Biomaterial Database

Morphogenesis of the retinal pigment epithelium: toward understanding retinal degenerative diseases. 1998

A D Marmorstein, and S C Finnemann, and V L Bonilha, and E Rodriguez-Boulan

Margaret Dyson Vision Research Institute, Department of Ophthalmology, Cornell University Medical College, New York, New York 10021, USA.

The phenotype of an epithelial cell is defined by a unique combination of morphology, gene and protein expression, and protein localization. Results indicate that the terminal differentiation of the RPE cell can be described in part by changes in the polarity of its surface proteins alpha v beta 5 integrin, Na,K-ATPase, N-CAM, and EMMPRIN. Changes in protein/gene expression and protein localization in late stages of RPE development identify alpha v beta 5 integrin as a key player in RPE phagocytosis, and N-CAM and EMMPRIN as potentially important molecules in other RPE functions necessary for photoreceptor survival. By studying the trafficking of the later two proteins it is shown that entry into an apical or basolateral pathway in RPE cells cannot be predicted by the distribution of a given protein in other epithelial cells, and that this distribution may change through the course of RPE development. The mechanisms used by RPE and other epithelia to establish and maintain their specific polarity properties are fundamental to the formation and maintenance of their specific epithelial phenotype. The ability to therapeutically direct molecules incorporated into RPE by gene therapy into apical or basal surfaces requires an understanding of protein localization and expression. Furthermore, evidence is provided that assays capitalizing on changes in gene/protein expression and protein localization during the late stages of RPE development can prove a productive way of identifying proteins used by RPE for photoreceptor support. This approach can continue to be exploited to identify other proteins essential for the mission of the RPE cell, that may thus be likely candidates for participation in retinal degenerative disease.

UI	MeSH Term	Description	Entries
D008562	Membrane Glycoproteins	Glycoproteins found on the membrane or surface of cells.	Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D009024	Morphogenesis	The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
D010857	Pigment Epithelium of Eye	The layer of pigment-containing epithelial cells in the RETINA; the CILIARY BODY; and the IRIS in the eye.	Eye Pigment Epithelium
D012162	Retinal Degeneration	A retrogressive pathological change in the retina, focal or generalized, caused by genetic defects, inflammation, trauma, vascular disease, or aging. Degeneration affecting predominantly the macula lutea of the retina is MACULAR DEGENERATION. (Newell, Ophthalmology: Principles and Concepts, 7th ed, p304)	Degeneration, Retinal,Degenerations, Retinal,Retinal Degenerations
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000254	Sodium-Potassium-Exchanging ATPase	An enzyme that catalyzes the active transport system of sodium and potassium ions across the cell wall. Sodium and potassium ions are closely coupled with membrane ATPase which undergoes phosphorylation and dephosphorylation, thereby providing energy for transport of these ions against concentration gradients.	ATPase, Sodium, Potassium,Adenosinetriphosphatase, Sodium, Potassium,Na(+)-K(+)-Exchanging ATPase,Na(+)-K(+)-Transporting ATPase,Potassium Pump,Sodium Pump,Sodium, Potassium ATPase,Sodium, Potassium Adenosinetriphosphatase,Sodium-Potassium Pump,Adenosine Triphosphatase, Sodium, Potassium,Na(+) K(+)-Transporting ATPase,Sodium, Potassium Adenosine Triphosphatase,ATPase Sodium, Potassium,ATPase, Sodium-Potassium-Exchanging,Adenosinetriphosphatase Sodium, Potassium,Pump, Potassium,Pump, Sodium,Pump, Sodium-Potassium,Sodium Potassium Exchanging ATPase,Sodium Potassium Pump
D000375	Aging	The gradual irreversible changes in structure and function of an organism that occur as a result of the passage of time.	Senescence,Aging, Biological,Biological Aging
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000951	Antigens, Neoplasm	Proteins, glycoprotein, or lipoprotein moieties on surfaces of tumor cells that are usually identified by monoclonal antibodies. Many of these are of either embryonic or viral origin.	Neoplasm Antigens,Tumor Antigen,Tumor Antigens,Antigen, Tumor,Antigens, Tumor
D015316	Genetic Therapy	Techniques and strategies which include the use of coding sequences and other conventional or radical means to transform or modify cells for the purpose of treating or reversing disease conditions.	Gene Therapy,Somatic Gene Therapy,DNA Therapy,Gene Therapy, Somatic,Genetic Therapy, Gametic,Genetic Therapy, Somatic,Therapy, DNA,Therapy, Gene,Therapy, Somatic Gene,Gametic Genetic Therapies,Gametic Genetic Therapy,Genetic Therapies,Genetic Therapies, Gametic,Genetic Therapies, Somatic,Somatic Genetic Therapies,Somatic Genetic Therapy,Therapies, Gametic Genetic,Therapies, Genetic,Therapies, Somatic Genetic,Therapy, Gametic Genetic,Therapy, Genetic,Therapy, Somatic Genetic