scholarly journals Mice Expressing Myc in Neural Precursors Develop Choroid Plexus and Ciliary Body Tumors

2018 ◽  
Vol 188 (6) ◽  
pp. 1334-1344 ◽  
Author(s):  
Morgan L. Shannon ◽  
Ryann M. Fame ◽  
Kevin F. Chau ◽  
Neil Dani ◽  
Monica L. Calicchio ◽  
...  
Keyword(s):  
Choroid Plexus ◽  
Ciliary Body ◽  
Neural Precursors

scholarly journals INFOLDED BASAL PLASMA MEMBRANES FOUND IN EPITHELIA NOTED FOR THEIR WATER TRANSPORT

1956 ◽  
Vol 2 (4) ◽  
pp. 203-208 ◽  
Author(s):  
Daniel C. Pease
Keyword(s):  
Choroid Plexus ◽  
Water Transport ◽  
Ciliary Body ◽  
Plasma Membranes ◽  
Cell Layer ◽  
Submaxillary Gland ◽  
Basal Surface ◽  
Basal Plasma ◽  
Marked Tendency ◽  
Secretory Ducts

Epithelia noted for their water transport have been studied by electron microscopy with particular emphasis upon basal specializations. Epithelia of the submaxillary gland, choroid plexus, and ciliary body are described in this article, and compared with previous observations on the kidney. The basal surface of all these epithelia is tremendously expanded by folds which penetrate deeply into the cytoplasm. In the submaxillary gland this is particularly notable in cells of the serous alveoli and in the secretory ducts. In these instances the folds have a fairly regular distribution and have a marked tendency to turn back upon themselves and so form repeating S-shaped patterns. In the choroid plexus the penetrating basal folds are limited to the lateral regions of each ependymal cell where they blend with the intercellular membranes that are also folded. In the epithelium of the ciliary body it is the inner layer that is specialized. The surface adjacent to the cavity of the eye penetrates irregularly, nearly through the full depth of the cell layer. The exposed surface is, in a fundamental sense, the basal surface of this epithelial layer. It is apparent that the pattern of folding is quite distinctive in the different epithelia. Therefore, the specializations should be regarded as analogous rather than homologous. Topographic considerations presumably limit the manner in which basal cell surfaces might be expanded. Penetrating folds would seem to represent almost the only possible solution.

Extrarenal tissue distribution of CHIP28 water channels by in situ hybridization and antibody staining

1994 ◽  
Vol 266 (4) ◽  
pp. C893-C903 ◽  
Author(s):  
H. Hasegawa ◽  
S. C. Lian ◽  
W. E. Finkbeiner ◽  
A. S. Verkman
Keyword(s):  
In Situ Hybridization ◽  
Epithelial Cells ◽  
Tissue Distribution ◽  
Choroid Plexus ◽  
Ciliary Body ◽  
Fluid Transport ◽  
Pancreatic Acini ◽  
Antibody Staining ◽  
Strong Hybridization

This study is an extension of in situ hybridization experiments showing expression of mRNA encoding CHIP28 in selected epithelial or endothelia in spleen, colon, lung, and eye (H. Hasegawa, R. Zhang, A. Dohrman, and A. S. Verkman. Am. J. Physiol. 264 (Cell Physiol. 33): C237-C245, 1993). Additional tissues from rat were screened by in situ hybridization, and tissues from rat and humans were stained with a polyclonal anti-CHIP28 antibody. Northern blot showed the 2.8-kilobase mRNA encoding CHIP28 in kidney, lung, and heart. In situ hybridization showed strong hybridization in epithelial cells in choroid plexus, iris, ciliary body, and lens and in epithelial and subepithelial layers of trachea. Except for colonic crypts, specific hybridization was not observed in the gastrointestinal tract, liver, thyroid gland, and muscle. Immunoblot of tissues from exsanguinated rats showed immunoreactive CHIP28 protein in kidney, lung, trachea, and heart. In fixed frozen rat and/or human tissues, the anti-CHIP28 antibody stained epithelial cells in kidney proximal tubule and thin limb of Henle, lung alveolus, bronchial mucosa and glands, choroid plexus, ciliary body, iris, lens surface, colonic crypt, sweat gland, pancreatic acini, gallbladder epithelium, and placental syncytial trophoblast cells. Endothelial cells were stained in many tissues. These studies indicate a wide and selective CHIP28 tissue distribution, suggesting an important role for CHIP28 in fluid transport. The absence of CHIP28 in many nonrenal membranes believed to be water permeable suggests the existence of non-CHIP28 water transporters.

scholarly journals Organ distribution in rats of two members of the low-density lipoprotein receptor gene family, gp330 and LRP/alpha 2MR, and the receptor-associated protein (RAP).

