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Notes: Abstract: Monoclonal antibodies against bovine brain succinic semialdehyde reductase were produced and characterized. A total of nine monoclonal antibodies recognizing different epitopes of the enzyme were obtained, of which two inhibited the enzyme activity and three stained cytosol of rat spinal cord neurons as observed by indirect immunofluorescence microscopy. When unfractionated total proteins of bovine brain homogenate were separated by gel electrophoresis and immunoblotted, the antibodies specifically recognized a single protein band of 34 kDa, which comigrates with purified bovine succinic semialdehyde reductase. Using the antisuccinic semialdehyde reductase antibodies as probes, we investigated the cross-reactivities of brain succinic semialdehyde reductases from some mammalian and an avian species. The immunoreactive bands on western blots appeared to be the same in molecular mass—34 kDa—in all animal species tested, including humans. The result indicates that brain succinic semialdehyde reductase is distinct from other aldehyde reductases and that mammalian brains contain only one succinic semialdehyde reductase. Moreover, the enzymes among the species are immunologically very similar, although some properties of the enzymes reported previously were different from one another.

Notes: Abstract: Two soluble forms of bovine brain glutamate dehydrogenase (GDH) isoproteins were inactivated by pyridoxal 5′-phosphate. Spectral evidence is presented to indicate that the inactivation proceeds through Schiff's base formation with amino groups of the enzyme. Sodium borohydride reduction of the pyridoxal 5′-phosphate-inactivated GDH isoproteins produced a stable pyridoxyl enzyme derivative that could not be reactivated by dialysis. The pyridoxyl enzyme was studied through fluorescence spectroscopy. No substrates or coenzymes separately gave complete protection against pyridoxal 5′-phosphate. A combination of 10 mM 2-oxoglutarate with 2 mM NADH, however, gave complete protection against the inactivation. Tryptic peptides of the isoproteins, modified with and without protection, resulted in a selective modification of one lysine. In both GDH isoproteins, the sequences of the peptide containing the phosphopyridoxyllysine were clearly identical to sequences of other GDH species.

Notes: Abstract: The structural differences between two types of glutamate dehydrogenase (GDH) isoproteins (GDH I and GDH II), homogeneously isolated from bovine brain, were investigated using a biosensor technology and monoclonal antibodies. A total of seven monoclonal antibodies raised against GDH II were produced, and the antibodies recognized a single protein band that comigrates with purified GDH II on sodium dodecyl sulfatepolyacrylamide gel electrophoresis and immunoblot. Of seven anti-GDH II monoclonal antibodies tested in the immunoblot analysis, all seven antibodies interacted with GDH II, whereas only four antibodies recognized the protein band of the other GDH isoprotein, GDH I. When inhibition tests of the GDH isoproteins were performed with the seven anti-GDH II monoclonal antibodies, three antibodies inhibited GDH II activity, whereas only one antibody inhibited GDH i activity. The binding affinity of anti-GDH II monoclonal antibodies for GDH II (KD= 1.0 nM) determined using a biosensor technology (Pharmacia BIAcore) was fivefold higher than for GDH I (KD= 5.3 nM), These results, together with epitope mapping analysis, suggest that there may be structural differences between the two GDH isoproteins, in addition to their different biochemical properties. Using the anti-GDH II antibodies as probes, we also investigated the crossreactivities of brain GDHs from some mammalian and an avian species, showing that the mammalian brain GDH enzymes are related immunologically to each other.

