Retina cognin, cell signaling, and neuronal differentiation in the developing retina

Hausman, Robert E.; Rao, A. T.; Ren, Yi; Sagar, Gunisha; Shah, Bukhtiar H.

doi:10.1002/aja.1001960407

Cited by 9 publications

(3 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Of these, perhaps the most noteworthy is the cell-adhesion protein retina cognin [121], a 50 kDa retinaspecific protein which is probably a truncated version of PDI lacking the a domain and the C-terminal KDEL tetrapeptide [122,123]. This protein is involved in cell recognition and neuronal differentiation of the embryonic retina, and the exported protein has been observed to enhance specific aggregation of retina cells.…”

Section: Different Localizations Of Pdimentioning

confidence: 99%

The protein disulphide-isomerase family: unravelling a string of folds

Ferrari

Söling

1999

Biochemical Journal

404

359

View full text Add to dashboard Cite

show abstract

Section: Different Localizations Of Pdimentioning

confidence: 99%

The protein disulphide-isomerase family: unravelling a string of folds

Ferrari

Söling

1999

Biochemical Journal

404

359

View full text Add to dashboard Cite

show abstract

“…The interactive and pleiotropic nature of signaling molecules is particularly significant in view of the abundance and diversity of such molecules in the retina (e.g., Campochiaro et al, 1996; Hallbook et al, 1996; Schoen and Chader, 1997; Hicks, 1998; Belecky‐Adams et al, 1999; Frade et al, 1999; Belecky‐Adams and Adler, 2001; Carri, 2003; Yang, 2004). Retinal cell differentiation, moreover, can be influenced not only by secreted molecules but also by contact‐mediated interactions (Linser and Moscona et al, 1984; Moscona et al, 1988; Hausman et al, 1993; Henrique et al, 1997; Layer et al, 1998; Prada et al, 1998; Becker and Mobbs, 1999). Not surprisingly, therefore, a picture of high complexity has emerged since the development of techniques and reagents for loss‐ and gain‐of‐function experiments made it possible to investigate the role of extracellular signals not only in cell culture, but also within the complexity of the intact embryo.…”

Section: Role Of Extracellular Signals In the Regulation Of Neuronal mentioning

confidence: 99%

Challenges in the study of neuronal differentiation: A view from the embryonic eye

Adler

2005

Developmental Dynamics

View full text Add to dashboard Cite

Progress in the study of the molecular mechanisms that regulate neuronal differentiation has been quite impressive in recent years, and promises to continue to an equally fast pace. This should not lead us into a sense of complacency, however, because there are still significant barriers that cannot be overcome by simply conducting the same type of experiments that we have been performing thus far. This article will describe some of these challenges, while highlighting the conceptual and methodological breakthroughs that will be necessary to overcome them. Developmental Dynamics 234:454 -463, 2005.

show abstract

“…There have been several reports on the possible extracellular localization of PDI in some cell types, despite the integrity of the KDEL signal [118][119][120]. Of these, perhaps the most noteworthy is the cell-adhesion protein retina cognin [121], a 50 kDa retinaspecific protein which is probably a truncated version of PDI lacking the a domain and the C-terminal KDEL tetrapeptide [122,123]. This protein is involved in cell recognition and neuronal differentiation of the embryonic retina, and the exported protein has been observed to enhance specific aggregation of retina cells.…”

Section: Different Localizations Of Pdimentioning

confidence: 99%

The protein disulphide-isomerase family: unravelling a string of folds

1999

View full text Add to dashboard Cite

The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins, including peptide binding, cell adhesion and perhaps chaperone activities. Attention is now turning to the non-redox-active domains of the PDIs, which may play an important role in all of the known activities of these proteins. Thus the presence of both redox-active and -inactive domains within these proteins portends a complexity of functions differentially accommodated by the various family members.

show abstract

Retina cognin, cell signaling, and neuronal differentiation in the developing retina

Cited by 9 publications

References 31 publications

The protein disulphide-isomerase family: unravelling a string of folds

The protein disulphide-isomerase family: unravelling a string of folds

Challenges in the study of neuronal differentiation: A view from the embryonic eye

The protein disulphide-isomerase family: unravelling a string of folds

Contact Info

Product

Resources

About