PMID- 1650003
OWN - NLM
STAT- MEDLINE
DCOM- 19910829
LR  - 20061115
IS  - 0962-8436 (Print)
IS  - 0962-8436 (Linking)
VI  - 331
IP  - 1261
DP  - 1991 Mar 29
TI  - Neurotrophins: structural relatedness and receptor interactions.
PG  - 255-8
AB  - Nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF) and 
      neurotrophin-3 (NT-3) are structurally related proteins that allow the survival 
      of specific populations of embryonic vertebrate neurons. The primary structure of 
      these neurotrophins, deduced from their nucleotide sequences, indicates that all 
      three are synthesized in the form of precursor proteins presumably allowing for 
      appropriate folding, including the formation of disulphide bridges, cleavage and 
      secretion. While no information is yet available on the 3-dimensional structures 
      of the neurotrophins, results from binding studies using the three neurotrophins 
      as ligands indicate that their receptors do recognize similarities, as well as 
      differences, between them. High-affinity receptors, that presumably mediate the 
      biological response, as well as low-affinity receptors are present on neurons 
      responsive to the neurotrophins. Whereas a large excess of heterologous ligand is 
      needed to reduce binding of a particular neurotrophin to its high-affinity 
      receptor, the same concentration of homologous or heterologous ligand similarly 
      reduce the binding of any of the three neurotrophins to the low-affinity 
      receptor. For all three, the low-affinity receptor appears to be the already 
      characterized NGF low-affinity receptor that seems to be an integral part of the 
      high-affinity receptor complexes. These results suggest that the regulation of 
      neuronal survival by target cells can, in part, be explained by the release from 
      these cells of limiting quantities of the structurally related neurotrophins, 
      each being recognized by a specific high-affinity receptor complex located on the 
      nerve terminals of the responsive neurons.
FAU - Rodriguez-Tebar, A
AU  - Rodriguez-Tebar A
AD  - Cajal Institute of Neurobiology, Madrid, Spain.
FAU - Dechant, G
AU  - Dechant G
FAU - Barde, Y A
AU  - Barde YA
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Philos Trans R Soc Lond B Biol Sci
JT  - Philosophical transactions of the Royal Society of London. Series B, Biological 
      sciences
JID - 7503623
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Nerve Growth Factors)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Neurotrophin 3)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Receptors, Nerve Growth Factor)
SB  - IM
MH  - Animals
MH  - Brain-Derived Neurotrophic Factor
MH  - Molecular Structure
MH  - Nerve Growth Factors/*chemistry/metabolism
MH  - Nerve Tissue Proteins/chemistry/metabolism
MH  - Neurotrophin 3
MH  - Receptors, Cell Surface/metabolism
MH  - Receptors, Nerve Growth Factor
RF  - 34
EDAT- 1991/03/29 00:00
MHDA- 1991/03/29 00:01
CRDT- 1991/03/29 00:00
PHST- 1991/03/29 00:00 [pubmed]
PHST- 1991/03/29 00:01 [medline]
PHST- 1991/03/29 00:00 [entrez]
AID - 10.1098/rstb.1991.0013 [doi]
PST - ppublish
SO  - Philos Trans R Soc Lond B Biol Sci. 1991 Mar 29;331(1261):255-8. doi: 
      10.1098/rstb.1991.0013.