995; Halfter et al, 1998,2000; Chai and Morris, 1999).…”

Section: Discussionmentioning

confidence: 99%

Developmental expression patterns of bone morphogenetic proteins, receptors, and binding proteins in the chick retina

Belecky-Adams

Adler

2001

J. Comp. Neurol.

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Bone morphogenetic proteins (BMPs), a large subfamily of the transforming growth factor-beta (TGF-beta) superfamily of growth factors, have been implicated in patterning of the central nervous system, but their role in the retina is much less well known. As an initial step in addressing this issue, we have investigated by in situ hybridization the expression patterns of BMP-2, -4, -5, -6, and -7, BMP receptor kinases (BRKs) -1, -2, and -3, and BMP binding proteins noggin and chordin, in the chick embryonic eye at embryonic day 3 (E3), and in isolated retinas at E6, E8, and E18. Strikingly, all mRNAs examined had spatially restricted patterns of expression in the early eye, with the receptors found primarily in the ventral portion of the retina and in the optic stalk, and the ligands and binding proteins localized to other regions of the retina and/or retinal pigment epithelium. Dorso-ventrally restricted patterns of expression persisted at E8, but were no longer apparent at E18, whereas layer-specific patterns of expression were detectable at both E8 and E18. This distribution of BMP family members, receptors, and binding proteins within the retina appears consistent with a possible role in patterning and/or differentiation of this tissue.

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“…Although the minimal level for detection varies with each method, the above change in each PG-M form with the different stages suggests differentiation-dependent transcriptional regulation for the expression of each PG-M form in retina. Morris et al (1987) demonstrated that the major chondroitin sulfate/dermatan sulfate proteoglycans in E14 chicken retinas have M. values of >400 X iO~. Because PG-M + (VU) has an Mwith a similar range (Kimata et al, 1986;Shinomura et al, 1992), proteoglycans in Ei4 chicken retinas may have corresponded to PG-M (VU), suggesting that PG-M contributes a substantial fraction of chondroitin sulfate proteoglycans in developing retinas.…”

Section: Discussionmentioning

confidence: 99%

“…Several chondroitin sulfate proteoglycans have been identified and characterized in the nervous system (for review, see Small et al, 1996) and in the retina (Morris and Ting, 1981;Aquino et al, 1984;Morris, 1984;Morris et al, 1984Morris et al, , 1987Needham et a!., 1988;Brittis et al, 1992;Ring et a!., 1995 to extracellular matrix molecules, such as fibronectin, and that the activity can be attributed to chondroitin sulfate chains (Yamagata et al, 1989). Indeed, PG-MI versican-like chondroitin sulfate proteoglycan purified from sciatic nerve inhibited adhesion of several nerve cells and affected neurite outgrowth (Braunewell et al, 1995).…”

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confidence: 99%

Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

Zako

Shinomura

Miyaishi

et al. 1997

Journal of Neurochemistry

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Abstract:We previously showed the expression of PG-M/versican in embryonic chicken retina. In this study, we characterized the alternatively spliced forms of PG-MI versican and their developmental regulation to investigate the implication of PG-Mlversican in neurite outgrowth from retinal cells during development. On day 5, the immunolocalization of PG-M was first observed at the inner surface of neural retina. On day 7, the pronounced staining was observed in the nerve fiber layer and inner plexiform layer where neural networks of ganglion cells were being formed. As the development proceeded, more intensive staining was observed in these layers. The staining peaked on day 14 and then decreased. Northern analysis and western blotting revealed the presence of a single-sized transcript (13 kb) and the PG-Mlversican core protein (550 kDa) on day 14, but the absence of any transcripts or protein bands on day 20, indicating a transient expression of PG-M + (VO), the alternatively spliced form with the most abundant sites for the chondroitin sulfate attachment. Taken together, it is likely that PG-M/versican is involved in neurite outgrowth from ganglion cells during retinal development, and antiadhesion activity of its chondroitin sulfate chains may be important for regulation. Key Words: PG-M -Versican-Chondroitin sulfate proteoglycan-Neurite outgrowth -Ganglion cell-Retinal development.

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Proteoglycans synthesized by embryonic chicken retina in culture: Composition and compartmentalization

Cited by 33 publications

References 37 publications

Glycosaminoglycans in human retinoblastoma cells: Heparan sulfate, a modulator of the pigment epithelium-derived factor-receptor interactions

Glycosaminoglycans in human retinoblastoma cells: Heparan sulfate, a modulator of the pigment epithelium-derived factor-receptor interactions

Developmental expression patterns of bone morphogenetic proteins, receptors, and binding proteins in the chick retina

Transient Expression of PG‐M/Versican, a Large Chondroitin Sulfate Proteoglycan in Developing Chicken Retina

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