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Development. 2000 Dec;127(24):5487-95.
Adult corneal epithelium basal cells possess the capacity to activate epidermal, pilosebaceous and sweat gland genetic programs in response to embryonic dermal stimuli.

Ferraris C, Chevalier G, Favier B, Jahoda CA, Dhouailly D.

Equipe Biologie de la Differenciation Epitheliale, UMR CNRS 5538, LEDAC, Institut Albert Bonniot, Universite Joseph Fourier, Grenoble, France.

Recent work has shown remarkable plasticity between neural and hematopoeitic, as well as between hematopoeitic and muscle stem cells, depending on environmental stimuli (Fuchs, E. and Segre, J. A. (2000) Cell 100, 143-155). Stem cells give rise to a proliferative transient amplifying population (TA), which is generally considered to be irreversibly committed. Corneal epithelium provides a particularly useful system for studying the ability of TA cells to activate different genetic programs in response to a change in their fibroblast environment. Indeed, corneal stem and TA cells occupy different localities - stem cells at the periphery, and TA cells more central (Lehrer, M. S., Sun, T. T. and Lavker, R. M. (1998) J. Cell Sci. 111, 2867-2875) - and thus can be discretely dissected from each other. It is well known that pluristratified epithelia of cornea and skin display distinct programs of differentiation: corneal keratinocytes express keratin pair K3/K12 and epidermal keratinocytes keratin pair K1-2/K10; moreover, the epidermis forms cutaneous appendages, which express their own set of keratins. In our experiments, central adult rabbit corneal epithelium was thus associated either with a mouse embryonic dorsal, upper-lip or plantar dermis before grafting onto nude mice. Complementary experiments were performed using adult mouse corneal epithelium from the Rosa 26 strain. The origin of the differentiated structures were identified in the first case by Hoechst staining and in the second by the detection of beta-galactosidase activity. The results show that adult central corneal cells are able to respond to specific information originating from embryonic dermis. They give rise first to a new basal stratum, which does not express anymore corneal-type keratins, then to pilosebaceous units, or sweat glands, depending of the dermis, and finally to upper layers expressing epidermal-type keratins. Our results provide the first evidence that a distinct TA cell population can be reprogrammed.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11076768&dopt=Abstract

J Cell Biol. 2000 Nov 13;151(4):811-24.
CaM kinase IV regulates lineage commitment and survival of erythroid progenitors in a non-cell-autonomous manner.

Wayman GA, Walters MJ, Kolibaba K, Soderling TR, Christian JL.

Vollum Institute, Oregon Health Sciences University, Portland, Oregon 97201-3098, USA.

Developmental functions of calmodulin-dependent protein kinase IV (CaM KIV) have not been previously investigated. Here, we show that CaM KIV transcripts are widely distributed during embryogenesis and that strict regulation of CaM KIV activity is essential for normal primitive erythropoiesis. Xenopus embryos in which CaM KIV activity is either upregulated or inhibited show that hematopoietic precursors are properly specified, but few mature erythrocytes are generated. Distinct cellular defects underlie this loss of erythrocytes: inhibition of CaM KIV activity causes commitment of hematopoietic precursors to myeloid differentiation at the expense of erythroid differentiation, on the other hand, constitutive activation of CaM KIV induces erythroid precursors to undergo apoptotic cell death. These blood defects are observed even when CaM KIV activity is misregulated only in cells that do not contribute to the erythroid lineage. Thus, proper regulation of CaM KIV activity in nonhematopoietic tissues is essential for the generation of extrinsic signals that enable hematopoietic stem cell commitment to erythroid differentiation and that support the survival of erythroid precursors.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11076966&dopt=Abstract

Leuk Res. 2000 Dec;24(12):1023-31.
The homeodomain protein PRH influences the differentiation of haematopoietic cells.

Jayaraman PS, Frampton J, Goodwin G.

Department of Biochemistry, University of Bristol, University Walk, BS8 1TD, Bristol, UK. sheela.jayaramaristol.ac.uk

Haematopoiesis involves the differentiation of a self-renewing stem cell into all of the lineages found in circulating blood. Myb-Ets transformed chicken blastoderm cells (MEPs) have many of the characteristics of multipotent haematopoietic cells and represent a useful model system for the study of haematopoiesis. The proline-rich homeodomain protein (PRH) has previously been shown to be expressed in the haematopoietic compartment. In this report we show that PRH mRNA and protein levels are down regulated as MEPs differentiate along the myelomonocytic and erythrocytic lineages. In contrast, PRH mRNA and protein levels remain high as MEPs differentiate toward the thrombocytic lineage. Over-expression of full length PRH in MEPs inhibits their transformation and/or proliferation. However, the over-expression of N-terminally truncated PRH proteins results in normally proliferating cells that are predominantly differentiated along the myelomonocytic and eosinophilic lineages. These results suggest that PRH plays a role in the proliferation and differentiation of haematopoietic cells.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11077116&dopt=Abstract

Tsitologiia. 2000;42(9):903-6.
[The effect of extracts from Rhododendron aureum Georgi and Artemisia yacutica drod. on wheat root meristem cells division]

[Article in Russian]

Zhuravskaia AN, Ivanova-Afanas'eva NV, Nureeva GV, Kershengol'ts BM.

Institute of Biological Problems of Cryolithozone, Siberian Branch of RAS, Yakutsk.

A study was made of the action of extracts from two Yakutian plant species in the course of mitosis in the rootlet meristemic tissue in germs of the local variety of common wheat. The examined extracts contain a large amount of biologically active substances and colchicine-like compounds causing (at certain dilutions) the increase in mitotic activity of the meristemic tissue in wheat germs, with simultaneous augmentation of the number of abnormal cells in mitosis, which well compares with the action of 0.01% colchicine solution.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11077680&dopt=Abstract

Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13312-7.
Survival motor neuron protein modulates neuron-specific apoptosis.

Kerr DA, Nery JP, Traystman RJ, Chau BN, Hardwick JM.

Departments of Neurology, Molecular Microbiology and Immunology, Anesthesiology and Critical Care Medicine, and Pharmacology and Molecular Sciences, The Johns Hopkins Schools of Medicine and Public Health, Baltimore, MD 21205, USA.

Spinal muscular atrophy (SMA) is attributed to mutations in the SMN1 gene, leading to loss of spinal cord motor neurons. The neurotropic Sindbis virus vector system was used to investigate a role for the survival motor neuron (SMN) protein in regulating neuronal apoptosis. Here we show that SMN protects primary neurons and differentiated neuron-like stem cells, but not cultured cell lines from virus-induced apoptotic death. SMN also protects neurons in vivo and increases survival of virus-infected mice. SMN mutants (SMNDelta7 and SMN-Y272C) found in patients with SMA not only lack antiapoptotic activity but also are potently proapoptotic, causing increased neuronal apoptosis and animal mortality. Full-length SMN is proteolytically processed in brains undergoing apoptosis or after ischemic injury. Mutation of an Asp-252 of SMN abolished cleavage of SMN and increased the antiapoptotic function of full-length SMN in neurons. Taken together, deletions or mutations of the C terminus of SMN that result from proteolysis, splicing (SMNDelta7), or germ-line mutations (e.g., Y272C), produce a proapoptotic form of SMN that may contribute to neuronal death in SMA and perhaps other neurodegenerative disorders.

online pharmacy ref. source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11078511&dopt=Abstract

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