Enhanced Level of Site-Specific Proteolysis of GAP-43 Protein during Early Stages of Brain Development. Mosevitsky, M., Konovalova, E., Bichevaya, N., & Klementiev, B. Biochemistry (Moscow), 65(10):1153-1156, 2000. cited By 5![Enhanced Level of Site-Specific Proteolysis of GAP-43 Protein during Early Stages of Brain Development [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper abstract bibtex GAP-43 protein of nerve terminals (B-50, F1, F57, pp46, neuromodulin) is thought to be one of key proteins involved in the control of outgrowth of neuntes, release of neuromediators, synapse plasticity, etc. GAP-43 is usually considered as a whole protein. Along with the intact protein, nerve cells also contain two large native fragments of GAP-43 deprived of four or of about forty N-terminal amino acid residues (GAP-43-2 and GAP-43-3, respectively). The full-length GAP-43 is predominant in the mature brain. However, the ratio of the full-length protein and its fragments can vary under different physiological conditions. Changes in the GAP-43 proteins (the full-length protein and its fragments) were studied during embryonal and postnatal development of rat brain. The GAP-43 proteins were found to be expressed not later than on the 12-13th day of embryogenesis. Then their contents increased, and, until the 10th day after birth, GAP-43-3 dominated rather than the full-length protein. It is suggested that during this period the activity of a specific protease, which cleaves the N-terminal peptide of about 40 residues from the full-length GAP-43 molecule, is increased. The cleavage occurs in the region responsible for the interaction of GAP-43 with calmodulin. In the full-length molecule, this region is responsible also for the recognition of Ser4l residue by protein kinase C during phosphorylation. Another functionally important region that determines, in particular, the attachment of GAP-43 to the plasma membrane is cleaved from the main pan of the molecule together with the N-terminal peptide. Thus, the specific fragmentation of GAP-43 that depends on developmental stage should be considered as a controlled structural rearrangement fundamentally affecting the functions of this protein.
@ARTICLE{Mosevitsky20001153,
author={Mosevitsky, M.I. and Konovalova, E.S. and Bichevaya, N.K. and Klementiev, B.I.},
title={Enhanced Level of Site-Specific Proteolysis of GAP-43 Protein during Early Stages of Brain Development},
journal={Biochemistry (Moscow)},
year={2000},
volume={65},
number={10},
pages={1153-1156},
note={cited By 5},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034297206&partnerID=40&md5=b462a526bc02b4c0c63449b18e6f815d},
affiliation={Petersburg Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningrad Region, 188350, Russian Federation; Institute of Experimental Medicine, Russian Academy of Medical Sciences, ul. Akademika Pavlova 12, St. Petersburg 197376, Russian Federation},
abstract={GAP-43 protein of nerve terminals (B-50, F1, F57, pp46, neuromodulin) is thought to be one of key proteins involved in the control of outgrowth of neuntes, release of neuromediators, synapse plasticity, etc. GAP-43 is usually considered as a whole protein. Along with the intact protein, nerve cells also contain two large native fragments of GAP-43 deprived of four or of about forty N-terminal amino acid residues (GAP-43-2 and GAP-43-3, respectively). The full-length GAP-43 is predominant in the mature brain. However, the ratio of the full-length protein and its fragments can vary under different physiological conditions. Changes in the GAP-43 proteins (the full-length protein and its fragments) were studied during embryonal and postnatal development of rat brain. The GAP-43 proteins were found to be expressed not later than on the 12-13th day of embryogenesis. Then their contents increased, and, until the 10th day after birth, GAP-43-3 dominated rather than the full-length protein. It is suggested that during this period the activity of a specific protease, which cleaves the N-terminal peptide of about 40 residues from the full-length GAP-43 molecule, is increased. The cleavage occurs in the region responsible for the interaction of GAP-43 with calmodulin. In the full-length molecule, this region is responsible also for the recognition of Ser4l residue by protein kinase C during phosphorylation. Another functionally important region that determines, in particular, the attachment of GAP-43 to the plasma membrane is cleaved from the main pan of the molecule together with the N-terminal peptide. Thus, the specific fragmentation of GAP-43 that depends on developmental stage should be considered as a controlled structural rearrangement fundamentally affecting the functions of this protein.},
author_keywords={Gap-43 protein of nerve terminals; Neuroontogenesis; Site-specific proteolysis},
correspondence_address1={Mosevitsky, M.I.; Petersburg Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningrad Region, 188350, Russian Federation; email: mm5768@mm5768.spb.edu},
issn={00062979},
coden={BIORA},
pubmed_id={11092958},
language={English},
abbrev_source_title={Biochemistry Moscow},
document_type={Article},
source={Scopus},
}
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Akademika Pavlova 12, St. Petersburg 197376, Russian Federation","abstract":"GAP-43 protein of nerve terminals (B-50, F1, F57, pp46, neuromodulin) is thought to be one of key proteins involved in the control of outgrowth of neuntes, release of neuromediators, synapse plasticity, etc. GAP-43 is usually considered as a whole protein. Along with the intact protein, nerve cells also contain two large native fragments of GAP-43 deprived of four or of about forty N-terminal amino acid residues (GAP-43-2 and GAP-43-3, respectively). The full-length GAP-43 is predominant in the mature brain. However, the ratio of the full-length protein and its fragments can vary under different physiological conditions. Changes in the GAP-43 proteins (the full-length protein and its fragments) were studied during embryonal and postnatal development of rat brain. The GAP-43 proteins were found to be expressed not later than on the 12-13th day of embryogenesis. Then their contents increased, and, until the 10th day after birth, GAP-43-3 dominated rather than the full-length protein. It is suggested that during this period the activity of a specific protease, which cleaves the N-terminal peptide of about 40 residues from the full-length GAP-43 molecule, is increased. The cleavage occurs in the region responsible for the interaction of GAP-43 with calmodulin. In the full-length molecule, this region is responsible also for the recognition of Ser4l residue by protein kinase C during phosphorylation. Another functionally important region that determines, in particular, the attachment of GAP-43 to the plasma membrane is cleaved from the main pan of the molecule together with the N-terminal peptide. Thus, the specific fragmentation of GAP-43 that depends on developmental stage should be considered as a controlled structural rearrangement fundamentally affecting the functions of this protein.","author_keywords":"Gap-43 protein of nerve terminals; Neuroontogenesis; Site-specific proteolysis","correspondence_address1":"Mosevitsky, M.I.; Petersburg Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningrad Region, 188350, Russian Federation; email: mm5768@mm5768.spb.edu","issn":"00062979","coden":"BIORA","pubmed_id":"11092958","language":"English","abbrev_source_title":"Biochemistry Moscow","document_type":"Article","source":"Scopus","bibtex":"@ARTICLE{Mosevitsky20001153,\r\nauthor={Mosevitsky, M.I. and Konovalova, E.S. and Bichevaya, N.K. and Klementiev, B.I.},\r\ntitle={Enhanced Level of Site-Specific Proteolysis of GAP-43 Protein during Early Stages of Brain Development},\r\njournal={Biochemistry (Moscow)},\r\nyear={2000},\r\nvolume={65},\r\nnumber={10},\r\npages={1153-1156},\r\nnote={cited By 5},\r\nurl={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0034297206&partnerID=40&md5=b462a526bc02b4c0c63449b18e6f815d},\r\naffiliation={Petersburg Inst. of Nuclear Physics, Russian Academy of Sciences, Gatchina, Leningrad Region, 188350, Russian Federation; Institute of Experimental Medicine, Russian Academy of Medical Sciences, ul. 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