Role of the cell recognition molecule, cognin, in GABAergic differentiation in chick retina

Shah, Bukhtiar H.; Rao, A. T.; Hausman, Robert E.

doi:10.1016/0006-8993(92)91286-n

Cited by 10 publications

(4 citation statements)

References 40 publications

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“…Grunwald et al [1997] (this issue) demonstrate that developmental downregulation of N-cadherin is correlated with phosphorylation of this molecule by tyrosine kinases. Other recent studies in vertebrate retina have implicated adhesion molecules in retinal patterning and cell fate determination [e.g., Hunter et al, 1992;Shah et al, 1992;Bradshaw et al, 1995], and the formation of electrical connections [e.g., Kljavin et al, 1994;Balsamo et al, 1995]. Adhesion molecules have also recently been implicated in fly retinal morphogenesis.…”

Section: Uniting Developmental Mechanisms In Vertebrates and Fliesmentioning

confidence: 98%

Perspectives on eye development

Fini¹,

Strissel²,

West‐Mays³

1997

Dev. Genet.

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Section: Uniting Developmental Mechanisms In Vertebrates and Fliesmentioning

confidence: 98%

Perspectives on eye development

Fini¹,

Strissel²,

West‐Mays³

1997

Dev. Genet.

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“…The apparent homology of R-cognin with MFP raises questions about the mechanisms by which R-cognin mediates histotypic adhesion (1) and neuronal differentiation (34,37) of retina cells. R-cognin does not bind to itself but can be crosslinked to a 64-kDa protein (8).…”

Section: Discussionmentioning

confidence: 99%

“…In addition to the role of R-cognin in mediating retina cell-cell adhesion (8,9), there is evidence that interference with R-cognin perturbs expression of both cholinergic and y-aminobutyratergic differentiation in retina neurons (34,37).…”

Section: Discussionmentioning

confidence: 99%

cDNA for R-cognin: homology with a multifunctional protein.

Rao

Hausman²

1993

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

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Retina cognin (R-cognin) is a developmentally regulated 50-kDa protein that was isolated from chicken embryo retina cell membranes. It mediates the adhesion and reaggregation in vitro of retina cells from chicken and mouse embryos, but not of cells from other tissues, and may be involved in neuronal differentiation. We report here the cloning of a cDNA for R-cognin. A chicken embryo retina cDNA library was constructed in Agtll vector and was screened with polyclonal R-cognin antiserum, yielding several immunoreactive clones. Antiserum prepared to the R-cognin-galactosidase fusion protein produced by one recombinant lysogen recognized the 50-kDa R-cognin protein derived from retina cell membranes. This antiserum inhibited the reaggregation of dissociated retina cells and immunostalned chicken embryo retina tissue in a pattern similar to that obtained with R-cognin antiserum. In vit translation of RNA from a cDNA subclone yielded a 50-kDa protein that was recognized by R-cognin antiserum on a Western blot. By these criteria we identify the cDNA clone as representative of the gene encoding R-cognin.This cDNA is nearly identical to a major portion of the cDNA for the multifunctionail protein that is the ,B subunit of prolyl 4-hydroxylase and has both protein disulde isomerase activity and thyroid hormone-binding activity. These rmdings demonstrate that R-cognin differs from other cell adhesion molecules and suggest possible mechanisms for its action in cell adhesion and neuronal differentiation.Following the discovery of the retina celi recognition and adhesion molecule R-cognin (1-4), numerous cell adhesion molecules have been identified in the nervous system (5, 6) and implicated in cell aggregation, attachment, and migration and in neurite outgrowth and differentiation. R-cognin is a 50-kDa protein isolated from chicken embryo retina cell membranes (2). When R-cognin is added to suspensions of trypsin-dissociated embryonic retina cells, it binds to the cell surface (7), possibly to a 64-kDa protein (8), and enhances cell-cell aggregation. It has no similar effect on dissociated cells from other tissues (7). In the chicken embryo retina, R-cognin is initially expressed on the surface of virtually all the cells; as development progresses it becomes limited to the ganglion cell layer (9-11). In the mature retina, R-cognin is no longer detected on the cell surfaces (11).The role of R-cognin in cell recognition/adhesion and its suggested involvement in cell interactions and neuronal differentiation in the retina (1, 4, 9, 12) led us to investigate its molecular characteristics. We previously reported the construction and screening of a Agtll expression library with antiserum to R-cognin (13 from New England Nuclear. The bacterial strains E. coli Y1088 (r-, ml), Y1089 and Y1090 (r+, m+), and XL1-Blue (r-, m+) were obtained from Stratagene.Library Construction and Screening. RNA was isolated from chicken 8-day embryonic retinal tissue as described by Davis et al. (16), and poly(A)+ RNA was selected by oligo(dT)-...

