The Metabolism of Chemically Modified Insulins

1978 ◽  
Vol 6 (3) ◽  
pp. 555-557
Author(s):  
D. PAPACHRISTODOULOU ◽  
D. BRANDENBURG ◽  
D. I. DRON ◽  
R. H. JONES ◽  
P. H. SÖNKSEN ◽  
...  
Diabetologia ◽  
1974 ◽  
Vol 10 (1) ◽  
pp. 1-5 ◽  
Author(s):  
P. Freychet ◽  
D. Brandenburg ◽  
A. Wollmer

1979 ◽  
Vol 184 (2) ◽  
pp. 355-360 ◽  
Author(s):  
S H L Thomas ◽  
M H Wisher ◽  
D Brandenburg ◽  
P H Sönksen

1. The dose-response relationships of insulin stimulation of lipogenesis and inhibition of lipolysis were studied simultaneously by using rat adipocytes to determine whether these different effects of insulin are mediated through the same or different sets of receptors. 2. The sensitivity (defined as the concentration of insulin required to produce a half-maximal effect) of the stimulated lipogenic response to insulin was not significantly different from the sensitivity of the anti-lipolytic response to insulin. The addition of different adrenaline and glucose concentrations did not alter the half-maximal concentration of insulin required to inhibit lipolysis. 3. The specificities of the lipogenic and antilipolytic responses were studied by using insulin analogues. The sensitivities of the lipogenic and anti-lipolytic responses were the same for five chemically modified insulins and hagfish insulin, which have potencies compared with bovine insulin of between 3 and 90%. 4. Starving rats for 48h significantly increased the sensitivities of both the antilipolytic and lipogenic responses to insulin, but the changes in the sensitivities of both lipogenesis and anti-lipolysis returned to that of fed rats. 5. We conclude that insulin stimulates lipogenesis and inhibits lipolysis over the same concentration range. These observations provide powerful evidence that the different effects of insulin are mediated through the same set of receptors.


ChemBioChem ◽  
2021 ◽  
Author(s):  
Kasper K Sørensen ◽  
Narendra Kumar Mishra ◽  
Maciej P Paprocki ◽  
Amit Mehrotra ◽  
Knud J. Jensen

Diabetologia ◽  
1976 ◽  
Vol 12 (6) ◽  
pp. 601-608 ◽  
Author(s):  
R. H. Jones ◽  
D. I. Dron ◽  
M. J. Ellis ◽  
P. H. S�nksen ◽  
D. Brandenburg

Author(s):  
J.H. Thomas ◽  
D.I. Dron ◽  
R.H. Jones ◽  
P.H. Sönksen ◽  
D. Brandenburg

2004 ◽  
Vol 14 (2) ◽  
pp. 481-483 ◽  
Author(s):  
Kentaro Nakashima ◽  
Makoto Miyagi ◽  
Koichi Goto ◽  
Yoko Matsumoto ◽  
Ryuichi Ueoka

Diabetologia ◽  
1980 ◽  
Vol 18 (1) ◽  
pp. 59-63 ◽  
Author(s):  
D. I. Dron ◽  
R. H. Jones ◽  
P. H. S�nksen ◽  
J. H. Thomas ◽  
D. Brandenburg

1989 ◽  
Vol 61 (01) ◽  
pp. 131-136 ◽  
Author(s):  
Richard A Harvey ◽  
Hugh C Kim ◽  
Jonathan Pincus ◽  
Stanley Z Trooskin ◽  
Josiah N Wilcox ◽  
...  

SummaryTissue plasminogen activator labeled with radioactive iodine (125I-tPA) was immobilized on vascular prostheses chemically modified with a thin coating of water-insoluble surfactant, tridodecylmethylammonium chloride (TDM AC). Surfactant- treated Dacron, polytetrafluoroethylene (PTFE), silastic, polyethylene and polyurethane bound appreciable amounts of 125I- tPA (5-30 μg 125I-tPA/cm2). Upon exposure to human plasma, the amount of 125I-tPA bound to the surface shows an initial drop during the first hour of incubation, followed by a slower, roughly exponential release with a t½ of appoximately 75 hours. Prostheses containing bound tPA show fibrinolytic activity as measured both by lysis of clots formed in vitro, and by hydrolysis of a synthetic polypeptide substrate. Prior to incubation in plasma, tPA bound to a polymer surface has an enzymic activity similar, if not identical to that of the native enzyme in buffered solution. However, exposure to plasma causes a decrease in the fibrinolytic activity of both bound tPA and enzyme released from the surface of the polymer. These data demonstrate that surfactant-treated prostheses can bind tPA, and that these chemically modified devices can act as a slow-release drug delivery system with the potential for reducing prosthesis-induced thromboembolism.


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