Expression of Hypoxia Inducible Factor–1α, Macrophage Migration Inhibition Factor, Matrix Metalloproteinase–2 and −9, and Their Inhibitors in Hemodialysis Grafts and Arteriovenous Fistulas

2008 ◽  
Vol 19 (2) ◽  
pp. 252-259 ◽  
Author(s):  
Sanjay Misra ◽  
Alex A. Fu ◽  
Dheeraj K. Rajan ◽  
Luis A. Juncos ◽  
Michael A. McKusick ◽  
...  
Keyword(s):  
Matrix Metalloproteinase ◽  
Hypoxia Inducible Factor ◽  
Matrix Metalloproteinase 2 ◽  
Macrophage Migration ◽  
Migration Inhibition ◽  
Factor Matrix ◽  
Inhibition Factor ◽  
Arteriovenous Fistulas ◽  
Macrophage Migration Inhibition Factor ◽  
Macrophage Migration Inhibition

Human macrophage migration inhibition factor: evidence for subunit structure

Science ◽  
1979 ◽  
Vol 205 (4403) ◽  
pp. 300-301 ◽  
Author(s):  
G Possanza ◽  
MC Cohen ◽  
T Yoshida ◽  
S Cohen
Keyword(s):  
Molecular Weight ◽  
Migration Inhibition Factor ◽  
Human Macrophage ◽  
Subunit Structure ◽  
Macrophage Migration ◽  
Migration Inhibition ◽  
Inhibition Factor ◽  
Macrophage Migration Inhibition Factor ◽  
Human Lymphoid Cell ◽  
Macrophage Migration Inhibition

Macrophage migration inhibition factor (MIF) derived from human lymphoid cell lines was found to lose biologic activity on dialysis. Although activity was not recovered in the dialyzate, mixing experiments demonstrated that the components in the retentate and dialyzate could reassociate to restore activity. The fragment of larger molecular weight (less than 10,000) could inhibit the activity of intact MIF, whereas the smaller molecular weight fragment (5,000 to 10,000) could not. These findings suggest that human MIF is composed of at least two noncovalently linked subunits. In analogy to the situation for certain bacterial toxins, one of these may represent an attachment piece for a target cell membrane receptor.

Sign in / Sign up

Export Citation Format

Share Document