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“…The activity in specific regions indicates no difference between the chick retina, optic lobe and cerebellum, at least from E9 onwards (Gonzales et al, 1990). Cultures of embryonic retinal cells from the chick also exhibit GAD activity (de Mello, 1984;Shah et al, 1992). The functional implication of early GAD activity and possible GABA accumulation is unclear, although it has been suggested that GABA has a trophic effect rather than an inhibitory transmitter function (Spoem and Wolff, 198 1;Cherubini et al, 1991;Antal et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Two Glutamate Decarboxylase Forms Corresponding to the Mammalian GAD₆₅ and GAD₆₇ are Expressed During Development of the Chick Telencephalon

Åhman

Wågberg

Mattsson

1996

Eur J of Neuroscience

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The gamma-aminobutyric acid (GABA)-synthesizing enzyme glutamate decarboxylase (GAD) was studied during development of the chick telencephalon. By means of reverse-phase HPLC analysis, we showed that GABA indeed accumulates during embryogenesis, whereas the levels of glutamate, the substrate for GAD, are more or less unchanged up to later developmental stages. The enzyme activity increased approximately 25-fold from embryonic day 3 to embryonic day 17. Immunoblotting data revealed that two GAD proteins, of approximately 65 and 67 kDa, were present during the period investigated. Furthermore, Northern blot analysis with probes obtained from rat cDNA sequences, as well as a chicken-specific probe for GAD65 generated by means of reverse transcriptase-polymerase chain reaction (RT-PCR), strengthened the interpretation that the chick embryo expresses genes corresponding to GAD65 and GAD67. The rat probes recognized transcript sizes of 3.9 kb (GAD65) and 5.6 kb (GAD67), sizes which are different from those of the rat brain (Erlander et al., Neuron, 7, 91-100, 1991). Sequencing of the RT-PCR products revealed a high level of homology (82% at the nucleotide level) between the mammalian and chick GAD65 genes. Taken together, these findings suggest that the chick embryo expresses two GAD genes during embryogenesis. The functional properties of each gene product remain to be investigated.

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Role of the cell recognition molecule, cognin, in GABAergic differentiation in chick retina

Cited by 10 publications

References 40 publications

Perspectives on eye development

Perspectives on eye development

cDNA for R-cognin: homology with a multifunctional protein.

Two Glutamate Decarboxylase Forms Corresponding to the Mammalian GAD₆₅ and GAD₆₇ are Expressed During Development of the Chick Telencephalon

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Role of the cell recognition molecule, cognin, in GABAergic differentiation in chick retina

Cited by 10 publications

References 40 publications

Perspectives on eye development

Perspectives on eye development

cDNA for R-cognin: homology with a multifunctional protein.

Two Glutamate Decarboxylase Forms Corresponding to the Mammalian GAD65 and GAD67 are Expressed During Development of the Chick Telencephalon

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Two Glutamate Decarboxylase Forms Corresponding to the Mammalian GAD₆₅ and GAD₆₇ are Expressed During Development of the Chick Telencephalon