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Showing papers on "Transdifferentiation published in 1985"


Journal Article
TL;DR: Findings show that human neuroblastoma cells can undergo bidirectional transdifferentiation in vitro between a neuronal and a melanocyte phenotype, possibly reflecting a process which occurs in the patient.
Abstract: The human neuroblastoma cell line SK-N-SH comprises cells that undergo morphological and biochemical interconversion between a primitive sympathoblast and a variant, epithelial-like cell type which does not express the neuronal characteristics of the SK-N-SH cell line. Since neural crest cells, from which neuroblastomas are presumed to arise, can undergo transdifferentiation in culture from a neuronal phenotype into other cellular phenotypes, particularly into neurilemmal cells and melanocytes, the present study was undertaken to determine whether this capacity is preserved in malignant cells of the peripheral nervous system. Activities for tyrosinase, a melanocyte marker enzyme, and 2':3'-cyclic nucleotide phosphohydrolase, a Schwann-cell marker enzyme, were measured in clones of the two cell types. While no significant differences in 2':3'-cyclic nucleotide phosphohydrolase activity were measurable, tyrosinase activity was detectable only in the flattened neuroblastoma variant cell lines and was comparable to that in some human melanoma cell lines. The tyrosinase activity in neuroblastoma cell variants increased with cell density and was significantly elevated by melanocyte-stimulating hormone and 8-bromo-cyclic adenosine monophosphate, similar to that seen in melanoma cells in culture. Thus, our findings show that human neuroblastoma cells can undergo bidirectional transdifferentiation in vitro between a neuronal and a melanocyte phenotype, possibly reflecting a process which occurs in the patient.

114 citations


Journal ArticleDOI
TL;DR: In this article, an alpha A2-crystallin genomic probe was used to study the transcription and processing of alpha A 2-crystalin mRNA both during lens development and transdifferentiation.

13 citations


Journal ArticleDOI
TL;DR: The results are compatible with the idea that embryonic adrenal medullary cells have the environmentally controlled potential to develop along the neuronal or endocrine line, but could also be interpreted in terms of a selection of a specific subpopulation with predetermined potentialities by a specific microenvironment.

13 citations


Journal ArticleDOI
TL;DR: These nonpermissive media (FHGMEM and F199) indicate two different levels at which δ-crystallin gene expression can be controlled during transdifferentiation.

3 citations


Journal ArticleDOI
TL;DR: During transdifferentiation, mammalian α crystallin (B2 chain) exhibits considerable homology to four small Drosophila heat‐shock proteins, no significant antigenic similarity is apparent between δ crystallin and the major avian heat shock proteins, and crystallin production is not mediated by stress proteins resulting from a culture‐induced stress response.
Abstract: Embryonic chick neural retina responds to heat shock by the synthesis of “stress” polypeptides with molecular weights of 85 and 70 kd. Both stress proteins are synthesised from newly-transcribed messenger RNA. Sodium arsenite induces an additional stress protein of MW 25 kd. The heat shock response does not change during culture and subsequent transdifferentiation, and crystallin synthesis is not coinducible with the heat-shock proteins. We have also examined the pattern of protein synthesis at various stages of culture in both monolayer and aggregate systems; although changes in the protein synthetic profine are evident, there is no stress protein induction above basal levels at any time. Whilst mammalian α crystallin (B2 chain) exhibits considerable homology to four small Drosophila heat-shock proteins, no significant antigenic similarity is apparent between δ crystallin and the major avian heat shock proteins. Thus during transdifferentiation, (a) the crystallin proteins do not behave in a manner analogous to stress proteins; moreover (b) crystallin production is not mediated by stress proteins resulting from a culture-induced stress response.

2 citations