A letter from Paolo Animuccia: A composer's response to the Council of Trent

Sherr, Richard

doi:10.1093/earlyj/12.1.75

Cited by 34 publications

(18 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Early in this phase, at the point when the transformants require a functional v-abl protein, cells receive and integrate extrinsic signals that prepare the cell for late G1 and commitment to S. Stimulation by specific growth factors mediates early G1 transit in many hematopoietic cells and allows these cells to escape apoptotic death (10,11,39). Because the Ab-MLV-transformed pre-B cells studied here grow in the absence of such factors, the function of v-abl could be viewed as merely replacing a growth factor.…”

Section: Discussionmentioning

confidence: 99%

“…Despite the fundamental nature of this process, little is known about the exact ways in which transforming proteins affect cell cycle progression. Among the protein-tyrosine kinases, the normal homologues of the receptor class function in the G1 phase of the cycle, following interaction with appropriate ligand (8)(9)(10)(11). Although the cellular forms of some nonreceptor protein-tyrosine kinases interface with growth factor receptors, the picture for these molecules is less clear.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Lymphoid cells transformed by Abelson virus require the v-abl protein-tyrosine kinase only during early G1.

Chen

Rosenberg

1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Cells infected with temperature-sensitive transformation mutants of the Abelson murine leukemia virus express low levels of kinase activity at the nonpermissive temperature, causing transformed pre-B cells to die under these conditions. Examination of cell cycle profiles of such populations prior to cell death reveals that the cells accumulate in the G1 phase of the cell cycle. Following GI arrest, the cells die via apoptosis, an active process of cell elimination. Cell synchronization and temperature-shift experiments show that GI arrest reflects the requirement for a functional v-abl protein during early G1 and that the molecule is not required at other phases of the cell cycle. These data indicate that the substrate(s) critical to v-abl-mediated transformation is involved in regulating GI transit and that these interactions are dominant over all other changes required for the multistep process that results in the fully malignant phenotype associated with v-abl expression in lymphoid cells.The v-abl protein expressed by Abelson murine leukemia virus (Ab-MLV) (1) and the BCR/ABL proteins that are associated with several human leukemias (2) are among a large group of protein-tyrosine kinases that induce malignant transformation (3). This response is dependent on the kinase activity of these proteins (1, 3), probably because transformation involves the interaction of the enzyme with other proteins that stimulate cell growth when activated by tyrosine phosphorylation. This model is consistent with the role of tyrosine phosphorylation in signaling mediated by extracellular growth factor receptors that are themselves proteintyrosine kinases or interact with such molecules (3-5). However, the complex, multistep process of malignant transformation associated with many oncogenes, including v-abl (6, 7), cannot be fully explained by acquisition of growth factor independence. Transformation of pre-B cells requires both constitutive expression of the abl-encoded kinase and changes in as yet unidentified cellular genes (6, 7). These latter changes do not involve alterations in abl protein expression or activity but rather selection of cells with reduced requirements for growth factors supplied by bone marrow stromal cells (6). Understanding how these changes couple with the alterations induced by the v-abl protein is necessary to unravel the mechanisms controlling ablmediated transformation.Lymphoid cells fully transformed by Ab-MLV, like most transformed cells, grow under conditions that are distinct from those required by their normal counterparts. Thus, one important feature of transformation is malfunction of normal cell cycle controls. Despite the fundamental nature of this process, little is known about the exact ways in which transforming proteins affect cell cycle progression. Among the protein-tyrosine kinases, the normal homologues of the receptor class function in the G1 phase of the cycle, following interaction with appropriate ligand (8-11). Although the cellular forms of some nonreceptor protein-tyros...

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Lymphoid cells transformed by Abelson virus require the v-abl protein-tyrosine kinase only during early G1.

