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

Zako, Masaru; Shinomura, Tamayuki; Miyaishi, Osamu; Iwaki, Masaya; Kimata, Koji

doi:10.1046/j.1471-4159.1997.69052155.x

Cited by 28 publications

(14 citation statements)

References 37 publications

(34 reference statements)

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“…In the eye, MY-174 specifically stains the photoreceptor layer (1). However, recently we demonstrated an absence of PG-M/versican at the chick photoreceptor layer using a polyclonal antibody that recognizes all alternatively spliced forms of PG-M/versican (5). These inconsistent results suggest that MY-174 does not recognize PG-M/versican but another molecule in the photoreceptor layer.…”

mentioning

confidence: 80%

Molecular Cloning and Characterization of Chick Sialoprotein Associated with Cones and Rods, a Developmentally Regulated Glycoprotein of Interphotoreceptor Matrix

Zako¹,

Iwaki²,

Yoneda³

et al. 2002

Journal of Biological Chemistry

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MY-174 is an IgM class monoclonal antibody originally established against chick PG-M/versican. The antibody specifically stains the photoreceptor layer, where we recently reported an absence of PG-M/versican. In this study, we re-characterized the antibody and identified the molecule that reacts to MY-174 at the photoreceptor layer. Immunohistochemistry localized the antigen to the matrix surrounding photoreceptors. A variety of glycosidase digestions showed that the antigen is the 150-kDa glycoprotein that has sialylated N-and O-linked glycoconjugates having a molecular mass of more than 30-kDa. The peptide sequences obtained from purified MY-174 antigen showed we had sequenced a full-length cDNA with an open reading frame of 2787 base pairs, encoding a polypeptide of 928 amino acids, with 56 and 54% identities to human and mouse sialoprotein associated with cones and rods (SPACRs), respectively, and with the structural features observed in SPACRs. The specific sialylated O-glycoconjugates here are involved in the epitope structure for MY-174. SPACR first appeared by embryonic days 15-16, and expression increased with developmental age, paralleling the adhesion between neural retina and retinal pigment epithelium. Thus, we concluded that the MY-174 antigen at the photoreceptor layer, a developmentally regulated glycoprotein, is identical to chick SPACR and may be involved in a novel system mediating adhesion between neural retina and retinal pigment epithelium.MY-174, a monoclonal antibody, has been shown to recognize chick PG-M/versican (1), a member of the hyaluronan-binding chondroitin sulfate proteoglycan family (2-4). In the eye, MY-174 specifically stains the photoreceptor layer (1). However, recently we demonstrated an absence of PG-M/versican at the chick photoreceptor layer using a polyclonal antibody that recognizes all alternatively spliced forms of PG-M/versican (5). These inconsistent results suggest that MY-174 does not recognize PG-M/versican but another molecule in the photoreceptor layer.The IPM (interphotoreceptor matrix), 1 resides in an extracellular compartment between the outer limiting membrane of the neural retina and apical surface of the retinal pigment epithelium and is composed of proteins, glycoproteins, proteoglycans, and glycosaminoglycans (6, 7). A variety of important reactions relating to vision, including visual pigment chromophore exchange, metabolite trafficking, photoreceptor alignment, and membrane turnover, is thought to be mediated by the IPM (8). However, one of the most essential functions of IPM is that of a biological glue for retinal adhesion through its viscous adhesive properties (9, 10). Retinal adhesiveness can be weakened by treatments with enzymes such as neuraminidase, hyaluronidase, and chondroitinase ABC (11,12). Intracellular blocking of glycosylation with xyloside also prevents the secretion of proteoglycans and results in retinal detachment (13). These results suggest that the proteoglycans, glycosaminoglycans, or glycoproteins of the IPM are involved in...

