Commercial Recombinant Human β‐Nerve Growth Factor and Adult Rat Dorsal Root Ganglia Contain an Identical Molecular Species of Nerve Growth Factor Prohormone

: Examination of commercial recombinant human β‐nerve growth factor (rh‐β‐NGF) preparations with polyclonal antibodies specific to 13‐kDa NGF and pro‐NGF‐specific domains revealed the presence of high‐molecular‐mass immunoreactive proteins, including a 60‐kDa NGF prohormone. On incubation with a mix...

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Published in:Journal of neurochemistry 2000-05, Vol.74 (5), p.2127-2133
Main Authors: Reinshagen, Max, Geerling, Irmlind, Eysselein, Viktor E., Adler, Guido, Huff, Kenneth R., Moore, Geoffrey Philip, Lakshmanan, Jayaraman
Format: Article
Language:English
Subjects:
Animals
chemiluminescence
Colon - chemistry
Deglycosylation
Dorsal root ganglia
Ganglia, Spinal - chemistry
Humans
Immunoblotting
Luminescent Measurements
Molecular Weight
Nerve growth factor
Nerve Growth Factor - analysis
Nerve Growth Factor - chemistry
Prohormone
Protein Precursors - analysis
Protein Precursors - chemistry
Rats
Rats, Sprague-Dawley
Recombinant Proteins - chemistry
Spinal Cord - chemistry
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Summary:: Examination of commercial recombinant human β‐nerve growth factor (rh‐β‐NGF) preparations with polyclonal antibodies specific to 13‐kDa NGF and pro‐NGF‐specific domains revealed the presence of high‐molecular‐mass immunoreactive proteins, including a 60‐kDa NGF prohormone. On incubation with a mixture of N‐ and O‐specific glycosidases, the 60‐kDa NGF prohormone generated a 32‐kDa protein corresponding to the molecular size of NGF precursor predicted by the cloned human NGF cDNA. Highly sensitive chemiluminescence immunoblot analysis of adult rat dorsal root ganglia, spinal cord, and colon tissues with NGF‐ and pro‐NGF domain‐specific antibodies also revealed the presence of high‐molecular‐mass proteins, including the 60‐kDa NGF prohormone. Based on the presence of the 60‐kDa NGF prohormone in dorsal root ganglia and its efferent tissues, we suggest that proteolytically unprocessed, glycosylated NGF prohormone may mediate interactions between neurons and the tissues they innervate.
ISSN:0022-3042
1471-4159
DOI:10.1046/j.1471-4159.2000.0742127.x