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1.
AJNR Am J Neuroradiol ; 43(6): 893-898, 2022 06.
Article in English | MEDLINE | ID: mdl-35550283

ABSTRACT

BACKGROUND AND PURPOSE: In patients with ischemic stroke, DWI lesions can occasionally be reversed by reperfusion therapy. This study aimed to ascertain the relationship between ADC levels and DWI reversal in patients with acute ischemic stroke who underwent recanalization treatment. MATERIALS AND METHODS: We conducted a retrospective cohort study in patients with acute ischemic stroke who underwent endovascular mechanical thrombectomy with successful recanalization between April 2017 and March 2021. DWI reversal was assessed through follow-up MR imaging approximately 24 hours after treatment. RESULTS: In total, 118 patients were included. DWI reversal was confirmed in 42 patients. The ADC level in patients with reversal was significantly higher than that in patients without reversal. Eighty-three percent of patients with DWI reversal areas had mean ADC levels of ≥520 × 10-6 mm2/s, and 71% of patients without DWI reversal areas had mean ADC levels of <520 × 10-6 mm2/s. The mean ADC threshold was 520 × 10-6 mm2/s with a sensitivity and specificity of 71% and 83%, respectively. In multivariate analysis, the mean ADC level (OR, 1.023; 95% CI, 1.013-1.033; P < .0001) was independently associated with DWI reversal. Patients with DWI reversal areas had earlier neurologic improvement (NIHSS at 7 days) than patients without reversal areas (P < .0001). CONCLUSIONS: In acute ischemic stroke, the ADC value is independently associated with DWI reversal. Lesions with a mean ADC of ≥520 × 10-6 mm2/s are salvageable by mechanical thrombectomy, and DWI reversal areas regain neurologic function. The ADC value is easily assessed and is a useful tool to predict viable lesions.


Subject(s)
Brain Ischemia , Ischemic Stroke , Stroke , Brain Ischemia/complications , Brain Ischemia/diagnostic imaging , Brain Ischemia/surgery , Diffusion Magnetic Resonance Imaging , Humans , Ischemic Stroke/diagnostic imaging , Ischemic Stroke/surgery , Retrospective Studies , Stroke/complications , Stroke/diagnostic imaging , Stroke/surgery , Thrombectomy
2.
Intern Med ; 38(5): 407-11, 1999 May.
Article in English | MEDLINE | ID: mdl-10397077

ABSTRACT

This study was performed to confirm 1) the difference in the trinucleotide CAG repeat number among tissues, 2) somatic mosaicism in each tissue, 3) the correlation of the repeat number with pathological severity in Huntington's disease. The CAG repeat number was determined by analysis of the polymerase chain reaction (PCR) product in various tissues, including central nervous system (CNS) tissues and non-CNS tissues. We also determined the pathological severity grade in each brain section and compared this with the results of CAG repeat analyses. The patient was a Japanese male with Huntington's disease who died at 62 years of age. Genomic DNA was extracted from 10 parts of the central nervous system and 6 parts of other tissues from the patient. Each part of the formalin-fixed brain was subjected to gross and microscopic pathological assessment. The main peaks of CAG repeat in all tissues were 22 and 44. In analysis of somatic mosaicism, high degrees of mosaicism were obtained in the caudate nucleus, putamen and cerebral cortex, in which more severe degeneration was observed by pathological examination. These results, although this is a single case study, indicated that pathological severity did not correlate with the CAG repeat number, but it did relate to the degree of somatic mosaicism. Somatic mosaicism might reflect region-specific neuronal degeneration in Huntington's disease.


Subject(s)
DNA/analysis , Huntington Disease/genetics , Trinucleotide Repeats/genetics , Brain/pathology , Brain Chemistry , DNA Primers/chemistry , Humans , Huntington Disease/pathology , Male , Middle Aged , Mosaicism/genetics , Polymerase Chain Reaction
3.
J Biol Chem ; 266(30): 20218-22, 1991 Oct 25.
Article in English | MEDLINE | ID: mdl-1718959

ABSTRACT

Basic amphipathic alpha-helical peptides Ac-(Leu-Ala-Arg-Leu)3 or 4-NHCH3 (4(3) or 4(4)) and H-(Leu-Ala-Arg-Leu)3-(Leu-Arg-Ala-Leu)2 or 3-OH (4(5) or 4(6)) were synthesized and studied in terms of their interactions with phospholipid membranes, biological activity, and ion channel-forming ability. CD study of the peptides showed that they form alpha-helical structures in the presence of phospholipid liposomes and thus they have amphipathic distribution of the side chains along the axis of the helix. A leakage study of carboxyfluorescein encapsulated in phospholipid vesicles indicated that the peptides possess a highly potent ability to perturb the membrane structure. Membrane current measurements using the planar lipid bilayer technique revealed that the peptide 4(6), which was long enough to span the lipid bilayer in the alpha-helical structure, formed cation-selective ion channels at a concentration of 0.5 microM in a planar diphytanoylphosphatidylcholine bilayer. In contrast, other shorter peptides failed to form discrete and stable channels though they occasionally induced an increase in the membrane current with erratic conductance levels. The probability of detecting a conductance increase was in the order of 4(6) greater than 4(5) greater than 4(4) greater than 4(3), which corresponds to the order of the peptide chain lengths. Furthermore, 4(6) but not 4(5) showed an antimicrobial activity against both Gram-positive and -negative bacteria. The structure of ion channels formed by 4(6) and the relationship between the peptide chain length and biological activity of the synthetic peptides are discussed.


Subject(s)
Anti-Bacterial Agents , Ion Channels/metabolism , Lipid Bilayers , Peptides/chemistry , Phospholipids/metabolism , Amino Acid Sequence , Circular Dichroism , Fluoresceins/chemistry , Liposomes , Membrane Potentials , Molecular Sequence Data , Peptides/pharmacology , Protein Conformation
4.
Biochim Biophys Acta ; 1063(2): 191-6, 1991 Apr 02.
Article in English | MEDLINE | ID: mdl-2012817

ABSTRACT

In order to investigate the conformation and orientation of lipid-bound peptides and proteins in the lipid bilayer, basic amphipathic alpha-helical peptides with a long alkyl chain, palmitoyl-(Leu-Ala-Arg-Leu)3-NHCH3 (P-4(3)) and Ac-Leu-Ala-Arg-Leu-Trp-Amy-Arg-Leu-Leu-Ala-Arg-Leu-NHCH3 (Amy-4(3), Amy; alpha-aminomyristic acid) were designed and synthesized. The conformational features and spectroscopic behavior in a buffer solution and in neutral and acidic liposomes were studied by CD, dye-leakage, and fluorescence measurements. The CD data indicated that P-4(3) took an alpha-helical structure in aqueous solution and in neutral and acidic liposomes. On the other hand, Amy-4(3) took a beta-structure in aqueous solution and an alpha-helical structure in neutral and acidic liposomes. The conformational change of Amy-4(3) was confirmed by fluorescence study on lipid titration of the peptide. The dye-leakage experiment showed that both peptides interacted with acidic liposomes to perturb them, but less effectively than Ac-(Leu-Ala-Arg-Leu)3-NHCH3 (4(3)) which has no long alkyl group. Based on these results, a discussion is made concerning the conformation and orientation of peptides in aqueous solution and in the lipid bilayer.


Subject(s)
Amino Acids/chemistry , Lipid Bilayers , Liposomes/metabolism , Peptides/chemistry , Amino Acid Sequence , Circular Dichroism , Molecular Sequence Data , Protein Conformation , Spectrometry, Fluorescence
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