Nonradioactive In Situ Hybridization of RNA Probes to Sections of Plant Tissues

2008 ◽  
Vol 2008 (3) ◽  
pp. pdb.prot4943-pdb.prot4943 ◽  
Author(s):  
C. Ferrandiz ◽  
A. Sessions
1992 ◽  
Vol 67 (2) ◽  
pp. 59-67 ◽  
Author(s):  
N. Arnold ◽  
R. Seibl ◽  
C. Kessler ◽  
J. Wienberg

2000 ◽  
Vol 48 (4) ◽  
pp. 499-507 ◽  
Author(s):  
Huguette Louis ◽  
Julie Lavie ◽  
Patrick Lacolley ◽  
Danièle Daret ◽  
Jacques Bonnet ◽  
...  

Because tissue freeze-drying is an excellent way to preserve antigenic conformation, we have tested the feasibility of this technique to reveal nonradioactive in situ hybridization (ISH) of tissue mRNA. We have compared mRNA detection after different methods of tissue preservation, freeze-drying, cryosectioning, and formaldehyde or methanol fixation. Our results show that nonradioactive ISH is more sensitive for tissues preserved by freeze-drying than for other tissue preparations. We have demonstrated that freeze-drying allows combination of ISH and immunohistochemistry for simultaneous detection of mRNA and antigen because with this technique of tissue preservation ISH does not affect the sensitivity or the amount of the detected antigens. This work underscores the fact that tissue freeze-drying is an easy, convenient, and reliable technique for both ISH and immunohistochemistry and achieves excellent structural conditions for nonradioactive detection.


Development ◽  
1988 ◽  
Vol 103 (1) ◽  
pp. 111-118 ◽  
Author(s):  
C.J. Devlin ◽  
P.M. Brickell ◽  
E.R. Taylor ◽  
A. Hornbruch ◽  
R.K. Craig ◽  
...  

During limb development, type I collagen disappears from the region where cartilage develops and synthesis of type II collagen, which is characteristic of cartilage, begins. In situ hybridization using antisense RNA probes was used to investigate the spatial localization of type I and type II collagen mRNAs. The distribution of the mRNA for type II collagen corresponded well with the pattern of type II collagen synthesis, suggesting control at the level of transcription and mRNA accumulation. In contrast, the pattern of mRNA for type I collagen remained more or less uniform and did not correspond with the synthesis of the protein, suggesting control primarily at the level of translation or of RNA processing.


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