Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system

Sangram S. Sisodia, Edward H. Koo, Paul N. Hoffman, George Perry, Donald L. Price

Research output: Contribution to journalArticle

Abstract

Amyloid deposits are a characteristic feature of the senile plaques identified in the brains of aged primates, individuals with Down's syndrome, and cases of Alzheimer's disease. The β-amyloid protein (Aβ), the principal component of amyloid, is a 4 kDa peptide derived from larger amyloid precursor protein(s) (APP). Four mRNAs, generated by alternative splicing of pre-mRNA derived from a single gene, encode Aβ-containing membrane glycoproteins termed APP-695, -714, -751, and -770; the latter two isoforms contain a domain homologous to Kunitz protease inhibitors (KPI). The present study uses in vitro and in vivo strategies to examine the expression of APP in neurons of the dorsal root ganglia and the nature of APP transported in sciatic nerves of rats. Using quantitative in situ hybridization and semiquantitative PCR analysis, we document that mRNAs encoding APP-695 are expressed preferentially over transcripts that encode KPI-containing isoforms in rat sensory ganglia. Furthermore, we provide compelling evidence that APP-695 is the predominant isoform synthesized in sensory neurons of the rat PNS and that full-length APP-695 and, to a lesser extent, APP-751/770 are rapidly transported anterogradely in axons.

Original languageEnglish (US)
Pages (from-to)3136-3142
Number of pages7
JournalJournal of Neuroscience
Volume13
Issue number7
StatePublished - 1993

Fingerprint

Amyloid beta-Protein Precursor
Peripheral Nervous System
Protein Isoforms
Amyloid Plaques
Protease Inhibitors
Sensory Ganglia
Serum Amyloid A Protein
Messenger RNA
RNA Precursors
Membrane Glycoproteins
Alternative Splicing
Spinal Ganglia
Sensory Receptor Cells
Sciatic Nerve
Down Syndrome
Amyloid
Primates
In Situ Hybridization
Axons
Alzheimer Disease

Keywords

  • β-amyloid precursor protein
  • Alzheimer's disease
  • Axonal transport
  • Dorsal root ganglia (DRG)
  • DRG expression
  • Holo-APP-695

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Sisodia, S. S., Koo, E. H., Hoffman, P. N., Perry, G., & Price, D. L. (1993). Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. Journal of Neuroscience, 13(7), 3136-3142.

Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. / Sisodia, Sangram S.; Koo, Edward H.; Hoffman, Paul N.; Perry, George; Price, Donald L.

In: Journal of Neuroscience, Vol. 13, No. 7, 1993, p. 3136-3142.

Research output: Contribution to journalArticle

Sisodia, SS, Koo, EH, Hoffman, PN, Perry, G & Price, DL 1993, 'Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system', Journal of Neuroscience, vol. 13, no. 7, pp. 3136-3142.
Sisodia, Sangram S. ; Koo, Edward H. ; Hoffman, Paul N. ; Perry, George ; Price, Donald L. / Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system. In: Journal of Neuroscience. 1993 ; Vol. 13, No. 7. pp. 3136-3142.
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