1994 ◽  
Vol 42 (4) ◽  
pp. 531-542 ◽  
Author(s):  
G Zheng ◽  
D R Bachinsky ◽  
I Stamenkovic ◽  
D K Strickland ◽  
D Brown ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cell Surface ◽  
Choroid Plexus ◽  
Ciliary Body ◽  
Organ Distribution ◽  
Surface Binding ◽  
Homologous Proteins ◽  
Cortical Cells ◽  
Receptor Associated Protein ◽  
Adrenal Cortical Cells

We investigated immunohistochemically the distribution in rats of the homologous proteins gp330 and the LDL receptor-related protein (LRP/alpha 2MR), and a receptor-associated protein (RAP), and the sites to which soluble exogenous RAP binds. We found gp330 in a restricted group of epithelial cells, including renal proximal tubule cells, podocytes, Type II pneumocytes, cells of the parathyroid, thyroid, epididymis, lining of the uterus, ependyma, retina, ciliary body, yolk sac, and placenta. In these cells gp330 was detected mainly at the cell surface, except for parathyroid and retinal epithelial cells, where diffuse cell staining was found. LRP/alpha 2MR was widely distributed in interstitial cells, notably in fibroblasts and macrophages, and was also present in a selected group of epithelial or specialized cells, including hepatocytes, adrenal cortical cells, follicular cells of the ovary, cells of the choroid plexus, ciliary body, mesangial cells, and some neurons. In certain cells, notably hepatocytes and adrenal cortical cells, LRP/alpha 2MR was detected mainly on the surface, but in others, including macrophages, fibroblasts, and epithelial cells of the choroid plexus and ciliary body, staining throughout the cell was seen. The only cells that clearly expressed both LRP/alpha 2MR and gp330 were retinal and ciliary epithelial cells. RAP was found in intracellular vesicles in all cells that expressed gp330 or LRP/alpha 2MR. RAP was not definitely detected on the cell surface. Binding sites for RAP were found on the surface of those cells with surface gp330 or LRP, and also throughout the cytoplasm in cells with diffuse cellular LRP/alpha 2MR or gp330. Because of their different locations, we conclude that gp330 and LRP/alpha 2MR serve distinct functions in vivo, despite similarities in ligand-binding properties observed in vitro. Since RAP is found largely within cells, its major physiological function may be concerned with intracellular assembly or trafficking of the receptors to which it binds.

scholarly journals Gene expression-based comparison of the human secretory neuroepithelia of the brain choroid plexus and the ocular ciliary body: potential implications for glaucoma

2014 ◽  
Vol 11 (1) ◽  
pp. 2 ◽  
Author(s):  
Sarah F Janssen ◽  
Theo GMF Gorgels ◽  
Jacoline B ten Brink ◽  
Nomdo M Jansonius ◽  
Arthur AB Bergen
Keyword(s):  
Gene Expression ◽  
Choroid Plexus ◽  
Ciliary Body ◽  
Body Potential ◽  
The Brain

Organization of tight junctions in the choroid plexus epithelium

1978 ◽  
Vol 36 (2) ◽  
pp. 336-337
Author(s):  
B. Van Deurs ◽  
J. K. Koehler
Keyword(s):  
Choroid Plexus ◽  
Present Report ◽  
Freeze Fracture ◽  
Barrier Properties ◽  
Cell Junctions ◽  
Structural Basis ◽  
Apical Surface ◽  
Choroid Plexus Epithelium ◽  
Solid Nitrogen ◽  
Special Composition

The choroid plexus epithelium constitutes a blood-cerebrospinal fluid (CSF) barrier, and is involved in regulation of the special composition of the CSF. The epithelium is provided with an ouabain-sensitive Na/K-pump located at the apical surface, actively pumping ions into the CSF. The choroid plexus epithelium has been described as “leaky” with a low transepithelial resistance, and a passive transepithelial flux following a paracellular route (intercellular spaces and cell junctions) also takes place. The present report describes the structural basis for these “barrier” properties of the choroid plexus epithelium as revealed by freeze fracture.Choroid plexus from the lateral, third and fourth ventricles of rats were used. The tissue was fixed in glutaraldehyde and stored in 30% glycerol. Freezing was performed either in liquid nitrogen-cooled Freon 22, or directly in a mixture of liquid and solid nitrogen prepared in a special vacuum chamber. The latter method was always used, and considered necessary, when preparations of complementary (double) replicas were made.

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