Kinetics of Serum Protein Secretion by Cultured Hepatoma Cells: Evidence for Multiple Secretory Pathways

Author(s):  
Barry E. Ledford ◽  
Donna F. Davis
1980 ◽  
Vol 204 (1) ◽  
pp. 277-287 ◽  
Author(s):  
Helen C. Hamman ◽  
John A. Simpson ◽  
Barry E. Ledford

2007 ◽  
Vol 39 (2) ◽  
pp. 85-91 ◽  
Author(s):  
Don-Hee Park ◽  
George W. Malaney ◽  
Robert D. Tanner

1997 ◽  
Vol 17 (9) ◽  
pp. 5210-5226 ◽  
Author(s):  
V I Titorenko ◽  
D M Ogrydziak ◽  
R A Rachubinski

We have identified and characterized mutants of the yeast Yarrowia lipolytica that are deficient in protein secretion, in the ability to undergo dimorphic transition from the yeast to the mycelial form, and in peroxisome biogenesis. Mutations in the SEC238, SRP54, PEX1, PEX2, PEX6, and PEX9 genes affect protein secretion, prevent the exit of the precursor form of alkaline extracellular protease from the endoplasmic reticulum, and compromise peroxisome biogenesis. The mutants sec238A, srp54KO, pex2KO, pex6KO, and pex9KO are also deficient in the dimorphic transition from the yeast to the mycelial form and are affected in the export of only plasma membrane and cell wall-associated proteins specific for the mycelial form. Mutations in the SEC238, SRP54, PEX1, and PEX6 genes prevent or significantly delay the exit of two peroxisomal membrane proteins, Pex2p and Pex16p, from the endoplasmic reticulum en route to the peroxisomal membrane. Mutations in the PEX5, PEX16, and PEX17 genes, which have previously been shown to be essential for peroxisome biogenesis, affect the export of plasma membrane and cell wall-associated proteins specific for the mycelial form but do not impair exit from the endoplasmic reticulum of either Pex2p and Pex16p or of proteins destined for secretion. Biochemical analyses of these mutants provide evidence for the existence of four distinct secretory pathways that serve to deliver proteins for secretion, plasma membrane and cell wall synthesis during yeast and mycelial modes of growth, and peroxisome biogenesis. At least two of these secretory pathways, which are involved in the export of proteins to the external medium and in the delivery of proteins for assembly of the peroxisomal membrane, diverge at the level of the endoplasmic reticulum.


1955 ◽  
Vol 38 (3) ◽  
pp. 283-293 ◽  
Author(s):  
H. Green ◽  
H. S. Anker

1. The effect of varying body temperature on the rate of amino acid incorporation into serum protein does not give support to the idea that the rate of this process is adjusted in vivo to restore those protein molecules destroyed by thermal denaturation. The experimentally observed Q10 was about 3.9. 2. When amino acids are injected into the blood of animals in a steady state of serum protein turnover, a period of time elapses before these amino acids can be found in the serum proteins. This has been called transit time. At a given temperature (31°) it is the same in rabbits, turtles, and Limulus (1 hour). In rabbits and turtles it has a Q10 of 3.2. It appears to be specifically related to the process of synthesis (or release) of serum proteins. 3. It was not possible to affect the transit time or the incorporation rate by the administration of amino acid analogues.


1998 ◽  
Vol 23 (5) ◽  
pp. 361-365 ◽  
Author(s):  
Hirofumi Kodama ◽  
Yasuo Kodama ◽  
Shinya Shinozawa ◽  
Reizo Kanemaru ◽  
Kazunari Todaka ◽  
...  

1973 ◽  
Vol 29 (02) ◽  
pp. 339-346 ◽  
Author(s):  
H Vinazzer

SummaryA simple test for the detection and quantitation of resistance to ancrod is described. The test is based on the polymerization of fibrinogen by ancrod. The possible variables of the method such as the concentration of fibrinogen, the adsorption of ancrod onto a normal serum protein and the kinetics of the reaction between ancrod and the inactivating substance are examined. By this method, in 4 out of 19 patients who had previously received ancrod, resistance could be detected up to 15 months after therapy. In one of those patients, a second series of doses of ancrod was given. When the dose was elevated to an extent corresponding to the concentration of the inactivating substance, hypofibrinogenemia could be promptly established. The clinical importance of the test is discussed.


1999 ◽  
Vol 47 (3) ◽  
pp. 295-298 ◽  
Author(s):  
Hirofumi Kodama ◽  
Yasuo Kodama ◽  
Shinya Shinozawa ◽  
Reizo Kanemaru ◽  
Kazunari Todaka ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document