Beta-secretase-cleaved amyloid precursor protein in Alzheimer brain: a morphologic study

Kristina Sennvik, N Bogdanovic, Inga Volkmann, J Fastbom, Eirikur Benedikz

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

beta-amyloid (Abeta) is the main constituent of senile plaques seen in Alzheimer's disease. Abeta is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases beta- and gamma-secretase. In this study, we examined content and localization of beta-secretase-cleaved APP (beta-sAPP) in brain tissue sections from the frontal, temporal and occipital lobe. Strong granular beta-sAPP staining was found throughout the gray matter of all three areas, while white matter staining was considerably weaker. beta-sAPP was found to be localized in astrocytes and in axons. We found the beta-sAPP immunostaining to be stronger and more extensive in gray matter in Alzheimer disease (AD) cases than controls. The axonal beta-sAPP staining was patchy and unevenly distributed for the AD cases, indicating impaired axonal transport. beta-sAPP was also found surrounding senile plaques and cerebral blood vessels. The results presented here show altered beta-sAPP staining in the AD brain, suggestive of abnormal processing and transport of APP.
Original languageEnglish
JournalJournal of Cellular and Molecular Medicine
Volume8
Issue number1
Pages (from-to)127-34
Number of pages8
ISSN1582-1838
Publication statusPublished - 2004

Fingerprint

Alzheimer Disease
Amyloid Plaques
Peptide Hydrolases
Gray Matter

Keywords

  • Alzheimer Disease
  • Amyloid Precursor Protein Secretases
  • Amyloid beta-Protein Precursor
  • Aspartic Acid Endopeptidases
  • Astrocytes
  • Axons
  • Brain
  • Endopeptidases
  • Humans
  • Immunohistochemistry
  • Microscopy, Fluorescence

Cite this

Sennvik, Kristina ; Bogdanovic, N ; Volkmann, Inga ; Fastbom, J ; Benedikz, Eirikur. / Beta-secretase-cleaved amyloid precursor protein in Alzheimer brain: a morphologic study. In: Journal of Cellular and Molecular Medicine. 2004 ; Vol. 8, No. 1. pp. 127-34.
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abstract = "beta-amyloid (Abeta) is the main constituent of senile plaques seen in Alzheimer's disease. Abeta is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases beta- and gamma-secretase. In this study, we examined content and localization of beta-secretase-cleaved APP (beta-sAPP) in brain tissue sections from the frontal, temporal and occipital lobe. Strong granular beta-sAPP staining was found throughout the gray matter of all three areas, while white matter staining was considerably weaker. beta-sAPP was found to be localized in astrocytes and in axons. We found the beta-sAPP immunostaining to be stronger and more extensive in gray matter in Alzheimer disease (AD) cases than controls. The axonal beta-sAPP staining was patchy and unevenly distributed for the AD cases, indicating impaired axonal transport. beta-sAPP was also found surrounding senile plaques and cerebral blood vessels. The results presented here show altered beta-sAPP staining in the AD brain, suggestive of abnormal processing and transport of APP.",
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Beta-secretase-cleaved amyloid precursor protein in Alzheimer brain: a morphologic study. / Sennvik, Kristina; Bogdanovic, N; Volkmann, Inga; Fastbom, J; Benedikz, Eirikur.

In: Journal of Cellular and Molecular Medicine, Vol. 8, No. 1, 2004, p. 127-34.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Beta-secretase-cleaved amyloid precursor protein in Alzheimer brain: a morphologic study

AU - Sennvik, Kristina

AU - Bogdanovic, N

AU - Volkmann, Inga

AU - Fastbom, J

AU - Benedikz, Eirikur

PY - 2004

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N2 - beta-amyloid (Abeta) is the main constituent of senile plaques seen in Alzheimer's disease. Abeta is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases beta- and gamma-secretase. In this study, we examined content and localization of beta-secretase-cleaved APP (beta-sAPP) in brain tissue sections from the frontal, temporal and occipital lobe. Strong granular beta-sAPP staining was found throughout the gray matter of all three areas, while white matter staining was considerably weaker. beta-sAPP was found to be localized in astrocytes and in axons. We found the beta-sAPP immunostaining to be stronger and more extensive in gray matter in Alzheimer disease (AD) cases than controls. The axonal beta-sAPP staining was patchy and unevenly distributed for the AD cases, indicating impaired axonal transport. beta-sAPP was also found surrounding senile plaques and cerebral blood vessels. The results presented here show altered beta-sAPP staining in the AD brain, suggestive of abnormal processing and transport of APP.

AB - beta-amyloid (Abeta) is the main constituent of senile plaques seen in Alzheimer's disease. Abeta is derived from the amyloid precursor protein (APP) via proteolytic cleavage by proteases beta- and gamma-secretase. In this study, we examined content and localization of beta-secretase-cleaved APP (beta-sAPP) in brain tissue sections from the frontal, temporal and occipital lobe. Strong granular beta-sAPP staining was found throughout the gray matter of all three areas, while white matter staining was considerably weaker. beta-sAPP was found to be localized in astrocytes and in axons. We found the beta-sAPP immunostaining to be stronger and more extensive in gray matter in Alzheimer disease (AD) cases than controls. The axonal beta-sAPP staining was patchy and unevenly distributed for the AD cases, indicating impaired axonal transport. beta-sAPP was also found surrounding senile plaques and cerebral blood vessels. The results presented here show altered beta-sAPP staining in the AD brain, suggestive of abnormal processing and transport of APP.

KW - Alzheimer Disease

KW - Amyloid Precursor Protein Secretases

KW - Amyloid beta-Protein Precursor

KW - Aspartic Acid Endopeptidases

KW - Astrocytes

KW - Axons

KW - Brain

KW - Endopeptidases

KW - Humans

KW - Immunohistochemistry

KW - Microscopy, Fluorescence

M3 - Journal article

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EP - 134

JO - Journal of Cellular and Molecular Medicine

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