Distribution of an APP homolog, APLP2, in the mouse olfactory system: A potential role for APLP2 in axogenesis

G. Thinakaran, C. A. Kitt, A. J I Roskams, H. H. Slunt, E. Masliah, C. Von Koch, S. D. Ginsberg, G. V. Ronnett, Randall R Reed, D. L. Price, S. S. Sisodia

Research output: Contribution to journalArticle

Abstract

Deposition of β-amyloid (Aβ) in senile plaques is a major pathological characteristic of Alzheimer's disease. Aβ is generated by proteolytic processing of amyloid precursor proteins (APP). APP is a member of a family of related polypeptides that includes amyloid precursor-like proteins APLP1 and APLP2. To examine the distribution of APLP2 in the nervous system, we generated antibodies specific for APLP2 and used these reagents in immunocytochemical and biochemical studies of the rodent nervous system. In this report, we document that in cortex and hippocampus, APLP2 is enriched in postsynaptic compartments. In the olfactory system, however, APLP2 is abundant in olfactory sensory axons, and axon terminals in glomeruli. Confocal microscopy revealed that APLP2 is present in both pre- and postsynaptic compartments in the olfactory bulb. Notably, mRNA encoding chondroitin sulfate glycosaminoglycan (CS GAG)-modified forms of APLP2 are enriched in the olfactory epithelium, relative to alternatively-spliced mRNA, encoding CS GAG-free forms of APLP2. In addition, we demonstrate that CS- modified APLP2 forms accumulate in the olfactory bulb. CS proteoglycans are known to play an important role in regulating cell migration and neuronal outgrowth. Since sensory neurons in the olfactory epithelium are in a state of continual turnover, axons of newly generated cells must establish synaptic connections with neurons in the olfactory bulb in adult life. The presence of APLP2 in olfactory sensory axons and glomeruli is consistent with the view that this protein may play an important role in axonal pathfinding and/or synaptogenesis.

Original languageEnglish (US)
Pages (from-to)6314-6326
Number of pages13
JournalJournal of Neuroscience
Volume15
Issue number10
StatePublished - 1995

Fingerprint

Amyloid beta-Protein Precursor
Olfactory Bulb
Axons
Olfactory Mucosa
Nervous System
Messenger RNA
Amyloid Plaques
Presynaptic Terminals
Sensory Receptor Cells
Proteoglycans
Amyloid
Confocal Microscopy
Cell Movement
Rodentia
Hippocampus
Alzheimer Disease
Neurons
Peptides
Antibodies
Proteins

Keywords

  • alternative splicing
  • amyloid precursor-like protein 2
  • APLP2
  • APP
  • chondroitin sulfate glycosaminoglycan
  • glomeruli
  • olfactory epithelium
  • olfactory sensory neurons

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Thinakaran, G., Kitt, C. A., Roskams, A. J. I., Slunt, H. H., Masliah, E., Von Koch, C., ... Sisodia, S. S. (1995). Distribution of an APP homolog, APLP2, in the mouse olfactory system: A potential role for APLP2 in axogenesis. Journal of Neuroscience, 15(10), 6314-6326.

Distribution of an APP homolog, APLP2, in the mouse olfactory system : A potential role for APLP2 in axogenesis. / Thinakaran, G.; Kitt, C. A.; Roskams, A. J I; Slunt, H. H.; Masliah, E.; Von Koch, C.; Ginsberg, S. D.; Ronnett, G. V.; Reed, Randall R; Price, D. L.; Sisodia, S. S.

In: Journal of Neuroscience, Vol. 15, No. 10, 1995, p. 6314-6326.

