Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0016632 (Fox)
 1,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Increased utilization of the granulocyte-macrophage colony-forming unit (CFU-GM) assay for quality control, dosing, and clinical investigation of peripheral blood (PB) stem cell and bone marrow (BM) products led us to compare two commercially available media ("Ready-Mix" [RM] from Terry Fox, Vancouver, Canada and Stem Cell CFU Kit [SCCK]) from GIBCO, Grand Island, NY-Baxter Healthcare Corp., Deerfield, IL) to our standard laboratory media (SLM). Aliquots of mononuclear cells (MNC) from PB and BM donors were cultured in triplicate in the three media and CFU-GM and erythroid burst-forming units (BFU-E) were enumerated. Similar colony growth was achieved in all media for PB; modestly increased BM CFU-GM were noted in SCCK. SCCK and RM are easy to use, are commercially available with lot-controlled conditioned media (PHA-LCM), and may facilitate the standardization of CFU assays in blood banks and bone marrow processing laboratories.
 ...
PMID:Colony-forming unit culture of bone marrow and peripheral blood stem cells: comparison of commercially available media. 136 35

Activation of protein 4.1R exon 16 (E16) inclusion during erythropoiesis represents a physiologically important splicing switch that increases 4.1R affinity for spectrin and actin. Previous studies showed that negative regulation of E16 splicing is mediated by the binding of heterogeneous nuclear ribonucleoprotein (hnRNP) A/B proteins to silencer elements in the exon and that down-regulation of hnRNP A/B proteins in erythroblasts leads to activation of E16 inclusion. This article demonstrates that positive regulation of E16 splicing can be mediated by Fox-2 or Fox-1, two closely related splicing factors that possess identical RNA recognition motifs. SELEX experiments with human Fox-1 revealed highly selective binding to the hexamer UGCAUG. Both Fox-1 and Fox-2 were able to bind the conserved UGCAUG elements in the proximal intron downstream of E16, and both could activate E16 splicing in HeLa cell co-transfection assays in a UGCAUG-dependent manner. Conversely, knockdown of Fox-2 expression, achieved with two different siRNA sequences resulted in decreased E16 splicing. Moreover, immunoblot experiments demonstrate mouse erythroblasts express Fox-2. These findings suggest that Fox-2 is a physiological activator of E16 splicing in differentiating erythroid cells in vivo. Recent experiments show that UGCAUG is present in the proximal intron sequence of many tissue-specific alternative exons, and we propose that the Fox family of splicing enhancers plays an important role in alternative splicing switches during differentiation in metazoan organisms.
 ...
PMID:Fox-2 splicing factor binds to a conserved intron motif to promote inclusion of protein 4.1R alternative exon 16. 1653 40