Ruthenium red staining of vaginal epithelial cells and adherent bacteria

1985 ◽  
Vol 212 (1) ◽  
pp. 41-46 ◽  
Author(s):  
Barry F. King
1988 ◽  
Vol 102 (9) ◽  
pp. 760-765 ◽  
Author(s):  
Masaya Takumida ◽  
Dan Bagger-Sjöbäck ◽  
Helge Rask-Andersen

AbstractThe ultrastructure of the guinea pig endolymphatic sac was studied, using the ruthenium red staining technique. The dye stained the apical cell surface coat and the homogeneous substance in the luminal space of the endolymphatic sac, when introduced from the luminal side of the epithelium. It is suggested that the surface coat and homogeneous substance may play an important part in the endolymph regulatory mechanism in the endolymphatic sac. When ruthenium red was introduced from the subepithelial side, the basolateral surface of the epithelial cells usually became brightly stained in the absence of staining of the apical cell surface, due to the presence of the tight junctions. In some instances, however, the dye penetrated beyond the level of the tight junctions. Pinocytotic vesicles and larger vacuoles in the epithelial cells were also sometimes stained, both apically and near the lateral cell surface. These findings suggest that endolymph efflux mechanisms in the endolymphatic sac may involve the combined actions of a paracellular and transepithelial flow as well as a transcellular, vacuolar bulk flow.


Author(s):  
M. C. Buhrer ◽  
R. A. Mathews

Ruthenium red has been used as a stain to demonstrate a variety of extracellular materials, especially acid mucopolysaccharides. It also reacts with certain intracellular and extracellular lipids. Since biochemical studies in our laboratory demonstrated the presence of a variety of monosaccharides in human hair ruthenium red staining procedures were adopted in order to evaluate the presence and morphological location of acid oligosaccharides in the keratinized aspect of hair.


2011 ◽  
Vol 92 (9) ◽  
pp. 1981-1993 ◽  
Author(s):  
Xiao-Dan Yao ◽  
Kenneth Lee Rosenthal

Viruses that establish persistent infections have evolved numerous strategies to evade host innate antiviral responses. We functionally assessed the role of herpes simplex virus type 2 (HSV-2) virion host shutoff (vhs) protein on innate immune sensing pathways in human vaginal epithelial cells (VK2 ECs). Infection of cells with wild-type (WT) HSV-2 significantly decreased expression of innate immune sensors of viral infection, Toll-like receptor (TLR)2, TLR3, retinoic acid inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (Mda-5), relative to cells infected with a mutant that lacks vhs (vhsB) or mock-infected cells. Transfection with HSV-2 vhs similarly decreased expression of TLR2, TLR3, RIG-I and Mda-5, which was also confirmed in human embryonic kidney (HEK) 293 cells. vhsB infection of VK2 cells caused robust increases in the active form of interferon regulatory factor (IRF)3 and its translocation to the nucleus compared with the WT. Additionally, IRF3 activation by Sendai virus and polyinosinic : polycytidylic acid-induced stimulation of beta interferon (IFN-β) was significantly inhibited in vhs-transfected cells. Overall, our findings provide the first evidence that HSV-2 vhs plays roles in selectively inhibiting TLR3 and RIG-I/Mda-5, as well as TLR2-mediated antiviral pathways for sensing dsRNA and effectively suppresses IFN-β antiviral responses in human vaginal ECs.


2001 ◽  
Vol 360 (1) ◽  
pp. 107-115 ◽  
Author(s):  
Abinash Chandra MISTRY ◽  
Shinji HONDA ◽  
Shigehisa HIROSE

Using a Japanese-eel (Anguilla japonica) gill cDNA subtraction library, two novel β-d-galactose-binding lectins were identified that belong to group VII of the animal C-type lectin family. The eel C-type lectins, termed eCL-1 and eCL-2, are simple lectins composed of 163 amino acid residues, including a 22-residue signal peptide for secretion and a single carbohydrate-recognition domain (CRD) of ∼ 130 residues typical of C-type lectins. The galactose specificity of the CRD was suggested by the presence of a QPD motif and confirmed by a competitive binding assay. Using Ruthenium Red staining, the lectins were shown to bind Ca2+ ions. SDS/PAGE showed that native eCL-1 and eCL-2have an SDS-resistant octameric structure (a tetramer of disulphide-linked dimers). Northern and Western blot analyses demonstrated high-level expression of eCL-1 and eCL-2 mRNAs and their protein products in gills from freshwater eels, which decreased markedly when the eels were transferred from freshwater to seawater. Immunohistochemistry showed that the eel lectins are localized in the exocrine mucous cells of the gill.


Sign in / Sign up

Export Citation Format

Share Document