Brief communicationPeripheral benzodiazepine binding sites in Alzheimer's disease frontal and temporal cortex
References (40)
- et al.
Autoradiographic localization of peripheral benzodiazepine binding sites in the cat brain with [3H]PK 11195
Brain Res. Bull.
(1984) - et al.
Peripheral type benzodiazepine binding sites are a more sensitive index of excitotoxic lesions of the rat striatum than the neuronal marker enzymes choline acetyltransferase or glutamate decar☐ylase
Brain Res.
(1987) - et al.
Short and long term effects of the excitotoxin, quinolinic acid, as evidenced by GFA immunohistochemistry of astrocytes
Brain Res.
(1986) - et al.
Pathological changes in the nucleus of Meynert in Alzheimer's and Parkinson's diseases
J. Neurol. Sci.
(1983) - et al.
Imaging of primary and remote ischaemic and excitotoxic brain lesions
- et al.
Peripheral benzodiazepine binding sites: effect of PK 11195, 1-(2-chlorophenyl)-N-methyl-N-(methylpropyl)-3-isoquiisoquinoline-car☐amide
Life Sci.
(1983) - et al.
Protein measurement with pholin phenol reagent
J. Biol. Chem.
(1951) - et al.
[3H]Ro5-4864 and [3H]Ro5-4864 binding in kainate-lesioned rat striatum and temporal cortex of brains from patients with senile dementia of the Alzheimer type
Brain Res.
(1983) - et al.
Specific high affinity binding of [3h]Ro5-4864 to benzodiazepine binding sites in the rat cerebral cortex
Eur. J. Pharmacol.
(1981) - et al.
[3H]Ro5-4864 benzodiazepine binding in kainate lesioned striatum and Huntington's diseased basal ganglia
Brain Res.
(1982)
Huntington's disease: changes in striatal proteins reflect astrocytic gliosis
Brain Res.
Neurofibrillary tangles and pathogenesis of dementia: a quantitative study
Neuropathol. Appl. Neurobiol.
Labelling of “peripheral type” benzodiazepine receptors in the rat using [3H]PK 11195, an isoquinoline car☐amide derivative
Imaging of human brain lesions with a W3 site radioligand
Ann. Neurol.
Flunitrazepam binding to intact and homogenized astrocytes and neurons in primary culture
J. Neurochem.
Imaging of brain tumors using peripheral benzodiazepine receptor ligands
J. Neurosurg.
Specific benzodiazepine receptors in rat brain characterized by high affinity [3H]diazepam binding
Peripheral type benzodiazepine receptors in the living heart characterized by positron emission tomography
Circulation
In vivo imaging of rat C6 gliomas by [125I]-iodinated benzodiazepines and isoquinolines
Soc. Neurosci. Abstr.
Altered expression of neuronal messenger RNA in Alzheimer cortex
Cited by (109)
Neuroimaging biomarkers of glial activation for predicting the annual cognitive function decline in patients with Alzheimer's disease
2023, Brain, Behavior, and ImmunityTSPO in diverse CNS pathologies and psychiatric disease: A critical review and a way forward
2019, Pharmacology and TherapeuticsCitation Excerpt :The use of the non-benzodiazepine isoquinoline carboxamide PK11195 (initial studies used the R,S-racemic form and later studies used the active R-enantiomer) and the GABAa receptor non-active derivative of diazepam Ro5–4864 (4′-chlorodiazepam) as selective ligands for PBR with no affinity for the CBR facilitated the characterization of brain PBR binding sites. Early studies using different models of brain injury and neurodegeneration indicated that PBR levels measured by [3H]PK11195 and [3H]Ro5–4864 specific binding increased markedly at primary and secondary sites of brain injury (Benavides et al., 1988; Benavides et al., 1990; Benavides et al., 1987; Diorio et al., 1991; Doble et al., 1987; Dubois et al., 1988; Gehlert et al., 1985; Guilarte et al., 1995; Miyazawa et al., 1995) and these studies provided the first description of PBR's association with gliosis in animal models of brain injury (Benavides et al., 1990; Diorio et al., 1991; Dubois et al., 1988; Guilarte et al., 1995; Miyazawa et al., 1995). Despite the fact that the name PBR was used for many years, it was misleading since it was not an exclusively “peripheral” organ protein nor was it a receptor in the classical sense of neurotransmitter receptors.
Metal complexes targeting the Translocator Protein 18 kDa (TSPO)
2017, Coordination Chemistry ReviewsCitation Excerpt :Interestingly, TSPO is overexpressed in a variety of tumors (e.g., certain brain tumors, ovarian cancer, liver tumors, breast carcinoma, colorectal cancer, etc.) and its expression appears to be related to the degree of tumor malignancy [13–16]. In addition, TSPO is overexpressed on activated microglial cells localized in lesioned brain areas of patients with neurodegenerative or neuroinflammatory diseases like Alzheimer’s disease, Huntington’s disease, and multiple sclerosis [17,18]. Thus, TSPO has become an extremely attractive subcellular target not only to image but also to treat diseases overexpressing this protein (theranostic drugs combine in a single molecule the two functions i.e. they act both as a diagnostic and a therapeutic agent).
Synthesis of [<sup>11</sup>C]PBR170, a novel imidazopyridine, for imaging the translocator protein with PET
2014, Applied Radiation and IsotopesThe impact of oxidative stress in thiamine deficiency: A multifactorial targeting issue
2013, Neurochemistry InternationalCitation Excerpt :In addition, an important use for TSPO has been demonstrated in the imaging of inflammatory processes in various neurological disorders in humans (Cagnin et al., 2001; Gerhard et al., 2003; Ouchi et al., 2009) with PET. Increased binding of PK11195, a highly selective ligand for the TSPO was earlier demonstrated in post mortem brain tissue from patients with AD (Owen et al., 1983; Diorio et al., 1991), HD (Schoemaker et al., 1982), and cerebral ischemia (Myers et al., 1991) in which both gliosis and neuronal cell loss occur. This led to the postulate that TSPOs may also provide a reliable index of neuronal loss in such disorders (Benavides et al., 1987).
- 1
Dr. Sharon A. Welner, Douglas Hospital Research Centre, 6875 LaSalle Blvd., Verdun, Quebec, Canada, H4H 1R3.