93 research outputs found
Tuning the Mechanical Response of MetalâOrganic Frameworks by Defect Engineering
- Author
- Publication venue
- Publication date
- 31/08/2018
- Field of study
The incorporation
of defects into crystalline materials provides
an important tool to fine-tune properties throughout various fields
of materials science. We performed high-pressure powder X-ray diffraction
experiments, varying pressures from ambient to 0.4 GPa in 0.025 GPa
increments to probe the response of defective UiO-66 to hydrostatic
pressure for the first time. We observe an onset of amorphization
in defective UiO-66 samples around 0.2 GPa and decreasing bulk modulus
as a function of defects. Intriguingly, the observed bulk moduli of
defective UiO-66Â(Zr) samples do not correlate with defect concentration,
highlighting the complexity of how defects are spatially incorporated
into the framework. Our results demonstrate the large impact of point
defects on the structural stability of metalâorganic frameworks
(MOFs) and pave the way for experiment-guided computational studies
on defect engineered MOFs
WNT signaling enhances breast cancer cell motility and blockade of the WNT pathway by sFRP1 suppresses MDA-MB-231 xenograft growth
- Author
- A Ayyanan
- A Bafico
- AJ Minn
- Anne Boulay
- C Jones
- CJ Marsit
- D Lodygin
- E Klopocki
- Edward J Oakeley
- EL Huguet
- ES Witze
- F Takahashi-Yanaga
- F Ugolini
- F Ugolini
- GM Caldwell
- GP Gupta
- H Clevers
- H Hashizume
- J Ezan
- J Veeck
- J Vervoorts
- JM Gonzalez-Sancho
- JS Lee
- LR Howe
- M Katoh
- M Shtutman
- M Shulewitz
- MT Chung
- N Li
- N Meyer
- Nancy E Hynes
- O Tetsu
- R Habas
- R Nusse
- R van Amerongen
- RM Neve
- S Han
- S Wu
- T Milovanovic
- T Reya
- T Schlange
- T Takada
- TC He
- Thomas Schlange
- VI DeAlmeida
- X Zi
- Y Endo
- Yutaka Matsuda
- YY Cheng
- Publication venue
- BioMed Central
- Publication date
- 01/01/2009
- Field of study
ABSTRACT: INTRODUCTION: In breast cancer deregulation of the WNT signaling pathway occurs by autocrine mechanisms. WNT ligands and Frizzled (FZD) receptors are coexpressed in primary breast tumors and cancer cell lines. Moreover, many breast tumors show hypermethylation of secreted Frizzled-related protein 1 (sFRP1)'s promoter region, causing low expression of this WNT antagonist. We have previously shown that the WNT pathway influences proliferation of breast cancer cell lines via activation of canonical signaling and epidermal growth factor receptor (EGFR) transactivation, and that interference with WNT signaling reduces proliferation. Here we examine the role of WNT signaling in breast tumor cell migration and on xenograft outgrowth. METHODS: The breast cancer cell line MDA-MB-231 was used to study WNT signaling. We examined the effects of activating or blocking the WNT pathway on cell motility by treatment with WNT ligands or by ectopic sFPR1 expression, respectively. The ability of sFRP1 expressing MDA-MB-231 cells to grow as xenografts was also tested. Microarray analyses were carried out to identify targets with roles in MDA-MB-231/sFRP1 tumor growth inhibition. RESULTS: We show that WNT stimulates the migratory ability of MDA-MB-231 cells. Furthermore, ectopic expression of sFRP1 in MDA-MB-231 cells blocks canonical WNT signaling and decreases their migratory potential. Moreover, the ability of MDA-MB-231/sFRP1 expressing cells to grow as xenografts in mammary glands and to form lung metastases is dramatically impaired. Microarray analyses led to the identification of two genes, CCND1 and CDKN1A, whose expression level is selectively altered in vivo in sFRP1 expressing tumors. The encoded proteins, Cyclin D1 and p21Cip1 were down- and up-regulated, respectively, in sFRP1 expressing tumors, suggesting that they are downstream mediators of WNT signaling. CONCLUSIONS: Our results show that the WNT pathway influences multiple biological properties of MDA-MB-231 breast cancer cells. WNT stimulates tumor cell motility; conversely sFRP1 mediated WNT pathway blockade reduces motility. Moreover, ectopic sFRP1 expression in MDA-MB-231 cells has a strong negative impact on tumor outgrowth and blocked lung metastases. These results suggest that interference with WNT signaling using sFRP1 to block the ligand-receptor interaction may be a valid therapeutic approach in breast cancer
Cell cycle-dependent acetylation of Rb2/p130 in NIH3T3 cells
- Author
- A Chestukhin
- A Felsani
- A Laich
- A Loidl
- A Roman
- AJ Canhoto
- B Popov
- C Giacinti
- CH Choi
- CJ Nelson
- D Cobrinik
- D Tedesco
- DX Nguyen
- F Mantovani
- F Schwarze
- G Brosch
- HM Chan
- J Meraner
- J Meraner
- J Vervoorts
- K Hansen
- K Hansen
- L Litovchick
- M Classon
- M Lechner
- M Macaluso
- MK White
- MW Jackson
- P Loidl
- PP Claudio
- RJ Sims
- T Stasyk
- W Du
- W Gu
- X Mayol
- Y Zhang
- Publication venue
- Nature Publishing Group
- Publication date
- Field of study
The retinoblastoma protein (pRb) and the pRb-related proteins, p130 and p107, form the âpocket protein' family of cell cycle regulatory factors. A well characterized function of these proteins is the cell cycle-dependent regulation of E2F-responsive genes. The biological activity of pocket proteins is regulated by phosphorylation and for the founding member pRb it has been shown that acetylation also has an important role in modulating its function during the cell cycle. Here, we show that hyperphosphorylated retinoblastoma 2 (Rb2)/p130 also exists in an acetylated form in NIH3T3 cells. Acetylated p130 is present in the nucleus but not in the cytoplasm. Acetylation is cell cycle dependent, starting in S-phase and persisting until late G2-period. Using recombinant p130 and truncated forms for in vitro acetylation by the acetyltransferase p300, we could identify K1079 in the C-terminal part as the major acetylation site by mass spectrometry. Minor acetylation sites were pinpointed to K1068 and K1111 in the C-terminus, and K128 and K130 in the N-terminus. The human papilloma virus 16 protein-E7 preferentially binds to acetylated p130 and significantly increases in vitro p130 acetylation by p300
The opposing transcriptional functions of Sin3a and c-Myc are required to maintain tissue homeostasis.
- Author
- A Keller
- A Volz
- A Wilson
- AS Zervos
- B Ren
- BB McConnell
- Bernd KĂŒbler
- Brian Hendrich
- C Blanpain
- C van Oevelen
- C van Oevelen
- CA Hassig
- CD Laherty
- CJ Payne
- Claire L. Cox
- DE Ayer
- Duncan T. Odom
- E Fuchs
- E Guccione
- Elisabete M. Nascimento
- EM Blackwood
- ER Lawlor
- F Zambelli
- FM Watt
- G David
- G Rao
- G Smyth
- GC Prendergast
- I Arnold
- I Marenholz
- IM de Alboran
- J Kim
- J Toedling
- J Vervoorts
- J Wells
- JA Segre
- Jennifer Nichols
- JH Dannenberg
- JH Patel
- KM Braun
- L Soucek
- M Conacci-Sorrell
- M Eilers
- M Frye
- M Frye
- M Nair
- Matthew Trotter
- MD Cole
- Menon Suraj
- Michaela Frye
- N Popov
- NM Sodir
- P Soriano
- PB Rahl
- PJ Hurlin
- PJ Hurlin
- RC Gentleman
- RG Lopez
- RJ Klose
- S Hussain
- Salvador Aznar Benitah
- Sandra Blanco
- SB McMahon
- Shobbir Hussain
- SM Cowley
- Stewart MacArthur
- T Habib
- T Stoelzle
- TD Littlewood
- V Muncan
- VH Cowling
- X Wang
- YC Tai
- Publication venue
- Nat Cell Biol
- Publication date
- 20/11/2011
- Field of study
How the proto-oncogene c-Myc balances the processes of stem-cell self-renewal, proliferation and differentiation in adult tissues is largely unknown. We explored c-Myc's transcriptional roles at the epidermal differentiation complex, a locus essential for skin maturation. Binding of c-Myc can simultaneously recruit (Klf4, Ovol-1) and displace (Cebpa, Mxi1 and Sin3a) specific sets of differentiation-specific transcriptional regulators to epidermal differentiation complex genes. We found that Sin3a causes deacetylation of c-Myc protein to directly repress c-Myc activity. In the absence of Sin3a, genomic recruitment of c-Myc to the epidermal differentiation complex is enhanced, and re-activation of c-Myc-target genes drives aberrant epidermal proliferation and differentiation. Simultaneous deletion of c-Myc and Sin3a reverts the skin phenotype to normal. Our results identify how the balance of two transcriptional key regulators can maintain tissue homeostasis through a negative feedback loop