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confidence: 80%

Molecular Cloning and Characterization of Chick Sialoprotein Associated with Cones and Rods, a Developmentally Regulated Glycoprotein of Interphotoreceptor Matrix

Zako¹,

Iwaki²,

Yoneda³

et al. 2002

Journal of Biological Chemistry

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“…There are few reports on distribution of CSPGs in the retina and optic nerve [18,31,45]. In this study, we estimated the presence and distribution of C4S, C6S, aggrecan and biglycan in addition to keratan sulfate.…”

Section: Discussionmentioning

confidence: 98%

Spatiotemporal Distribution of Chondroitin Sulfate Proteoglycans in the Developing Mouse Retina and Optic Nerve

Ali

Hosaka

Uehara

2011

The Journal of Veterinary Medical Science

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ABSTRACT. The aim of the present study was to determine the distribution of chondroitin sulfate proteoglycans in the mouse retina and optic nerve of the prenatal and postnatal mouse by immunohistochemistry. At embryonic day (E) 18, chondroitin-4-sulfate (C4S), chondroitin-6-sulfate (C6S) and biglycan were detected in the retina and optic nerve. However, aggrecan was seen in the retina but not in the optic nerve. At postnatal day (P) 7, aggrecan and biglycan were clearly observed in the optic nerve, inner nuclear layer and ganglion cell layer and diffuse in the outer retina. C4S diffusely distributed in the retina and optic nerve, but C6S was mainly confined to the photoreceptor layer and optic nerve sheath. At P42, biglycan showed diffuse distribution in the retina and optic nerve with intense staining in nerve-fiber rich layers. Aggrecan showed weak staining at the inner plexiform layer with higher density in the outer and inner nuclear layers, outer plexiform layer and ganglion cell layer. Both C4S and C6S were detected in the optic nerve and retina, but C6S showed strong immunostaining in the photoreceptor layer. The distributions of these proteoglycans with respect of time course during development of the retina and optic nerve suggest that they may have unique or overlapping roles in development and maintenance of the retina and optic nerve.KEY WORDS: chondroitin sulfate proteoglycan, development, optic nerve, retina, spatiotemporal distribution.

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“…With further retinal development at the early larval stage, the d1C4-positive regions could be identified as inner and outer plexiform layers. Chondroitin sulfate proteoglycans have been localized to plexiform layers during development of the eye in both chick (Zako et al, 1997;Li et al, 2000) and rat (Inatani et al, 2000). It has been proposed that these proteoglycans function in regulation of neurite outgrowth and cellular organization within the retina.…”

Section: Discussionmentioning

confidence: 99%

Heterogeneity of chondroitin sulfate glycosaminoglycan localization during early development of the striped bass (Morone saxatilis)

et al. 2002

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Recent studies have suggested important functions for proteoglycanassociated chondroitin sulfate glycosaminoglycans (GAGs) during embryonic and larval development in numerous organisms, including the teleost. Little is known, however, about the specific distribution of different chondroitin sulfate GAGs during early development. The present study utilized immunohistochemistry to localize chondroitin sulfate GAG antigens during development of the striped bass (Morone saxatilis). Immunoreagents utilized were monoclonal antibodies (MAbs) TC2, d1C4, and CS-56, which recognize, respectively, native epitopes on glycosaminoglycan chains enriched in chondroitin-4-, chondroitin-6-, and both chondroitin-4-and -6-sulfate. Little or no immunoreactivity was observed in gastrulating embryos at 18 hr postfertilization with any MAb tested. By 24 hr (8 somites), the CS-56 epitope was localized around the notochord. At hatching (48 hr) and early larval (72 hr) stages, d1C4 and CS-56 antigens codistributed in some sites (e.g., the notochord and myosepta), but a striking heterogeneity of chondroitin sulfate GAG localization was observed in other developing tissues, including the eye and specific subsets of basement membrane. At these latter time points, TC2 reacted primarily with the extracellular matrix of the developing heart, particularly the ventricular and conotruncal segments. Heterogeneous patterning of these chondroitin sulfate GAG epitopes suggests dynamic regulation of proteoglycan function during critical morphogenetic events in early development of the striped bass. Anat

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

Cited by 28 publications

References 37 publications

Molecular Cloning and Characterization of Chick Sialoprotein Associated with Cones and Rods, a Developmentally Regulated Glycoprotein of Interphotoreceptor Matrix

Molecular Cloning and Characterization of Chick Sialoprotein Associated with Cones and Rods, a Developmentally Regulated Glycoprotein of Interphotoreceptor Matrix

Spatiotemporal Distribution of Chondroitin Sulfate Proteoglycans in the Developing Mouse Retina and Optic Nerve

Heterogeneity of chondroitin sulfate glycosaminoglycan localization during early development of the striped bass (Morone saxatilis)

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