Immunohistochemical studies of brain pyridoxine-5′-phosphate oxidase

Bahn, Jae Hoon; Kwon, Oh Nam; Joo, Hye Mee; Jang, Sang Ho; Park, Jinseu; Hwang, In Koo; Kang, Tae Cheon; Won, Moo Ho; Kwon, Hyeok Yil; Kwok, Francis; Kim, Hyong Bai; Cho, Sung Woo; Choi, Soo Young

doi:10.1016/s0006-8993(01)03271-1

Cited by 21 publications

(20 citation statements)

References 32 publications

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“…In the present study, we identified (with at least 3 peptides) 23 proteins with significantly increased (Table 1) and 23 proteins with decreased ( Table 2) (1) - (Chihara et al, 2007), (2) - (Folci et al, 2014), (3) - (Chen et al, 2002), (4) - (Tanaka et al, 2000), (5) - (Ding and Shen, 2008), (6) - (Na et al, 2012), (7) - (Lyon et al, 2007), (8) - (Sweatt et al, 2004), (9) - (Bahn et al, 2002), (10) - (Manya et al, 1998), (11) - (Kamada et al, 2003), (12) - (McKenna et al, 2000), (13) - (Christel et al, 2012), (GO) -According to Gene Ontology database. …”

Section: Functional Clusters Of Altered Proteinsmentioning

confidence: 68%

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Chronic Cerebral Hypoperfusion Induced Synaptic Proteome Changes in the rat Cerebral Cortex

et al. 2017

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Chronic cerebral hypoperfusion (CCH) evokes mild cognitive impairment (MCI) and contributes to the progression of vascular dementia and Alzheimer's disease (AD). How CCH 2 induces these neurodegenerative processes that may spread along the synaptic network and whether they are detectable at the synaptic proteome level of the cerebral cortex remains to be established.In the present study, we report the synaptic protein changes in the cerebral cortex after stepwise bilateral common carotid artery occlusion (BCCAO) induced CCH in the rat. The occlusions were confirmed with Magnetic Resonance Angiography 5 weeks after the surgery.Synaptosome fractions were prepared using sucrose gradient centrifugation from cerebral cortex dissected 7 weeks after the occlusion. The synaptic protein differences between the sham operated and CCH groups were analysed with label free nanoUHPLC-MS/MS.

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Section: Functional Clusters Of Altered Proteinsmentioning

confidence: 68%

“…enzymes (Bahn et al, 2002). BCAT1 is localized exclusively in neurons in the adult rat brain and catalyzes the reversible transamination of α-ketoglutarate to glutamate while GAD catalyzes the decarboxylation of glutamate to GABA (Sweatt et al, 2004).…”

Section: Chronic Cerebral Hypoperfusion Effects On Gabaergic / Glutammentioning

confidence: 99%

Chronic Cerebral Hypoperfusion Induced Synaptic Proteome Changes in the rat Cerebral Cortex

et al. 2017

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“…Thus, we suggest that Rho GTPase down-regulation by GDI activation in ischemic brain injury mediates neuronal cell death. Pyridoxal-5'-phosphate (PLP) is the active coenzyme form of vitamin B6 and is a cofactor in neurotransmitter synthesis [1]. PLP phosphatase (PLPP) regulates PLP concentration [13] and is an actin-depolymerizing factor that is fundamental in cellular structure remodeling, cell growth, differentiation, and neurotransmission [7].…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Focal Cerebral Ischemic Injury in Male Rats

