scholarly journals Pentoxifylline Induces Lipolysis and Apoptosis of Human Preadipocytes, Keratinocytes and Fibroblasts In Vitro

2010 ◽  
Vol 18 (1) ◽  
pp. 56-64 ◽  
Author(s):  
Il-Kyu Lee ◽  
Yun-Jung Choi ◽  
In-Sop Shim ◽  
Kyung-Soo Kim ◽  
Chang-Jin Choi
Keyword(s):  
Human Preadipocytes

scholarly journals Hypoxia Alters the Expression of Dipeptidyl Peptidase 4 and Induces Developmental Remodeling of Human Preadipocytes

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Helena H. Chowdhury ◽  
Jelena Velebit ◽  
Nataša Radić ◽  
Vito Frančič ◽  
Marko Kreft ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Transmembrane Protein ◽  
Human Adipose Tissue ◽  
Dipeptidyl Peptidase ◽  
Dipeptidyl Peptidase 4 ◽  
Hypoxic Conditions ◽  
Human Preadipocytes ◽  
Developmental Remodeling

Dipeptidyl peptidase 4 (DPP4), a transmembrane protein, has been identified in human adipose tissue and is considered to be associated with obesity-related type 2 diabetes. Since adipose tissue is relatively hypoxic in obese participants, we investigated the expression of DPP4 in human preadipocytes (hPA) and adipocytes in hypoxia, during differentiation and upon insulin stimulation. The results show that DPP4 is abundantly expressed in hPA but very sparsely in adipocytes. During differentiationin vitro, the expression of DPP4 in hPA is reduced on the addition of differentiation medium, indicating that this protein can be hPA marker. Long term hypoxia altered the expression of DPP4 in hPA. Inin vitrohypoxic conditions the protease activity of shed DPP4 is reduced; however, in the presence of insulin, the increase in DPP4 expression is potentiated by hypoxia.

Human preadipocytes seeded on freeze-dried collagen scaffolds investigated in vitro and in vivo

Biomaterials ◽  
2001 ◽  
Vol 22 (5) ◽  
pp. 429-438 ◽  
Author(s):  
Dennis von Heimburg ◽  
Sascha Zachariah ◽  
Hendrik Kühling ◽  
Ingo Heschel ◽  
Heike Schoof ◽  
...  
Keyword(s):  
Collagen Scaffolds ◽  
Freeze Dried ◽  
Human Preadipocytes

scholarly journals Extracellular cystine influences human preadipocyte differentiation and correlates with fat mass in healthy adults

Amino Acids ◽  
2021 ◽  
Author(s):  
Hagar Elkafrawy ◽  
Radwa Mehanna ◽  
Fayrouz Ali ◽  
Ayman Barghash ◽  
Iman Dessouky ◽  
...  
Keyword(s):  
Fat Mass ◽  
Adipogenic Differentiation ◽  
Healthy Adults ◽  
Total Antioxidant ◽  
Human Preadipocytes ◽  
Modifiable Factor ◽  
Mixed Disulfides ◽  
Positive Correlations

AbstractPlasma cysteine is associated with human obesity, but it is unknown whether this is mediated by reduced, disulfide (cystine and mixed-disulfides) or protein-bound (bCys) fractions. We investigated which cysteine fractions are associated with adiposity in vivo and if a relevant fraction influences human adipogenesis in vitro. In the current study, plasma cysteine fractions were correlated with body fat mass in 35 adults. Strong positive correlations with fat mass were observed for cystine and mixed disulfides (r ≥ 0.61, P < 0.001), but not the quantitatively major form, bCys. Primary human preadipocytes were differentiated in media containing cystine concentrations varying from 10–50 μM, a range similar to that in plasma. Increasing extracellular cystine (10–50 μM) enhanced mRNA expression of PPARG2 (to sixfold), PPARG1, PLIN1, SCD1 and CDO1 (P = 0.042– < 0.001). Adipocyte lipid accumulation and lipid-droplet size showed dose-dependent increases from lowest to highest cystine concentrations (P < 0.001), and the malonedialdehyde/total antioxidant capacity increased, suggesting increased oxidative stress. In conclusion, increased cystine concentrations, within the physiological range, are positively associated with both fat mass in healthy adults and human adipogenic differentiation in vitro. The potential role of cystine as a modifiable factor regulating human adipocyte turnover and metabolism deserves further study.

