Temperature Profiles During Cryolipolysis

2021 ◽  
Author(s):  
Dillon McClintock ◽  
Neil T. Wright

Abstract Cryolipolysis is a noninvasive clinical procedure for the local reduction of adipose tissue. Paddles as cold as ~10 °C are placed in good thermal contact the epidermis. The goal is to cool the subcutaneous adipose tissue to ~10 °C, which induces apoptosis and an inflammatory response in the adipocytes. The dermis is, of course, cooler than the adipocytes, but the triglyceride in the adipocytes are thought to crystalize, causing apoptosis. The clinical procedure have been developed empirically. A mathematical model could aid in understanding the mechanisms of response and improving the design of the procedure. Here, the Pennes equation is used to model the temperature of the tissue during cooling. The two parameters identified are the thermal diffusivity of the tissue and a blood perfusion parameter, which also gives the characteristic length. Green's functions are used to solve the Pennes equation, which simplifies to a transient fin equation.

1980 ◽  
Vol 59 (3) ◽  
pp. 199-201 ◽  
Author(s):  
P. Arner ◽  
J. Östman

1. The activation of lipolysis on incubation of human subcutaneous adipose tissue was examined in terms of the relationship between the release of glycerol and the concentration of tissue cyclic AMP. 2. A strong positive correlation was obtained between the maximum concentration of cyclic AMP and the rate of glycerol release in the presence of noradrenaline (r = 0.9), whereas, in the basal state, these two parameters were only weakly correlated (r = 0.45). 3. It appears that the noradrenaline-induced rate of lipolysis depends upon the maximal concentration of cyclic AMP that is present in human adipose tissue.


2019 ◽  
Author(s):  
Frederique Van de Velde ◽  
Margriet Ouwens ◽  
Arsene-Helene Batens ◽  
Samyah Shadid ◽  
Bruno Lapauw ◽  
...  

Diabetes ◽  
2020 ◽  
Vol 69 (Supplement 1) ◽  
pp. 701-P
Author(s):  
PALLAVI VARSHNEY ◽  
BENJAMIN J. RYAN ◽  
CHIWOON AHN ◽  
MICHAEL W. SCHLEH ◽  
JEFFREY F. HOROWITZ

1999 ◽  
Vol 40 (6) ◽  
pp. 1071-1077
Author(s):  
Stéphane Thumelin ◽  
Claude Kohl ◽  
Jean Girard ◽  
Jean-Paul Pégorier

Animals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 2114
Author(s):  
Yusheng Liang ◽  
Nana Ma ◽  
Danielle N. Coleman ◽  
Fang Liu ◽  
Yu Li ◽  
...  

The objective was to perform a proof-of-principle study to evaluate the effects of methionine (Met) and arginine (Arg) supply on protein abundance of amino acid, insulin signaling, and glutathione metabolism-related proteins in subcutaneous adipose tissue (SAT) explants under ceramide (Ce) challenge. SAT from four lactating Holstein cows was incubated with one of the following media: ideal profile of amino acid as the control (IPAA; Lys:Met 2.9:1, Lys:Arg 2:1), increased Met (incMet; Lys:Met 2.5:1), increased Arg (incArg; Lys:Arg 1:1), or incMet plus incArg (Lys:Met 2.5:1 Lys:Arg 1:1) with or without 100 μM exogenous cell-permeable Ce (N-Acetyl-d-sphingosine). Ceramide stimulation downregulated the overall abundance of phosphorylated (p) protein kinase B (AKT), p-mechanistic target of rapamycin (mTOR), and p-eukaryotic elongation factor 2 (eEF2). Without Ce stimulation, increased Met, Arg, or Met + Arg resulted in lower p-mTOR. Compared with control SAT stimulated with Ce, increased Met, Arg, or Met + Arg resulted in greater activation of mTOR (p-mTOR/total mTOR) and AKT (p-AKT/total AKT), with a more pronounced response due to Arg. The greatest protein abundance of glutathione S-transferase Mu 1 (GSTM1) was detected in response to increased Met supply during Ce stimulation. Ceramide stimulation decreased the overall protein abundance of the Na-coupled neutral amino acid transporter SLC38A1 and branched-chain alpha-ketoacid dehydrogenase kinase (BCKDK). However, compared with controls, increased Met or Arg supply attenuated the downregulation of BCKDK induced by Ce. Circulating ceramides might affect amino acid, insulin signaling, and glutathione metabolism in dairy cow adipose tissue. Further in vivo studies are needed to confirm the role of rumen-protected amino acids in regulating bovine adipose function.


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