Key signalling nodes in mammary gland development and cancer: Myc
- Author
- A Ayyanan
- A Bafico
- A Efstratiadis
- A Wilson
- AJ Butt
- BA Howard
- C Brisken
- C Escot
- C Grandori
- C Schulein
- C Williams
- CJ Watson
- CM Blakely
- CM D'Cruz
- D Cappellen
- DR Rhodes
- EA Musgrove
- F Sotgia
- G Arpino
- GW Robinson
- HA Lane
- I Wierstra
- J Teuliere
- J Vervoorts
- JE Visvader
- JM Rosen
- JS Carroll
- KD Sutherland
- KH Salter
- KI Zeller
- KR Reed
- L Ciarloni
- L Hennighausen
- M Barna
- M Eilers
- M Reedijk
- M Vita
- M Welcker
- MC Alles
- MD Cole
- MH Jeng
- MR Moore
- N Meyer
- N Popov
- Nancy E Hynes
- OJ Sansom
- R Callahan
- RC Hovey
- RL Sutherland
- RM Neve
- S Huang
- S Pece
- SL Deming
- SR Master
- T Schlange
- T Stoelzle
- T Tanos
- TA Stewart
- Tina Stoelzle
- VH Cowling
- Y Chen
- Y Matsuda
- Y Nikolsky
- Publication venue
- BioMed Central
- Publication date
- 15/10/2009
- Field of study
Myc has been intensely studied since its discovery more than 25 years ago. Insight has been gained into Myc's function in normal physiology, where its role appears to be organ specific, and in cancer where many mechanisms contribute to aberrant Myc expression. Numerous signals and pathways converge on Myc, which in turn acts on a continuously growing number of identified targets, via transcriptional and nontranscriptional mechanisms. This review will concentrate on Myc as a signaling mediator in the mammary gland, discussing its regulation and function during normal development, as well as its activation and roles in breast cancer
Deep Sequencing of MYC DNA-Binding Sites in Burkitt Lymphoma
- Author
- A Saunders
- AL Bookout
- AL Gartel
- Anke Ehlers
- Anke Sommerfeld
- B Hirsch
- B Langmead
- Burkhard Hirsch
- C Bellan
- C Brenner
- Christian Zinser
- Christoph König
- CJ Chapman
- CV Dang
- D Lenze
- Dido Lenze
- DW Felsher
- dW Huang
- Edda von der Wall
- Elisabeth Oker
- F Wolfertstetter
- G Dennis Jr
- GK Smyth
- Ines GĂŒtgemann
- J Fan
- J Vervoorts
- JJ Jacobs
- JL Hecht
- JM God
- Jochen Hecht
- K Isobe
- K Klapproth
- K Weigelt
- KA O'Donnell
- KI Zeller
- KI Zeller
- L Ma
- LA Baker
- LJ Zhu
- LM Boxer
- Luwen Zhang
- M Sauvageau
- M Vallespinos
- Michael Hummel
- MS Dai
- Peter Butzhammer
- PS Knoepfler
- Rainer Spang
- RD Hawkins
- S Anders
- S Heinz
- S Rottmann
- SH Swerdlow
- SJ Brown
- SK Oster
- SR Eberhardy
- SR Frank
- TC Chang
- TI Lee
- TV Bui
- VH Cowling
- Volkhard Seitz
- W Huber
- X Liu
- Y Benjamini
- Y Haupt
- YC Liu
- Z Li
- Publication venue
- Public Library of Science
- Publication date
- 01/01/2011
- Field of study
BACKGROUND:
MYC is a key transcription factor involved in central cellular processes such as regulation of the cell cycle, histone acetylation and ribosomal biogenesis. It is overexpressed in the majority of human tumors including aggressive B-cell lymphoma. Especially Burkitt lymphoma (BL) is a highlight example for MYC overexpression due to a chromosomal translocation involving the c-MYC gene. However, no genome-wide analysis of MYC-binding sites by chromatin immunoprecipitation (ChIP) followed by next generation sequencing (ChIP-Seq) has been conducted in BL so far.
METHODOLOGY/PRINCIPAL FINDINGS:
ChIP-Seq was performed on 5 BL cell lines with a MYC-specific antibody giving rise to 7,054 MYC-binding sites after bioinformatics analysis of a total of approx. 19 million sequence reads. In line with previous findings, binding sites accumulate in gene sets known to be involved in the cell cycle, ribosomal biogenesis, histone acetyltransferase and methyltransferase complexes demonstrating a regulatory role of MYC in these processes. Unexpectedly, MYC-binding sites also accumulate in many B-cell relevant genes. To assess the functional consequences of MYC binding, the ChIP-Seq data were supplemented with siRNA- mediated knock-downs of MYC in BL cell lines followed by gene expression profiling. Interestingly, amongst others, genes involved in the B-cell function were up-regulated in response to MYC silencing.
