Abstract
All the nine common cytokines in this study (including NT-3, IGF-1, CNTF and TGF-α) bind noncovalently, yet with different specificities and to different degrees, with both normal α2-macroglobulin (α2M) and monoamine-modified α2M. The binding of NGF is by far the most efficient and is least affected by cationic proteins. The binding of NT-3 is slightly affected by cationic proteins but is completely blocked by NGF. The binding of TGF-α, TGF-β1, CNTF, and IL-6 is severely blocked by cationic proteins/NGF. We conclude that NGF and NT-3 appear to bind specifically in significant quantities to the same α2M sites; but the other cytokines by comparison bind minimally, and primarily or entirely use nonspecific molecular interactions in their binding to α2M.
| Original language | English |
|---|---|
| Pages (from-to) | 1255-1261 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 193 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jan 1 1993 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Comparative binding of neurotrophins (NT-3, CNTF and NGF) and various cytokines to α2-macroglobulin. / Liebl, Daniel J; Koo, P. H.
In: Biochemical and Biophysical Research Communications, Vol. 193, No. 3, 01.01.1993, p. 1255-1261.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Comparative binding of neurotrophins (NT-3, CNTF and NGF) and various cytokines to α2-macroglobulin
AU - Liebl, Daniel J
AU - Koo, P. H.
PY - 1993/1/1
Y1 - 1993/1/1
N2 - All the nine common cytokines in this study (including NT-3, IGF-1, CNTF and TGF-α) bind noncovalently, yet with different specificities and to different degrees, with both normal α2-macroglobulin (α2M) and monoamine-modified α2M. The binding of NGF is by far the most efficient and is least affected by cationic proteins. The binding of NT-3 is slightly affected by cationic proteins but is completely blocked by NGF. The binding of TGF-α, TGF-β1, CNTF, and IL-6 is severely blocked by cationic proteins/NGF. We conclude that NGF and NT-3 appear to bind specifically in significant quantities to the same α2M sites; but the other cytokines by comparison bind minimally, and primarily or entirely use nonspecific molecular interactions in their binding to α2M.
AB - All the nine common cytokines in this study (including NT-3, IGF-1, CNTF and TGF-α) bind noncovalently, yet with different specificities and to different degrees, with both normal α2-macroglobulin (α2M) and monoamine-modified α2M. The binding of NGF is by far the most efficient and is least affected by cationic proteins. The binding of NT-3 is slightly affected by cationic proteins but is completely blocked by NGF. The binding of TGF-α, TGF-β1, CNTF, and IL-6 is severely blocked by cationic proteins/NGF. We conclude that NGF and NT-3 appear to bind specifically in significant quantities to the same α2M sites; but the other cytokines by comparison bind minimally, and primarily or entirely use nonspecific molecular interactions in their binding to α2M.
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UR - http://www.scopus.com/inward/citedby.url?scp=0027296472&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1993.1760
DO - 10.1006/bbrc.1993.1760
M3 - Article
C2 - 7686751
AN - SCOPUS:0027296472
VL - 193
SP - 1255
EP - 1261
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -