Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Projections from the medial (MSO) and lateral (LSO) superior olivary nuclei to the inferior colliculus (IC) were examined in the mole. In each mole, Fluoro-Gold was injected into one IC and wheat germ-agglutinated horseradish peroxidase (WGA-HRP) into the other IC; most MSO neurons were double-labeled bilaterally, while most LSO neurons were single-labeled bilaterally. The results indicate that the bilateral projections from the MSO and LSO to the IC are mainly established by single MSO neurons with axon collaterals to the IC on both sides, and by two separate populations of LSO neurons with axons to the contralateral or ipsilateral IC.
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PMID:Differential organization of crossed and uncrossed projections from the superior olive to the inferior colliculus in the mole. 170 16

A mouse monoclonal antibody, FKH1, was produced to detect cytoplasmic melanoma-associated antigen. FKH1 was raised using cultured human melanoma cell line KHm-6 as immunogen. Reactivity of this antibody was assessed by immunohistochemical techniques. Positive reactions were seen against 5 human melanoma cell lines and cultured human epidermal melanocyte. It stained cytoplasm of melanoma cells in a diffuse and granular pattern with indirect immunofluorescence. Immunoelectron microscopy showed diffuse distribution of immuno-reactant in the cytoplasm of KHm-1 cells excluding melanosomes and other subcellular organelles. In immunoblotting, FKH1 bound with proteins having molecular weight of 71 kd and 55 kd extracted from KHm-6 cells. Reactivity against frozen and alcohol-fixed paraffin-embedded melanocytic tumors was also tested with indirect immunofluorescence or ABC (avidin biotin peroxidase complex) techniques. All cases of frozen sections from benign and malignant melanocytic tumors including 2 cases of amelanotic melanoma showed positive staining with FKH1. In fixed tissues, reactivity was 16/19 (84.2%) in malignant melanoma and 30/44 (68.2%) in other melanocytic tumors. FKH1 did not react against normal melanocytes, C-type nevus cell, intradermal nevus pigmentosus with neuroid structure and neurofibroma. It was demonstrated that FKH1 recognized proliferative melanocytes originated from melanoblast or melanoblastic nevoblast. FKH1 failed to stain normal human peripheral nerves and nonmelanocytic tumors except APUDoma and malignant Merkel cell tumor. In halo nevus, nevus cells were clearly distinguished from intermingling inflammatory cell infiltrate. It was suggested that FKH1 is a useful monoclonal antibody in diagnosing human malignant melanoma, particularly in evaluating tumor thickness of Breslow more precisely.
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PMID:[Mouse monoclonal antibody (FKH1) detecting human melanoma-associated antigens: production, partial characterization and immunohistochemical analysis]. 188 56

The mechanism of NADPH oxidation catalyzed by horse-radish peroxidase (HRP) and 2,4-diacetyl-[2H]heme-substituted horse-radish peroxidase (DHRP) was studied. The roles of the different H2O2/peroxidase compounds were examined by spectral studies. The oxidized NADPH species were identified using the superoxide dismutase effect and by measuring the stoichiometry between NADPH oxidized and H2O2 used. In the presence of a mediating molecule, like scopoletin, both enzymes acted via a similar mechanism, producing only NADP degrees, which in turn reacted with O2 producing O2-. Consequently H2O2 was completely regenerated in the presence of superoxide dismutase and partially regenerated in its absence. In the absence of a mediating molecule, the H2O2 complex of both enzymes (compound I) catalysed NADPH oxidation by single-electron transfer, producing NADP degrees; compound II of these enzymes catalyzed NADPH oxidation more slowly by a direct two-electron transfer, producing NADPH+. There were difference between HRP and DHRP. HRP compound II was produced by the oxidation of 1 mol NADPH/mole compound I, while DHRP compound II was formed by the spontaneous conversion of compound I to compound II. The NADPH oxidation catalyzed by DHRP compound I did not lead to the formation of compound II. When H2O2 was produced slowly by the glucose/glucose-oxidase system, compound II was never formed and a pure O2- adduct of DHRP (compound III) accumulated.
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PMID:Mechanism of NADPH oxidation catalyzed by horse-radish peroxidase and 2,4-diacetyl-[2H]heme-substituted horse-radish peroxidase. 193 47