Koh

2010

J. Vet. Med. Sci.

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ABSTRACT. The present study identified the proteins that are differentially expressed during ischemic brain injury. Adult male rats were performed a middle cerebral artery occlusion (MCAO) to induce cerebral ischemia, and brains were collected at 24 hr after MCAO. Protein analysis was performed on the cerebral cortex using two-dimensional gel electrophoresis. Protein spots with a greater than 3 fold change in intensity between the sham and MCAO groups were identified by mass spectrometry. Among these proteins, 60 kDa heat shock protein, dehydropyrimidinase-related protein 2, t-complex protein 1, and Rho GDP dissociation inhibitor levels were significantly increased in MCAO group compared to those of the sham group. In contrast, thioredoxin, peroxiredoxin-2, stathmin, ubiquitin carboxyterminal hydrolase L1, guanine nucleotide-binding protein , pyridoxal-5'-phosphate phosphatase, and apoplipoprotein A-I levels were significantly decreased in MCAO group. These results suggest that cerebral ischemia induces neuronal cells death by changing expression levels of several proteins. Neurodegenerative disorders including Alzheimer's disease, Parkinson's disease and stroke are a major cause of adult disability and mortality. Among these disorders, stroke is a serious cerebrovascular disorder and the most common cause of death. A previous study demonstrated that cerebral ischemia in an experimental stroke model involves apoptotic and survival signaling pathways and leads to neuronal cells death [24]. Oxidative stress, metabolic compromise, and mitochondrial dysfunction may trigger neuronal apoptosis in neurodegenerative disorders [17]. The mechanisms of neuronal cell death are very complex and vague. At present, little is known about the changes in protein expression in damaged brain region during ischemic injury. The purpose of this study was to investigate these changes in expression in the cerebral cortex following ischemic brain injury. MATERIALS AND METHODSExperimental animals: Male Sprague-Dawley rats (225-250 g, n=40) were purchased from Samtako Co. (Animal Breeding Center, Osan, Korea) and were randomly divided into two groups, sham-operated group and middle cerebral artery occlusion (MCAO)-operated group (n=20 per group). Animals were maintained under controlled temperature (25C) and lighting (14L:10D), and allowed free access to food and water. All animal experiments were carried out in accordance with the Guide for care and use of laboratory animals, and use of Gyeongsang National University.Middle cerebral artery occlusion: The MCAO model was prepared following the previously described method of intra-luminal vascular occlusion [16]. Animals were anesthetized with sodium pentobarbital (100 mg/kg). The right common carotid artery, internal carotid artery, and external carotid artery were exposed through a midline cervical incision. A 4/0 monofilament nylon was inserted from the external carotid artery into the lumen of the internal carotid artery until it obstructed the origin of the middle cerebral artery. At ...

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“…1.4.3.5). 54,55 Structurally, aldehyde groups of PLP are bound covalently as internal aldimine (Schiff base)/imine linkage to the e-amine group of lysine residues, close to N-terminus 56 as in Fig. 11(a).…”

Section: Protein Oligomers Without Covalent Bondsmentioning

confidence: 99%

A review on protein oligomerization process

Liu

2015

Int. J. Precis. Eng. Manuf.

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Enzymes or proteins are commonly present in oligomeric forms for active biological functions. The formation of protein oligomers, either in nature or by artificial means, can take place via covalent bonding or through weak-bond-network associations. Disulfide bonds are more common in forming covalent protein oligomers. Covalent bound protein oligomers usually have additional elements introduced, while proteins associated through weak-bond-networks usually do not involve any additional bound chemical groups. Proteins are commonly present in stable forms or folds. Oligomerization can occur when stable proteins unfold, creating exposed interfaces for association interactions. One well-known process of weak-bond-network oligomerization is domain swapping (DS). Separating the two touching/interacting domains creates opportunities for similar interactions with different protein molecules, leading to oligomerization. Both disulfide bonding and DS oligomerization can be dynamic (or reversible) at least at low Degree of Polymerizations (DPs). The dynamic nature of the protein oligomerization is important for bioactivity control. The morpheein model and the polymorph model are thus important in quantifying enzyme catalyzed biotransformations. Disulfide bonding and DS can act together to form supramolecules. The formation of supramolecules, such as amyloids, in nature can be benign or harmful. Industrial applications of protein oligomerization exploit the special functions /properties of the resultant supramolecules, such as multiple biofunctions, niche structure, etc..

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Immunohistochemical studies of brain pyridoxine-5′-phosphate oxidase

Cited by 21 publications

References 32 publications

Chronic Cerebral Hypoperfusion Induced Synaptic Proteome Changes in the rat Cerebral Cortex

Chronic Cerebral Hypoperfusion Induced Synaptic Proteome Changes in the rat Cerebral Cortex

Proteomic Analysis of Focal Cerebral Ischemic Injury in Male Rats

A review on protein oligomerization process

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