scholarly journals Transcriptional regulation of plasma protein synthesis during inflammation.

1986 ◽  
Vol 261 (18) ◽  
pp. 8077-8080
Author(s):  
H E Birch ◽  
G Schreiber
1974 ◽  
Vol 31 (03) ◽  
pp. 395-402 ◽  
Author(s):  
V Bocci ◽  
T Conti ◽  
M Muscettola ◽  
A Pacini ◽  
G. P Pessina

SummaryRabbit fibrinogen digest products (FDP) have been separated by Pevikon block electrophoresis yielding fragments D, E and other unidentified FDP.The fragments were injected into rabbits. Surprisingly, as little as 4.3 mg of fragment D elicited a significant increase in plasma fibrinogen concentration 24 hr after injection. The stimulating activity of fragment D is at least 10-fold higher than that of fragment E.


1982 ◽  
Vol 257 (17) ◽  
pp. 10271-10277 ◽  
Author(s):  
G Schreiber ◽  
G Howlett ◽  
M Nagashima ◽  
A Millership ◽  
H Martin ◽  
...  

Blood ◽  
1969 ◽  
Vol 34 (3) ◽  
pp. 348-356 ◽  
Author(s):  
SEYMOUR WERTHAMER ◽  
CARL HICKS ◽  
LEONARD AMARAL

Abstract The in vitro effects of sterols, cholesterol and 3-methyl cholanthrene and steroids, cortisol, prednisolone and testosterone on protein synthesis in separate popultions of human lymphocytes and leukocytes has been investigated. It has been shown that all agents used result in the inhibition of protein synthesis under these conditions. It has also been shown that the inhibitory mechanism of the steroid hormones requires the presence of plasma, presumably as a protein binding factor in order to achieve its effect. The sterol, cholesterol and 3-methyl cholanthrene, in the absence of plasma, still inhibit amino acid incorporation. However, in the case of cholesterol, the magnitude of inhibition is lower than that observed in the presence of plasma, perhaps indicating a partial plasma dependence. The results presented therefore support the hypothesis that the inhibition of lymphocyte protein synthesis by steroid hormones occurs only when the steroid is bound to a plasma protein. The physiologic role of the plasma protein-cortisol complex and its relation to the condition of lymphopenia in man is discussed.


2009 ◽  
Vol 297 (4) ◽  
pp. E889-E897 ◽  
Author(s):  
Abdul Jaleel ◽  
Katherine A. Klaus ◽  
Dawn M. Morse ◽  
Helen Karakelides ◽  
Lawrence E. Ward ◽  
...  

It remains to be determined whether systemic insulin replacement normalizes synthesis rates of different plasma proteins and whether there are differential effects on various plasma proteins. We tested a hypothesis that insulin deprivation differentially affects individual plasma protein synthesis and that systemic insulin treatment may not normalize synthesis of all plasma proteins. We measured synthesis rates of 41 plasma proteins in seven each of type 1 diabetic (T1DM) and nondiabetic participants (ND) using [ ring-13C6]phenylalanine as a tracer. T1DM were studied while on chronic insulin treatment and during 8 h insulin deprivation. Insulin treatment normalized glucose levels, but plasma insulin levels were higher during insulin treatment than during insulin deprivation in T1DM and ND. Individual plasma proteins were purified by affinity chromatography and two-dimensional gel electrophoresis. Only 41 protein gel spots from over 300 were chosen based on their protein homogeneity. Insulin deprivation and hyperglycemia either significantly increased ( n = 12) or decreased ( n = 12) synthesis rates of 24 of 41 plasma proteins in T1DM compared with ND. Insulin treatment normalized synthesis rates of 13 of these 24 proteins, which were altered during insulin deprivation. However, insulin treatment significantly altered the synthesis of 14 additional proteins. In conclusion, acute insulin deprivation caused both a decrease and increase in synthesis rates of many plasma proteins with various functions. Moreover, chronic systemic insulin treatment not only did not normalize synthesis of all plasma proteins but also altered synthesis of several additional proteins that were unaltered during insulin deprivation.


Biomedicines ◽  
2020 ◽  
Vol 8 (7) ◽  
pp. 188
Author(s):  
Carla Almendáriz-Palacios ◽  
Zoe E. Gillespie ◽  
Matthew Janzen ◽  
Valeria Martinez ◽  
Joanna M. Bridger ◽  
...  

Cellular health is reliant on proteostasis—the maintenance of protein levels regulated through multiple pathways modulating protein synthesis, degradation and clearance. Loss of proteostasis results in serious disease and is associated with aging. One proteinaceous structure underlying the nuclear envelope—the nuclear lamina—coordinates essential processes including DNA repair, genome organization and epigenetic and transcriptional regulation. Loss of proteostasis within the nuclear lamina results in the accumulation of proteins, disrupting these essential functions, either via direct interactions of protein aggregates within the lamina or by altering systems that maintain lamina structure. Here we discuss the links between proteostasis and disease of the nuclear lamina, as well as how manipulating specific proteostatic pathways involved in protein clearance could improve cellular health and prevent/reverse disease.


1975 ◽  
Vol 38 (1) ◽  
pp. 114-116 ◽  
Author(s):  
G. E. Siefring ◽  
F. J. Castellino

Two major forms of plasminogen exist in the plasma of many different species. Each form is present in normal amounts in anephric patients and each form is synthesized de novo in bilaterally nephrectomized rats. Although the rate of synthesis of each form of plasminogen is lower than normal immediately after nephrectomy, the rate of plasma protein synthesis is also apparently lower than normal in these cases. This is thought to reflect the fact that the nephrectomized rat is in a state of circulatory distress immediately after kidney ligation. It is concluded that the kidney is not responsible for de novo biosynthesis of plasminogen. This point has been the subject of some confusion.


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