Ra. Murphy et al., IMMUNOLOGICAL RELATIONSHIPS OF NGF, BDNF, AND NT-3 - RECOGNITION AND FUNCTIONAL INHIBITION BY ANTIBODIES TO NGF, The Journal of neuroscience, 13(7), 1993, pp. 2853-2862
Polyclonal antibodies raised against mouse 2.5S NGF (mNGF) and against
synthetic peptides made from hydrophilic portions of mNGF have been u
sed to compare the immunological properties of mNGF, human recombinant
brain-derived neurotrophic factor (hrBDNF), and human recombinant neu
rotrophin-3 (hrNT-3). Affinity-isolated antibodies raised against inta
ct mNGF reacted with all three neurotrophins when tested by ELISA and
totally or partially blocked the bioactivities of the proteins in surv
ival assays of embryonic chicken sensory and sympathetic neurons. On W
estern blots, mNGF antibodies reacted with all three neurotrophins but
less well with hrBDNF and hrNT-3 than with mNGF. Antibodies to hydrop
hilic peptides within NGF (amino acids 23-35, 59-67, 69-79, and 91-100
) showed partial reactivity with some but not all of the neurotrophins
when tested by ELISA and on Western blots. The peptide antibodies wer
e also selectively effective in reducing the survival-promoting activi
ty of the neurotrophins on sensory neurons. Results show that mNGF, hr
BDNF, and hrNT-3 are immunologically related proteins and that mNGF an
tibodies react also with other members of the neurotrophin family.