CONCLUSION/SIGNIFICANCE:
The 7,054 MYC-binding sites identified by our ChIP-Seq approach greatly extend the knowledge regarding MYC binding in BL and shed further light on the enormous complexity of the MYC regulatory network. Especially our observations that (i) many B-cell relevant genes are targeted by MYC and (ii) that MYC down-regulation leads to an up-regulation of B-cell genes highlight an interesting aspect of BL biology
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)
- Author
- A. -G. Wu
- A. C. Ma
- A. K. Au
- Abdel-Aziz A. K.
- Abdelfatah S.
- Abdellatif M.
- Abdoli A.
- Abel S.
- Abeliovich H.
- Abildgaard M. H.
- Abudu Y. P.
- Acevedo-Arozena A.
- Adamopoulos I. E.
- Adeli K.
- Adolph T. E.
- Adornetto A.
- Aflaki E.
- Agam G.
- Agarwal A.
- Aggarwal B. B.
- Agnello M.
- Agostinis P.
- Agrewala J. N.
- Agrotis A.
- Aguilar P. V.
- Ahmad S. T.
- Ahmed Z. M.
- Ahumada-Castro U.
- Aits S.
- Aizawa S.
- Akkoc Y.
- Akoumianaki T.
- Akpinar H. A.
- Al-Abd A. M.
- Al-Akra L.
- Al-Gharaibeh A.
- Alaoui-Jamali M. A.
- Alberti S.
- Alcocer-Gomez E.
- Alessandri C.
- Ali M.
- Alim Al-Bari M. A.
- Aliwaini S.
- Alizadeh J.
- Almacellas E.
- Almasan A.
- Alonso A.
- Alonso G. D.
- Altan-Bonnet N.
- Altieri D. C.
- Alvarez E. M. C.
- Alves da Costa C.
- Alves S.
- Alzaharna M. M.
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- Ambrosio S.
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- Ammanathan V.
- An Z.
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- Andrabi S. A.
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- Anozie U. C.
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- Anton Z.
- Anwar T.
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- Apostolova N.
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- Publication date
- 01/01/2021
- Field of study
Structural prediction of the interaction of the tumor suppressor p27KIP1 with cyclin A/CDK2 identifies a novel catalytically relevant determinant
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- A Matte
- AA Russo
- AW Murray
- B Hao
- B Sarcevic
- BA Schulman
- BC Nair
- Bernhard LĂŒscher
- C Davies
- C Dominguez
- C Gaiddon
- C Hall
- CA Galea
- DK Morrison
- DM Jacobsen
- EA Bienkiewicz
- ER Lacy
- GE Crooks
- Giulia Rossetti
- GN Ramachandran
- H Huang
- H Ruffner
- I Ivanov
- I Matsuura
- IA Vakser
- IM Chu
- J Kuriyan
- J Li
- J Vervoorts
- J Zhang
- J Zheng
- JA Costoya
- JA Endicott
- Jinyu Li
- JK Holmes
- JS Myers
- JW Dennis
- Jörg Vervoorts
- K Do
- KJ Stanya
- KY Lee
- L Wohlbold
- LJ Holt
- LM Iakoucheva
- LN Johnson
- M Grimmler
- M Kamijo
- M Malumbres
- M Malumbres
- MA Marti-Renom
- MC Marazita
- ML Major
- N Narayan
- N Tokuriki
- NR Brown
- P Bukczynska
- P Huertas
- Paolo Carloni
- PD Adams
- PD Jeffrey
- PV Hornbeck
- R Pandithage
- R Suryadinata
- RJ Sheaff
- RW Deed
- S Chen
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- TA Chohan
- U Asghar
- U Linzen
- VB Chen
- WL Lai
- Y Chi
- Y Gu
- Y Huang
- Y Zhang
- Z Dong
- Z Songyang
- ZQ Bao
- Publication venue
- 'Springer Science and Business Media LLC'
- Publication date
- Field of study
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1.
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- Zimmermann CM
- Ziviani E
- Zoladek T
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- Zorzano A
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- Zwerschke W
- Ălvarez ĂMC
- Ăvalos Y
- Ănal G
- ĂstĂŒn S
- ÄoliÄ M
- ÄokiÄ J
- Ćœerovnik E
- Publication venue
- 'Informa UK Limited'
- Publication date
- 01/01/2021
- Field of study
In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field
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