Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:Q9UIJ5 (
Rec
)
58,342
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Extracellular calcium ions (Ca(2+)) are important in regulating the differentiation of keratinocytes and squamous epithelial cells. To clarify the mechanisms involved in the differentiation of human esophageal epithelial cells (EECs), we used the primary culture of human EECs, which can be differentiated by increasing the concentration of extracellular Ca(2+), and tried to reveal the extracellular Ca(2+) inducible genes using a differential display (DD) method. We found that the calcium-binding protein S100P showed a Ca(2+)-inducible expression in the EECs. Our immunohistochemical study demonstrated that differentiated large EECs expressing S100P overlie immature proliferating cells which lack S100P immunoreactivity. S100P was detected in vivo in the suprabasal layers of the epithelium. These findings indicate that S100P expression is closely associated with differentiation of human EECs. We also investigated the expression of other S100 proteins, including S100A2,
S100A6
, and CAAF1 (S100A12), in human EECs. Most of the immature EECs were positive for S100A2 and
S100A6
, whereas the S100A12-producing cells were similar to the S100P-producing cells. In vivo, S100A12 was strongly detected on all epithelial cells except for basal and proliferating cells. S100A2 was detected on all of the epithelial cells.
S100A6
was preferentially seen in the cells of basal layers. These findings suggest that within EECs S100 proteins might play important roles in cell differentiation during specific stages. Among them, S100P expression is unique in that this protein is transiently expressed during the early stage of differentiation.
Anat
Rec
2002 May 01
PMID:S100P expression in human esophageal epithelial cells: Human esophageal epithelial cells sequentially produce different S100 proteins in the process of differentiation. 1198 93
The lateral wall of the dog cochlear duct was investigated by classical staining and immunohistochemistry for NaK/ATPase beta2 isoform, cytokeratins (Cks), vimentin, nestin, and
S100A6
during the postnatal cochlear maturation, i.e., from birth to postnatal day 110. The dog stria vascularis was immature at birth. Fine melanin granules were evident in the stria from the second week of life, and melanin concentration increased drastically beyond the first month. The marginal cells were NaK/ATPase- and Ck-positive; intermediate cells were either nestin- and
S100A6
-positive or vimentin-positive; the basal cells were vimentin-positive; the capillary endothelium showed vimentin and nestin labeling; the cell layer underlying the stria was nestin-positive. The fibrocytes of the spiral ligament and spiral prominence expressed nestin and vimentin. The epithelial cells overlaying the spiral prominence and the external sulcus were Ck-positive, and transiently nestin- and vimentin-positive. Double immunolabeling, for
S100A6
and either nestin, vimentin, or NaK/ATPase, and for nestin and vimentin suggested the presence of two distinct intermediate cell types. The results enabled us to differentiate the cell types forming the lateral wall of the dog cochlear duct, and to follow their postnatal maturation. This study may form a basis for future investigations about spontaneous cochleosaccular degeneration in dogs. This species is an important companion animal, and a possible model for the study of comparable diseases in humans.
Anat
Rec
A Discov Mol Cell Evol Biol 2003 Jan
PMID:Postnatal maturation of the dog stria vascularis-- an immunohistochemical study. 1249 92