ZIB

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Cystic Fibrosis Transmembrane Conductance Regulator Is Found Within Brain Ventricular Epithelium and Choroid Plexus (1995)

Hincke, M. T. ; Nairn, A. C. ; Staines, W. A.

Oxford, UK : Blackwell Science Ltd

Journal of neurochemistry 64 (1995), S. 0

add to mindlist on the mindlist

Details

ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Abstract: The cystic fibrosis gene product, cystic fibrosis transmembrane conductance regulator (CFTR), functions as a CI− channel that is regulated by cyclic AMP-dependent phosphorylation. We have investigated the expression of CFTR protein in the rodent brain by both western blotting of samples prepared by microdissection and immunohistochemistry. CFTR was found to be expressed in choroid plexus and ependyma. In tissue sections, CFTR-like immunoreactivity was concentrated in fine puncta localized about 1–2 µm from the CSF-contacting side of ependyma and choroid plexus. CFTR in choroid plexus may play a role in the regulation of the composition of CSF by cyclic AMP-elevating agents, but the role of this chloride transporter in ependymal function remains to be determined.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1046/j.1471-4159.1995.64041662.x

Permalink

Library	Location	Call Number	Volume/Issue/Year	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Purification and immunochemistry of a soluble matrix protein of the chicken eggshell (ovocleidin 17) (1995)

Hincke, M. T. ; Tsang, C. P. W. ; Courtney, M. ; [et al.]

Springer

Calcified tissue international 56 (1995), S. 578-583

add to mindlist on the mindlist

Details

ISSN: 1432-0827

Keywords: Eggshell ; Shell matrix ; Biomineralization

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine , Physics

Notes: Abstract The protein components of biomineralized structures (matrix proteins) are believed to modulate crystal nucleation and growth, and theraby influence the shape and strength of the final structure. The chicken eggshell contains a complex array of distinct matrix proteins. The most abundant of these was purified to homogeneity by a combination of anionic exchange and hydroxyapatite chromatographies. Antibodies to this protein were raised in rabbit, and utilized for Western blotting and immunohistochemistry. These studies indicated that the 17 kDa antigen (ovocleidin 17, OC-17) is found in the shell gland mucosa, and that only the tubular gland cells were positive. Immunohistochemistry with decalcified shell indicated that OC-17 is uniformly distributed throughout the shell matrix, but concentrated in the mammillary bodies. Our results indicate that this protein is secreted during shell formation and becomes incorporated into this structure. It may therefore play a role in the crystallization process and influence the properties of the resulting eggshell.