PMID- 20164556
OWN - NLM
STAT- MEDLINE
DCOM- 20100907
LR  - 20211020
IS  - 1875-8908 (Electronic)
IS  - 1387-2877 (Print)
IS  - 1387-2877 (Linking)
VI  - 20
IP  - 2
DP  - 2010
TI  - The Herp protein pathway is not involved in the pro-amyloidogenic effect of 
      hyperhomocysteinemia.
PG  - 569-76
LID - 10.3233/JAD-2010-1394 [doi]
AB  - Diet-induced high circulating levels of homocysteine, also known as 
      hyper-homocysteinemia (HHcy), is associated with an acceleration of Alzheimer's 
      disease-like amyloidosis. Herp is a homocysteine-responsive stress protein, which 
      has been shown to increase the formation of amyloid-beta (Abeta) via interaction 
      with presenilins in vitro. The aim of our paper was to investigate the functional 
      role that Herp plays in HHcy-induced amyloidosis. Amyloidosis secondary to 
      diet-induced HHcy in Tg2576 mice is associated with an increase of Herp protein 
      and mRNA levels. By contrast, no other stress-related proteins are altered by the 
      same diet regimen. Compared to wild type animals, brains from a genetically 
      induced HHcy mouse model did not manifest any significant change in Herp levels. 
      Cells stably over-expressing human AbetaPP Swedish mutant incubated with high 
      levels of homocysteine had an increase in Abeta formation, but no change in Herp 
      level. Finally, over-expression of Herp did not result in any significant 
      modification of Abeta levels. We conclude that the Herp protein pathway is 
      unlikely to be directly involved in the pro-amyloidotic effect of HHcy.
FAU - Zhuo, Jia-Min
AU  - Zhuo JM
AD  - Department of Pharmacology, Temple University School of Medicine, Philadelphia, 
      PA, USA.
FAU - Kruger, Warren D
AU  - Kruger WD
FAU - Pratico, Domenico
AU  - Pratico D
LA  - eng
GR  - R01 AG022512/AG/NIA NIH HHS/United States
GR  - AG-22512/AG/NIA NIH HHS/United States
GR  - HLBI16327/PHS HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Alzheimers Dis
JT  - Journal of Alzheimer's disease : JAD
JID - 9814863
RN  - 0 (Amyloid beta-Peptides)
RN  - 0 (Amyloid beta-Protein Precursor)
RN  - 0 (HERPUD1 protein, human)
RN  - 0 (Membrane Proteins)
RN  - EC 4.2.1.22 (Cystathionine beta-Synthase)
SB  - IM
MH  - Amyloid beta-Peptides/*metabolism
MH  - Amyloid beta-Protein Precursor/genetics
MH  - Animals
MH  - Cell Line, Transformed
MH  - Cricetinae
MH  - Cricetulus
MH  - Cystathionine beta-Synthase/deficiency
MH  - Disease Models, Animal
MH  - Female
MH  - Humans
MH  - Hyperhomocysteinemia/*genetics/*metabolism
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Mice, Transgenic
MH  - Mutation/genetics
MH  - Signal Transduction/physiology
PMC - PMC3877940
MID - NIHMS540541
EDAT- 2010/02/19 06:00
MHDA- 2010/09/08 06:00
PMCR- 2014/01/02
CRDT- 2010/02/19 06:00
PHST- 2010/02/19 06:00 [entrez]
PHST- 2010/02/19 06:00 [pubmed]
PHST- 2010/09/08 06:00 [medline]
PHST- 2014/01/02 00:00 [pmc-release]
AID - V63326143NN52638 [pii]
AID - 10.3233/JAD-2010-1394 [doi]
PST - ppublish
SO  - J Alzheimers Dis. 2010;20(2):569-76. doi: 10.3233/JAD-2010-1394.