Chen

Rosenberg

1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…Colony stimulating factor-1 is a lineage-specific hemopoietin required for tile maturation of cells of the mononuclear phagocyte lineage [1]. CSFI binds with high affinity to a 972 amino acid transmembrane receptor expressed on macro phages and their precursors [2].…”

Section: Introductionmentioning

confidence: 99%

“…CSFI binds with high affinity to a 972 amino acid transmembrane receptor expressed on macro phages and their precursors [2]. CSFI binding stimulates receptor tyrosine kinase activity and a host of cellular responses believed to be important in transducing receptor signals [1]. As with other members of the class III receptor tyrosine kinases (PDGFR and KIT), the CSFIR cytoplasmic kinase domain is split into two segments by a hydrophilic sequence of approximately 70 amino acids termed the kinase insert domain [2].…”

Section: Introductionmentioning

confidence: 99%

The kinase insert domain of colony stimulating factor‐1 receptor is dispensable for CSF‐1 induced phosphatidylcholine hydrolysis

et al. 1991

View full text Add to dashboard Cite

Mouse NIH :~T3 fibtoblast~ transfected with human colony stimulatin$ t'actor.I re.plOt produced diacyllilycerol in response to CSFI and this ¢orrdated with elevated phosphatidylcholine hydrolyxinB activity measured in an in vitro assay, Treatment ~f cells with the isoflavone derivative ~:enistein attenu~tted PC hydroly~;is in vitro ~ugilestin8 a role for CSFIR tyrosiae kiaase activity. A CSFIK mutan¢ laekin|l 67 amino acidi or the kinase inert domain, which may affect the ~ssociation of receptor with certain subitrale~, stimulated PC hydrolysis in response to CSFI. Couplinl;to PC hydrolysis is likely a $eneral property or CSFI R and the kinase inserl domain is dispensable for this activity.Colony sdmulatinit l'a¢tor-! receptor; TI,'rosine kinase; Pho~phal dyleholine hydrol:tst~: NIH 3T] ¢oll

show abstract

“…APC differentiation is tightly controlled by extracellular stimuli, particularly cytokines, as well as by their downstream effector molecules. In this context, the fms-related tyrosine kinase 3 ligand (Flt3L), granulocyte͞macrophage colony-stimulating factor (GM-CSF), and macrophage colony-stimulating factor are well known positive regulators for APC development (1,(12)(13)(14). In addition, several intracellular signaling molecules and transcription factors that affect the development of individual DC subsets in vivo have been reported (9).…”

mentioning

confidence: 99%

Negative regulation of IFN-α/β signaling by IFN regulatory factor 2 for homeostatic development of dendritic cells

Honda

Mizutani

Taniguchi

2004

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

The development and cooperation of distinct subsets of antigenpresenting cells, particularly dendritic cells (DCs), may be critical for maintaining homeostatic immune responses. Recently, much attention has been focused on IFN-␣͞␤, the cytokines induced en masse by virus infection or the activation of Toll-like receptors, in the context of DC activation. Here, we show that mice deficient in IFN regulatory factor 2 exhibit selective loss of CD8␣ ؊ DCs, the so-called myeloid DCs, which is accompanied by a notable increase in CD11c ؊ CD11b high other myeloid lineage cells. Such deficiency is intrinsic to the bone marrow precursors, in which the abnormal induction of IFN-␣͞␤ genes causes excessive IFN signaling. The critical function of IFN regulatory factor 2 in the negative regulation of IFN-␣͞␤ signaling is underscored by the observation that the deficiency is rescued by introducing an additional null mutation for the IFN receptor complex. In view of accumulating evidence of the critical role of IFN-␣͞␤ signaling in DC activation, our present study offers a unique example in that the magnitude of a cytokine signal should be properly balanced in a stage-specific manner during the differentiation and activation of DCs.

show abstract

A letter from Paolo Animuccia: A composer's response to the Council of Trent

Cited by 34 publications

References 0 publications

Lymphoid cells transformed by Abelson virus require the v-abl protein-tyrosine kinase only during early G1.

Lymphoid cells transformed by Abelson virus require the v-abl protein-tyrosine kinase only during early G1.

The kinase insert domain of colony stimulating factor‐1 receptor is dispensable for CSF‐1 induced phosphatidylcholine hydrolysis

Negative regulation of IFN-α/β signaling by IFN regulatory factor 2 for homeostatic development of dendritic cells

Contact Info

Product

Resources

About