Research output: Contribution to journalArticle

Thinakaran, G, Kitt, CA, Roskams, AJI, Slunt, HH, Masliah, E, Von Koch, C, Ginsberg, SD, Ronnett, GV, Reed, RR, Price, DL & Sisodia, SS 1995, 'Distribution of an APP homolog, APLP2, in the mouse olfactory system: A potential role for APLP2 in axogenesis', Journal of Neuroscience, vol. 15, no. 10, pp. 6314-6326.
Thinakaran G, Kitt CA, Roskams AJI, Slunt HH, Masliah E, Von Koch C et al. Distribution of an APP homolog, APLP2, in the mouse olfactory system: A potential role for APLP2 in axogenesis. Journal of Neuroscience. 1995;15(10):6314-6326.
Thinakaran, G. ; Kitt, C. A. ; Roskams, A. J I ; Slunt, H. H. ; Masliah, E. ; Von Koch, C. ; Ginsberg, S. D. ; Ronnett, G. V. ; Reed, Randall R ; Price, D. L. ; Sisodia, S. S. / Distribution of an APP homolog, APLP2, in the mouse olfactory system : A potential role for APLP2 in axogenesis. In: Journal of Neuroscience. 1995 ; Vol. 15, No. 10. pp. 6314-6326.
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abstract = "Deposition of β-amyloid (Aβ) in senile plaques is a major pathological characteristic of Alzheimer's disease. Aβ is generated by proteolytic processing of amyloid precursor proteins (APP). APP is a member of a family of related polypeptides that includes amyloid precursor-like proteins APLP1 and APLP2. To examine the distribution of APLP2 in the nervous system, we generated antibodies specific for APLP2 and used these reagents in immunocytochemical and biochemical studies of the rodent nervous system. In this report, we document that in cortex and hippocampus, APLP2 is enriched in postsynaptic compartments. In the olfactory system, however, APLP2 is abundant in olfactory sensory axons, and axon terminals in glomeruli. Confocal microscopy revealed that APLP2 is present in both pre- and postsynaptic compartments in the olfactory bulb. Notably, mRNA encoding chondroitin sulfate glycosaminoglycan (CS GAG)-modified forms of APLP2 are enriched in the olfactory epithelium, relative to alternatively-spliced mRNA, encoding CS GAG-free forms of APLP2. In addition, we demonstrate that CS- modified APLP2 forms accumulate in the olfactory bulb. CS proteoglycans are known to play an important role in regulating cell migration and neuronal outgrowth. Since sensory neurons in the olfactory epithelium are in a state of continual turnover, axons of newly generated cells must establish synaptic connections with neurons in the olfactory bulb in adult life. The presence of APLP2 in olfactory sensory axons and glomeruli is consistent with the view that this protein may play an important role in axonal pathfinding and/or synaptogenesis.",
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T1 - Distribution of an APP homolog, APLP2, in the mouse olfactory system

T2 - A potential role for APLP2 in axogenesis

AU - Thinakaran, G.

AU - Kitt, C. A.

AU - Roskams, A. J I

AU - Slunt, H. H.

AU - Masliah, E.

AU - Von Koch, C.

AU - Ginsberg, S. D.

AU - Ronnett, G. V.

AU - Reed, Randall R

AU - Price, D. L.

AU - Sisodia, S. S.

PY - 1995

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N2 - Deposition of β-amyloid (Aβ) in senile plaques is a major pathological characteristic of Alzheimer's disease. Aβ is generated by proteolytic processing of amyloid precursor proteins (APP). APP is a member of a family of related polypeptides that includes amyloid precursor-like proteins APLP1 and APLP2. To examine the distribution of APLP2 in the nervous system, we generated antibodies specific for APLP2 and used these reagents in immunocytochemical and biochemical studies of the rodent nervous system. In this report, we document that in cortex and hippocampus, APLP2 is enriched in postsynaptic compartments. In the olfactory system, however, APLP2 is abundant in olfactory sensory axons, and axon terminals in glomeruli. Confocal microscopy revealed that APLP2 is present in both pre- and postsynaptic compartments in the olfactory bulb. Notably, mRNA encoding chondroitin sulfate glycosaminoglycan (CS GAG)-modified forms of APLP2 are enriched in the olfactory epithelium, relative to alternatively-spliced mRNA, encoding CS GAG-free forms of APLP2. In addition, we demonstrate that CS- modified APLP2 forms accumulate in the olfactory bulb. CS proteoglycans are known to play an important role in regulating cell migration and neuronal outgrowth. Since sensory neurons in the olfactory epithelium are in a state of continual turnover, axons of newly generated cells must establish synaptic connections with neurons in the olfactory bulb in adult life. The presence of APLP2 in olfactory sensory axons and glomeruli is consistent with the view that this protein may play an important role in axonal pathfinding and/or synaptogenesis.

AB - Deposition of β-amyloid (Aβ) in senile plaques is a major pathological characteristic of Alzheimer's disease. Aβ is generated by proteolytic processing of amyloid precursor proteins (APP). APP is a member of a family of related polypeptides that includes amyloid precursor-like proteins APLP1 and APLP2. To examine the distribution of APLP2 in the nervous system, we generated antibodies specific for APLP2 and used these reagents in immunocytochemical and biochemical studies of the rodent nervous system. In this report, we document that in cortex and hippocampus, APLP2 is enriched in postsynaptic compartments. In the olfactory system, however, APLP2 is abundant in olfactory sensory axons, and axon terminals in glomeruli. Confocal microscopy revealed that APLP2 is present in both pre- and postsynaptic compartments in the olfactory bulb. Notably, mRNA encoding chondroitin sulfate glycosaminoglycan (CS GAG)-modified forms of APLP2 are enriched in the olfactory epithelium, relative to alternatively-spliced mRNA, encoding CS GAG-free forms of APLP2. In addition, we demonstrate that CS- modified APLP2 forms accumulate in the olfactory bulb. CS proteoglycans are known to play an important role in regulating cell migration and neuronal outgrowth. Since sensory neurons in the olfactory epithelium are in a state of continual turnover, axons of newly generated cells must establish synaptic connections with neurons in the olfactory bulb in adult life. The presence of APLP2 in olfactory sensory axons and glomeruli is consistent with the view that this protein may play an important role in axonal pathfinding and/or synaptogenesis.

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