Biomedical subjects

F B Berry

Publications and source records attributed to F B Berry.

At least 19 recordsLinked to original sources

PubMed2001

Positive and negative regulation of myogenic differentiation of C2C12 cells by isoforms of the multiple homeodomain zinc finger transcription factor ATBF1.

The ATBF1 gene encodes two protein isoforms, the 404-kDa ATBF1-A, possessing four homeodomains and 23 zinc fingers, and the 306-kDa ATBF1-B, lacking a 920-amino acid N-terminal region of ATBF1-A which contains 5 zinc fingers. In vitro, ATBF1-A was expressed in proliferating C2C12 myoblasts, but its expression levels decreased upon induction of myogenic differentiation in low serum medium. Forced expression of ATBF1-A in C2C12 cells resulted in repression of MyoD and myogenin expression and elevation of Id3 and cyclin D1 expression, leading to inhibition of myogenic differentiation in low serum. In contrast, transfection of C2C12 cells with the ATBF1-B isoform led to an acceleration of myogenic differentiation, as indicated by an earlier onset of myosin heavy chain expression and formation of a higher percentage of multinucleated myotubes. The fourth homeodomain of ATBF1-A bound to an AT-rich element adjacent to the E1 E-box of the muscle regulatory factor 4 promoter mediating transcriptional repression. The ATBF1-A-specific N-terminal region possesses general transcription repressor activity. These results suggest that ATBF1-A plays a role in the maintenance of the undifferentiated myoblast state, and its down-regulation is a prerequisite to initiate terminal differentiation of C2C12 cells.

Animals↗

PubMed2001

Analyses of the effects that disease-causing missense mutations have on the structure and function of the winged-helix protein FOXC1.

Five missense mutations of the winged-helix FOXC1 transcription factor, found in patients with Axenfeld-Rieger (AR) malformations, were investigated for their effects on FOXC1 structure and function. Molecular modeling of the FOXC1 forkhead domain predicted that the missense mutations did not alter FOXC1 structure. Biochemical analyses indicated that, whereas all mutant proteins correctly localize to the cell nucleus, the I87M mutation reduced FOXC1-protein levels. DNA-binding experiments revealed that, although the S82T and S131L mutations decreased DNA binding, the F112S and I126M mutations did not. However, the F112S and I126M mutations decrease the transactivation ability of FOXC1. All the FOXC1 mutations had the net effect of reducing FOXC1 transactivation ability. These results indicate that the FOXC1 forkhead domain contains separable DNA-binding and transactivation functions. In addition, these findings demonstrate that reduced stability, DNA binding, or transactivation, all causing a decrease in the ability of FOXC1 to transactivate genes, can underlie AR malformations.

Amino Acid Sequence↗

PubMed1996

CaM I mRNA is localized to apical dendrites during postnatal development of neurons in the rat brain.

In the rat, a single calmodulin (CaM) protein is encoded by three separate genes which produce five different transcripts. The significance of the multiple CaM genes is not known; however, individual CaM transcripts could be targeted to specific intracellular sites. In this report, the cellular distribution of CaM I mRNAs was analyzed in the postnatal rat brain. The 4.0-kb CaM I transcript was present in neuronal cell bodies and also localized to apical dendritic processes. In cerebral cortical neurons, the 4.0-kb CaM I mRNA was detected in apical dendrites at postnatal day (PD) 5 to 15. In hippocampal neurons, this CaM message was present in dendritic processes from PD S to 20, whereas in Purkinje neurons it was detected in dendrites at PD 15 and 20. The presence of the 4.0-kb CaM I mRNA in dendrites of the rat brain supports the notion of targeting transcripts derived from the CaM multigene family to discrete intracellular destinations.

Aging↗

PubMed1996

Alteration of CaM I mRNA expression in the developing rat superior colliculus following chronic treatment with an NMDA receptor antagonist.

The spatial distribution of CaM I mRNA was investigated in the developing superior colliculus of rats that were chronically treated with the NMDA receptor antagonist AP-5. In control animals, CaM I message was localized in a continuous band of cells that extended across the entire rostro caudal axis of the superficial superior colliculus. Chronic AP-5 treatment resulted in a specific reduction of CaM I message in the caudal colliculus at postnatal day 10. Since normal NMDA receptor function has been implicated in activity dependent synaptic plasticity in the superior colliculus, these results suggest that the regulation of calmodulin may be part of a cascade of events that mediate this plasticity following NMDA receptor activation.

2-Amino-5-phosphonovalerate↗

PubMed1974