Notes: A 20-year-old Korean woman presented in August 1999 with a 3-month history of multiple, tiny papules on the periorbital and malar areas (〈link href="#f14431"〉Fig. 1a). She had noted hyperhidrosis for the preceding 6 months, even at room temperature. She had been well and had received no medication prior to her first visit to our clinic. Physical examination showed yellow colored, translucent, small papules, as well as finger tremor, exophthalmos, and a goiter. Histologic examination demonstrated cystic structures in the dermis lined with two layers of cuboidal epithelial cells (〈link href="#f14432"〉Fig. 2). The epidermis was normal and the rete ridges were partially effaced. Immunohistochemical studies revealed that the epithelial cells of the cyst wall were carcinoembryonic antigen (CEA) positive but S-100 protein negative.〈figure xml:id="f14431"〉1〈mediaResource alt="image" href="urn:x-wiley:00119059:IJD1443_5:IJD_1443_f1"/〉Multiple tiny papules on the periorbital and malar areas before (a) and after (b) treatment for Graves’ disease〈figure xml:id="f14432"〉2〈mediaResource alt="image" href="urn:x-wiley:00119059:IJD1443_5:IJD_1443_f2"/〉Staining with hematoxylin and eosin (× 100); (b) Staining with hematoxylin and eosin (× 200); (c) CEA-positive epithelial cells; (d) S-100 protein-negative epithelial cellsBecause a goiter and finger tremor were noted on physical examination, hyperthyroidism was suspected. Thyroid function test results were: triiodothyronine (T3), 8.0 ng/mL (normal range, 0.7–1.9 ng/mL); free thyroxine (T4), 8.1 ng/mL (0.7–1.9 ng/mL); T4, 35 µg/dL (6.0–11.8 µg/dL); thyroid-stimulating hormone (TSH), 0.04 IU/mL (0.25–4.0 IU/mL); positive for anti-TSH receptor antibody. On the basis of these findings, the patient was diagnosed with Graves’ disease and treated with methimazole, 40 mg/day. As the patient's symptoms improved, the therapeutic dose was decreased to 20 mg/day. Four months after the beginning of treatment, the free T4 and T3 values had returned to the normal range (〈link href="#t14431"〉Table 1). The skin lesions, finger tremor, and hyperhidrosis had also disappeared. Exophthalmos was improved, but still present (〈link href="#f14431"〉Fig. 1b).〈tabular xml:id="t14431"〉1〈title type="main"〉 Comparison of thyroid hormone values in Graves’ disease pretreatment and post-treatment 〈table frame="topbot"〉〈tgroup cols="3" align="left"〉〈colspec colnum="1" colname="col1"/〉〈colspec colnum="2" colname="col2" align="char" char="."/〉〈colspec colnum="3" colname="col3" align="char" char="."/〉〈thead valign="bottom"〉 T3 (ng/mL) Free T4 (ng/mL) 〈tbody valign="top"〉Pretreatment8.08.1Post-treatment1.00.15〈note xml:id="t14431_note3" numbered="no"〉T3, triiodothyronine; T4, thyroxine.

Notes: A 43-year-old man presented with a 1-month history of a nodule on the left side of the neck. There were no subjective symptoms. He denied any history of trauma.On physical examination, a round, soft, and movable subcutaneous nodule, approximately 1 cm in size, was detected. The overlying skin was normal.The nodule was observed to be attached to the wall of the external jugular vein during biopsy. On histopathologic examination, attachment to the external jugular vein was noted to be via a fibrovascular stalk ( 〈link href="#f3-1"〉Fig. 1a), and a lobular proliferation of capillaries, some of which were embedded in a fibromyxoid stroma, was observed ( 〈link href="#f3-1"〉Fig. 1b). There were no atypical cells, and a sparse inflammatory cell infiltrate was seen. The endothelial cells of the capillaries were CD31 positive ( 〈link href="#f3-1"〉Fig. 1c).〈figure xml:id="f3-1"〉1〈mediaResource alt="image" href="urn:x-wiley:00119059:IJD1067-4:ijd1067.f3-1"/〉(a)  Nodule attached to the wall of the vein (hematoxylin and eosin, × 10). (b)  A lobular proliferation of capillaries, some of which are embedded in a fibromyxoid stroma (hematoxylin and eosin, × 40). (c)  CD31 positivity (× 200)

Notes: [Auszug] Amyloid plaque is the hallmark and primary cause of Alzheimer disease. Mutations of presenilin-1, the γ-secretase catalytic subunit, can affect amyloid-β (Aβ) production and Alzheimer disease pathogenesis. However, it is largely unknown whether and how γ-secretase activity and ...

Notes: To induce fine engineered domain configurations into potassium niobate (KNbO3) single crystals, two kindsof methods were performed, i.e., (1) high DC electric field exposure along the opposite direction ofpolarization of KNbO3 single-domain crystals at room temperature, and (2) introduction of randomlyoriented fine domain configuration by heat treatment at 700 ˚C and then high DC electric field exposurealong [001]c direction of KNbO3 multidomain crystals at room temperature. When the method (1) wasperformed, finally, the poled KNbO3 crystals became to single-domain state again through the formation ofmultidomain state. On the other hand, the KNbO3 multidomain crystals were obtained by using the method(2), and an enhancement of piezoelectric-related properties was observed