adipose conversion
Recently Published Documents


TOTAL DOCUMENTS

108
(FIVE YEARS 0)

H-INDEX

34
(FIVE YEARS 0)

Bone ◽  
2019 ◽  
Vol 127 ◽  
pp. 343-352 ◽  
Author(s):  
Xavier Coutel ◽  
Jérôme Delattre ◽  
Pierre Marchandise ◽  
Guillaume Falgayrac ◽  
Hélène Béhal ◽  
...  

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
Venus Welch‐White ◽  
Norma Dawkins ◽  
Thomas Graham ◽  
Olga Bolden‐Tiller

Life Sciences ◽  
2011 ◽  
Vol 89 (21-22) ◽  
pp. 779-785 ◽  
Author(s):  
Cheuk Ying Chan ◽  
Lai Wei ◽  
Federico Castro-Muñozledo ◽  
Wing Leung Koo

2008 ◽  
Vol 374 (4) ◽  
pp. 720-724 ◽  
Author(s):  
Jorge-Tonatiuh Ayala-Sumuano ◽  
Cristina Velez-Del Valle ◽  
Alicia Beltrán-Langarica ◽  
José Manuel Hernández ◽  
Walid Kuri-Harcuch
Keyword(s):  

Obesity ◽  
2006 ◽  
Vol 14 (11) ◽  
pp. 1890-1897 ◽  
Author(s):  
Carine Chavey ◽  
Jérémie Boucher ◽  
Marie-Noëlle Monthouël-Kartmann ◽  
E. Helene Sage ◽  
Isabelle Castan-Laurell ◽  
...  

2006 ◽  
Vol 1 (2) ◽  
pp. 203-220 ◽  
Author(s):  
Andreas Böttcher ◽  
Alfred Böttcher ◽  
Gerd Schmitz ◽  
Petra Schling

AbstractAngiotensin-converting enzyme (ACE, kininase II) is a plasma membrane zinc metallopeptidase that acts as a key enzyme for the extracellular conversion of vasoactive peptides. Recently, ACE outside-in signalling in endothelial cells has been described. The present study tested the hypothesis that ACE signalling is not restricted to endothelial cells and may act as an additional peptide receptor on human preadipocytes and adipocytes. ACE protein levels were not changed during adipose conversion of human primary preadipocytes. The enzyme was primarily localized to the non-detergent-resistant fraction of the membrane and phosphorylated in non-dividing cells. Antibody arrays of whole cell lysate detected putative ACE-interacting proteins, which all share important roles in cell cycle control and/or apoptosis. These findings suggest that ACE is a versatile molecule, involved both in the regulation of extracellular peptide concentrations and direct intracellular signalling. In human adipose cells ACE may potentially influence exit from the cell cycle, differentiation, and programmed cell death signalling.


PROTEOMICS ◽  
2004 ◽  
Vol 4 (6) ◽  
pp. 1840-1848 ◽  
Author(s):  
Kai-Luk Choi ◽  
Yu Wang ◽  
Cynthia A. Tse ◽  
Karen S. L. Lam ◽  
Garth J. S. Cooper ◽  
...  

2002 ◽  
Vol 159 (1) ◽  
pp. 135-146 ◽  
Author(s):  
Jeremy Skillington ◽  
Lisa Choy ◽  
Rik Derynck

Mesenchymal cells can differentiate into osteoblasts, adipocytes, myoblasts, or chondroblasts. Whether mesenchymal cells that have initiated differentiation along one lineage can transdifferentiate into another is largely unknown. Using 3T3-F442A preadipocytes, we explored whether extracellular signals could redirect their differentiation from adipocyte into osteoblast. 3T3-F442A cells expressed receptors and Smads required for bone morphogenetic protein (BMP) signaling. BMP-2 increased proliferation and induced the early osteoblast differentiation marker alkaline phosphatase, yet only mildly affected adipogenic differentiation. Retinoic acid inhibited adipose conversion and cooperated with BMP-2 to enhance proliferation, inhibit adipogenesis, and promote early osteoblastic differentiation. Expression of BMP-RII together with BMP-RIA or BMP-RIB suppressed adipogenesis of 3T3-F442A cells and promoted full osteoblastic differentiation in response to retinoic acid. Osteoblastic differentiation was characterized by induction of cbfa1, osteocalcin, and collagen I expression, and extracellular matrix calcification. These results indicate that 3T3-F442A preadipocytes can be converted into fully differentiated osteoblasts in response to extracellular signaling cues. Furthermore, BMP and retinoic acid signaling cooperate to stimulate cell proliferation, repress adipogenesis, and promote osteoblast differentiation. Finally, BMP-RIA and BMP-RIB induced osteoblast differentiation and repressed adipocytic differentiation to a similar extent.


Sign in / Sign up

Export Citation Format

Share Document