Assessment of fat-specific protein 27 in the adipocyte lineage suggests a dual role for FSP27 in adipocyte metabolism and cell death

2008 ◽  
Vol 294 (4) ◽  
pp. E654-E667 ◽  
Author(s):  
Ji Young Kim ◽  
Kun Liu ◽  
Shengli Zhou ◽  
Kristin Tillison ◽  
Yu Wu ◽  
...  
Keyword(s):  
Cell Death ◽  
Mammalian Cells ◽  
Ectopic Expression ◽  
Transcript Level ◽  
Specific Protein ◽  
Fatty Acid Binding ◽  
Brown Adipose ◽  
Tnf Α ◽  
Human Preadipocytes

Fat-specific protein 27 (FSP27)/CIDEC was initially identified by its upregulation in TA1 adipogenesis and is one of three cell death-inducing DFF45-like effector (CIDE) family proapoptotic proteins. Ectopic expression of CIDEs promotes apoptosis of mammalian cells. On the other hand, FSP27 has very recently been illustrated to regulate lipid droplet size and promote lipid storage in adipocytes. Regulation of endogenous FSP27 expression is unknown. We assessed the FSP27 transcript level in the well-characterized 3T3-L1 in vitro adipocyte differentiation model and found its emergence parallels the adipocyte-enriched transcript adipocyte fatty acid binding protein and stearoyl Co-A desaturase 1. Furthermore, FSP27 is a differentiation-dependent transcript in adipogenesis of primary rodent and human preadipocytes and in brown adipogenesis. The FSP27 transcript is inversely regulated by TNF-α and insulin, consistent with an antilipolytic function. It is nearly abolished with a 4-h exposure of 3T3-L1 adipocytes to 10 ng/ml TNF-α, while treatment with 100 nM insulin increased the FSP27 transcript eightfold. In the latter case LY-294002 blocked this response, indicating involvement of phosphatidylinositol 3-kinase signals. Northern blot analysis of murine tissues indicated exclusive expression of FSP27 in white and brown adipose tissue; however, a dramatic upregulation occurred in the liver of ob/ob mice. Ectopic expression of murine FSP27 in 293T cells and in 3T3-L1 preadipocytes led to the appearance of key apoptotic hallmarks and cell death. However, despite the upregulation for FSP27 in adipogenesis, we failed to detect DNA laddering indicative of apoptosis in 3T3-L1 adipocytes. This suggests that adipogenesis is accompanied by decreased susceptibility to the proapoptotic effects of FSP27. Overall, our findings support roles for FSP27 in cell death and in adipocyte function.

Ultrastructural observations on differentiating human preadipocytes cultured in vitro

1976 ◽  
Vol 8 (3) ◽  
pp. 561-571 ◽  
Author(s):  
I. Dardick ◽  
W.J. Poznanski ◽  
I. Waheed ◽  
G. Setterfield
Keyword(s):  
Human Preadipocytes

scholarly journals Androgen receptors in human preadipocytes and adipocytes: regional specificities and regulation by sex steroids

1998 ◽  
Vol 274 (6) ◽  
pp. C1645-C1652 ◽  
Author(s):  
M. N. Dieudonné ◽  
R. Pecquery ◽  
A. Boumediene ◽  
M. C. Leneveu ◽  
Y. Giudicelli
Keyword(s):  
Androgen Receptors ◽  
Specific Binding ◽  
Fat Distribution ◽  
Men And Women ◽  
Fat Depots ◽  
Cell Extracts ◽  
Regional Specificity ◽  
Human Preadipocytes ◽  
Adipose Tissue Development

