Modulation of fibronectin and thymic stromal cell-dependent thymocyte maturation by retinoic acid. 1994

D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
Department of Experimental Medicine, University La Sapienza, Rome, Italy.

Retinoic acid (RA) controls the differentiation of a variety of cell types, although its role in influencing T cell development and the mechanisms potentially involved have not been thoroughly investigated. To study the ability of RA to modulate T cell development, we established a thymic stromal cell line (TC-1S) that supports the phenotypic maturation of CD4-8- double negative (DN) or CD3-4-8- triple negative (TN) thymocyte precursors. Cocultures of either DN or TN thymocytes on a monolayer of TC-1S cells resulted in the appearance of thymocytes with a more mature phenotype (CD4+8+ double positive, CD4+ or CD8+ single positive, and CD3(low) cells). Double negative T cell contact with TC-1S cells also increased the production of fibronectin (FN) by the thymic stroma and the expression of the VLA-4 FN receptor on the DN cells. Ab-mediated inhibition of the interaction between FN and its receptors significantly reduced the level of induced T cell maturation. Addition of RA either to TC-1S cells alone or to the coculture with DN cells decreased stromal cell FN expression, antagonized DN cell-induced increase in stromal cell FN production and significantly inhibited in vitro thymocyte maturation. The effects of RA were likely mediated by RA acid receptors alpha and gamma expressed both in DN thymocytes and TC-1S cells. Together these data suggest that FN/VLA-4 interaction may be an important component of stromal cell-dependent thymocyte phenotypic differentiation and that this interaction can be one of the targets for the influence of RA in T cell development.

UI MeSH Term Description Entries
D008297 Male Males
D008810 Mice, Inbred C57BL One of the first INBRED MOUSE STRAINS to be sequenced. This strain is commonly used as genetic background for transgenic mouse models. Refractory to many tumors, this strain is also preferred model for studying role of genetic variations in development of diseases. Mice, C57BL,Mouse, C57BL,Mouse, Inbred C57BL,C57BL Mice,C57BL Mice, Inbred,C57BL Mouse,C57BL Mouse, Inbred,Inbred C57BL Mice,Inbred C57BL Mouse
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D002448 Cell Adhesion Adherence of cells to surfaces or to other cells. Adhesion, Cell,Adhesions, Cell,Cell Adhesions
D002454 Cell Differentiation Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs. Differentiation, Cell,Cell Differentiations,Differentiations, Cell
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D005353 Fibronectins Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins. Cold-Insoluble Globulins,LETS Proteins,Fibronectin,Opsonic Glycoprotein,Opsonic alpha(2)SB Glycoprotein,alpha 2-Surface Binding Glycoprotein,Cold Insoluble Globulins,Globulins, Cold-Insoluble,Glycoprotein, Opsonic,Proteins, LETS,alpha 2 Surface Binding Glycoprotein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated

Related Publications

D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
January 1997, Thymus,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
November 1998, Cellular immunology,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
January 2015, Journal of immunology research,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
November 1999, Experimental hematology,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
November 2013, Memorias do Instituto Oswaldo Cruz,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
June 1994, Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
July 1993, Journal of cell science,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
August 1987, The Journal of experimental medicine,
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
May 2012, Journal of immunology (Baltimore, Md. : 1950),
D Meco, and S Scarpa, and M Napolitano, and M Maroder, and D Bellavia, and R De Maria, and M Ragano-Caracciolo, and L Frati, and A Modesti, and A Gulino
May 2007, Biochemical and biophysical research communications,
Copied contents to your clipboard!