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 language | English (US) |
|---|---|
| Pages (from-to) | 3136-3142 |
| Number of pages | 7 |
| Journal | Journal of Neuroscience |
| Volume | 13 |
| Issue number | 7 |
| State | Published - 1993 |
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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
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 journal › Article
}
TY - JOUR
T1 - Identification and transport of full-length amyloid precursor proteins in rat peripheral nervous system
AU - Sisodia, Sangram S.
AU - Koo, Edward H.
AU - Hoffman, Paul N.
AU - Perry, George
AU - Price, Donald L.
PY - 1993
Y1 - 1993
N2 - 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.
AB - 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.
KW - β-amyloid precursor protein
KW - Alzheimer's disease
KW - Axonal transport
KW - Dorsal root ganglia (DRG)
KW - DRG expression
KW - Holo-APP-695
UR - http://www.scopus.com/inward/record.url?scp=0027212769&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027212769&partnerID=8YFLogxK
M3 - Article
C2 - 8331390
AN - SCOPUS:0027212769
VL - 13
SP - 3136
EP - 3142
JO - Journal of Neuroscience
JF - Journal of Neuroscience
SN - 0270-6474
IS - 7
ER -