Various clinical and epidemiological evidence strongly suggests a major role for sex steroid hormones in the determination of anatomical specificities of fat distribution in human. To date, no studies have examined the possible presence of androgen receptors (AR) in human adipocytes and preadipocytes. We have studied AR in preadipocytes from various anatomical locations (intra-abdominal and subcutaneous) in middle-aged men and women during the proliferation and differentiation processes (adipogenesis). Androgen binding sites quantified by [3H]R-1881-specific binding in whole cell extracts were twofold higher in intra-abdominal than in subcutaneous preadipocytes but identical for the same fat depots in men and women. Western blot analysis revealed 1) the presence of AR in the nuclear and cytosolic fractions of human preadipocytes, 2) a decrease of AR expression during adipogenesis, and 3) an upregulation of AR by androgens in vitro. RT-PCR experiments showed the presence of AR mRNA in human preadipocytes and adipocytes and also the regional specificity of AR distribution. However, AR mRNA expression was found to increase during adipogenesis. The same results were observed in rat preadipocytes. In conclusion, this study clearly demonstrates the presence of AR in human preadipocytes and adipocytes and suggests that androgens may contribute, through regulation of their own receptors, to the control of adipose tissue development.

Optimization of the differentiation of human preadipocytes in vitro

2005 ◽  
Vol 73 (1) ◽  
pp. 28-35 ◽  
Author(s):  
Karsten Hemmrich ◽  
Dennis von Heimburg ◽  
Kathrin Cierpka ◽  
Sevinc Haydarlioglu ◽  
Norbert Pallua
Keyword(s):  
Human Preadipocytes

scholarly journals Role of Substance P in the Regulation of Glucose Metabolism via Insulin Signaling-Associated Pathways

Endocrinology ◽  
2011 ◽  
Vol 152 (12) ◽  
pp. 4571-4580 ◽  
Author(s):  
Iordanes Karagiannides ◽  
Kyriaki Bakirtzi ◽  
Efi Kokkotou ◽  
Dimitris Stavrakis ◽  
Kara Gross Margolis ◽  
...  
Keyword(s):  
Weight Gain ◽  
Protein Kinase ◽  
Glucose Metabolism ◽  
Substance P ◽  
Insulin Receptor ◽  
Blood Levels ◽  
Insulin Receptor Substrate ◽  
Insulin Receptor Substrate 1 ◽  
Human Preadipocytes

Substance P (SP), encoded by the tachykinin 1 (Tac1) gene, is the most potent tachykinin ligand for the high-affinity neurokinin-1 receptor (NK-1R). We previously reported that NK-1R-deficient mice show less weight gain and reduced circulating levels of leptin and insulin in response to a high-fat diet (HFD) and demonstrated the presence of functional NK-1R in isolated human preadipocytes. Here we assessed the effects of SP on weight gain in response to HFD and determined glucose metabolism in Tac1-deficient (Tac1−/−) mice. The effect of SP on the expression of molecules that may predispose to reduced glucose uptake was also determined in isolated human mesenteric, omental, and sc preadipocytes. We show that although weight accumulation in response to HFD was similar between Tac1−/− mice and wild-type littermates, Tac1−/− mice demonstrated lower glucose and leptin and increased adiponectin blood levels and showed improved responses to insulin challenge after HFD. SP stimulated phosphorylation of c-Jun N-terminal kinase, protein kinase Cθ, mammalian target of rapamycin, and inhibitory serine insulin receptor substrate-1 phosphorylation in human preadipocytes in vitro. Preincubation of human mesenteric preadipocytes with the protein kinase Cθ pseudosubstrate inhibitor reduced insulin receptor substrate 1 phosphorylation in response to SP. Lastly, SP also induced insulin receptor substrate-1 phosphorylation in mature human sc adipocytes. Our results demonstrate an important role for SP in adipose tissue responses and obesity-associated pathologies. These novel SP effects on molecules that enhance insulin resistance at the adipocyte level may reflect an important role for this peptide in the pathophysiology of type 2 diabetes.

Sign in / Sign up

Export Citation Format

Share Document