Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.1.8 (cholinesterase)
 12,691 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nestin is an intermediate filament which was first identified in neuroepithelial stem cells. This expression has also been reported in restricted locations in adults. Previous studies have suggested that the periodontal Ruffini endings remain immature in nature even in adulthood. The present study reports on a characteristic expression of immunoreaction for nestin in the periodontal Ruffini endings during postnatal development. RT-PCR analysis detected nestin mRNA in a reverse transcripted cDNA sample from both the rat trigeminal ganglion and periodontal ligament. The nestin immunoreaction existed in the periodontal ligament at postnatal day 3 (PO 3 days), when many spindle-shaped Schwann cells were positive for nestin immunoreaction. At PO 1 week, when periodontal nerve fibers displayed a dendritic fashion, the round cells came to show the nestin immunoreaction. These immunopositive cells were also reactive for S-100 protein and non-specific cholinesterase, indicating that these cells could be categorized as terminal Schwann cells associated with the periodontal Ruffini endings. Some ordinary Schwann cells also exhibited nestin immunoreaction. From PO 2 to 3 weeks, nestin positive terminal Schwann cells increased in number in accordance with the postnatal development of the periodontal Ruffini endings, while this immuno-expression pattern remained unchanged. Nestin immunoreaction was also recognizable in the satellite cells - but never in the neurons - in the trigeminal ganglion throughout this observation period. This immuno-expression pattern suggests that nestin serves as an intermediate filament for mechanical stability in the periodontal Ruffini endings against external stimuli.
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PMID:Immunohistochemical detection of nestin in the periodontal Ruffini endings of the rat incisor. 1901 17

Adipose derived stem cells (ADSCs) are multipotent and can transdifferentiate into neural stem cells. We investigated the transdifferentiation of ADSCs to neural phenotype (NP) cells using selegiline and two-dimensional electrophoresis (2-DE). The perinephric and inguinal fat of rats was collected and used to isolate ADSCs that were characterized by immunophenotyping using flow cytometry. The ADSCs were differentiated into osteogenic and lipogenic cells. The NP cells were generated using 10-9 mM selegiline and characterized by immunocytochemical staining of nestin and neurofilament 68 (NF-68), and by qRT-PCR of nestin, neurod1 and NF68. Total protein of ADSCs and NP cells was extracted and their proteome patterns were examined using 2-DE. ADSCs carried CD73, CD44 and CD90 cell markers, but not CD34. ADSCs were differentiated into osteocyte and adipocyte lineages. The differentiated NP cells expressed nestin, neuro d1 and NF-68. The proteome pattern of ADSCs was compared with that of NP cells and eight spots showed more than a two fold increase in protein expression. The molecular weights and isoelectric points of these highly expressed proteins were estimated using Melanie software. We compared these results with those of the mouse proteomic database using the protein isoelectric point database, and the functions of the eight proteins in differentiation of NP cells were predicted using the UniProt database. The probable identities of the proteins that showed higher expression in NP cells included cholinesterase, GFRa2, protein kinase C (PKC-eta) and RING finger protein 121. The sequences of the proteins identified from mouse database were aligned by comparing them with similar proteins in rat database using the Basic Local Alignment Search Tool (BLAST). The E values of all aligned proteins were zero, which indicates consistency of the matched protein. These proteins participate in differentiation of the neuron and their overexpression causes ADSCs transdifferentiation into NP cells.
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PMID:Comparison of the proteome patterns of adipose-derived stem cells with those treated with selegiline using a two dimensional gel electrophoresis analysis. 3158 72