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Monoclonal antibody NM2 recognizes the protein kinase C phosphorylation site in B-50 (GAP-43) and in neurogranin (BICKS).

Abstract：

:Mouse monoclonal B-50 antibodies (Mabs) were screened to select a Mab that may interfere with suggested functions of B-50 (GAP-43), such as involvement in neurotransmitter release. Because the Mab NM2 reacted with peptide fragments of rat B-50 containing the unique protein kinase C (PKC) phosphorylation site at serine-41, it was selected and characterized in comparison with another Mab NM6 unreactive with these fragments. NM2, but not NM6, recognized neurogranin (BICKS), another PKC substrate, containing a homologous sequence to rat B-50 (34-52). To narrow down the epitope domain synthetic B-50 peptides were tested in ELISAs. In contrast to NM6, NM2 immunoreacted with B-50 (39-51) peptide, but not with B-50 (43-51) peptide or a C-terminal B-50 peptide. Preabsorption by B-50 (39-51) peptide of NM2 inhibited the binding of NM2 to rat B-50 in contrast to NM6. NM2 selectively inhibited phosphorylation of B-50 during endogenous phosphorylation of synaptosomal plasma membrane proteins. Preabsorption of NM2 by B-50 (39-51) peptide abolished this inhibition. In conclusion, NM2 recognizes the QASFR peptide in B-50 and neurogranin. Therefore, NM2 may be a useful tool in physiological studies of the role of PKC-mediated phosphorylation and calmodulin binding of B-50 and neurogranin.

journal_name

J Neurochem

journal_title

Journal of neurochemistry

authors

Oestreicher AB,Hens JJ,Marquart A,Mercken M,De Graan PN,Zwiers H,Gipsen WH

doi

10.1046/j.1471-4159.1994.62030881.x

subject

Has Abstract

pub_date

1994-03-01 00:00:00

pages

881-9

issue

3

eissn

0022-3042

issn

1471-4159

journal_volume

62

pub_type

杂志文章

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