The mole rat Spalax ehrenbergi is a fossorial rodent. Although its peripheral visual system--eye and optic nerve--is highly degenerated, it shows some sensitivity to light. However, in the usual sense, it is essentially blind. An auditory take-over of the visual lateral geniculate nucleus and at least part of the visual cortices was recently demonstrated. In order to visualize the retinal projections during ontogeny, we used an anterograde tracing technique, with monocular injection of wheat germ agglutinin-labeled horseradish peroxidase (WGA-HRP). In the newborn mole rat the retina projects to most of its normal targets as compared with seeing rodents, with bilateral projections to the suprachiasmatic nuclei, the dorsal and ventral lateral geniculate nuclei, the lateroposterior nuclei, the optic tract nuclei and the superior colliculi. During the course of ontogeny, the retinohypothalamic connection is stabilized but the main optic tract undergoes progressive degeneration. In adults, only a few retinal fibers enter the contralateral ventral lateral geniculate nucleus, the lateroposterior nucleus, the optic tract nucleus and the superior colliculus. No retinal fibers could be detected in the dorsal lateral geniculate nucleus. Thus, the retinofugal projections in the adult mole rat could explain its reduced sensitivity to light, whereas the complete degeneration of the retino-dorsal lateral geniculate nucleus projection could underlie the invasion of auditory input into this normally visual center.
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PMID:Retinal projections in the blind mole rat: a WGA-HRP tracing study of a natural degeneration. 202 63

Conformational changes of peroxidase and albumin in buffered solutions of propylthiouracil, an antithyroid drug, were evaluated by dialtometry and viscometry, showing that the structural alteration of peroxidase is related to the decoupling of the reactions which it catalyses. Thus, propylthiouracil probably inactivates the peroxidase by altering its structure. Equilibrium dialysis showed that albumin is the principle propylthiouracil-transporting protein in human serum. Propylthiouracil induces a conformational change in albumin when 1 mole of drug per mole of protein is bound, a structural alteration that can change the binding capability of other ligands.
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PMID:Conformational changes of peroxidase and albumin in solutions of propylthiouracil. 216 15

Anatomical organization of the central auditory system in the mole was studied at the lower brainstem levels. The cyto-, myelo-, and chemoarchitectures were examined in Nissl, myelin, and acetylcholinesterase stained materials, and then the origins of the ascending afferents to the inferior colliculus (IC) were identified by injecting wheatgerm agglutinin conjugated to horseradish peroxidase (WGA-HRP) into the unilateral IC and processing the tissue according to the standard retrograde tracing techniques. The results indicate that the auditory nuclei and pathways in the lower brainstem of the mole conform to the basic plan common to many other mammals. Nevertheless, several characteristic features are evidenced in the present study: (1) in the cochlear nucleus (CochN), granule cell fields are very large in both the ventral (VCN) and dorsal (DCN) nuclei; among several populations of neurons, fusiform cells in the DCN, multipolar cells in the VCN and DCN, and small spherical cells in the VCN project to the IC directly, (2) in the superior olivary complex (SOC), the medial nucleus (MSO) is well developed in comparison with that in the hedgehog, the opossum, the mouse, and the rat, although the general configuration of the SOC is similar to that in those mammals, most strikingly, the MSO projects to the IC bilaterally in the mole, and (3) the nuclei of the lateral lemniscus (NLL) show a great development and consist of three well-differentiated parts of the dorsal, intermediate, and ventral nuclei. The projections from these subnuclei to the IC conform to the basic mammalian plan.
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PMID:Auditory brainstem in the mole (Mogera): nuclear configurations and the projections to the inferior colliculus. 222 72

A new immunohistochemical assay was developed for the detection of human monoclonal antibody (HuMAb) bound to human biopsied tumor tissues. A murine anti-idiotype monoclonal antibody, alpha type, 18C6 (IgGl), was raised against an IgM HuMAb, L612, defining a tumor-associated ganglioside antigen (GM3) and used as a probe in a three step cell-binding assay (HuMAb + anti-id + biotinylated anti-mouse Ig). Anti-id 18C6 has an exclusive binding specificity for HuMAb L612, but does not interfere with the binding of L612 to antigen positive melanoma cell lines or to a purified antigen, GM3. The applicability of 18C6 in the three step cell-binding assay was tested first using a melanoma cell line, UCLASO-M12. L612 bound to M12 cells was specifically detected by 18C6 without any background reactivity in ELISA. When this assay was compared with the standard two-step cell-binding assay (HuMAb + peroxidase-conjugated anti-human IgM) using various cultured tumor cell lines, parallel reactivity was observed. The three-step cell-binding assay was then applied to various fresh-frozen human tumor sections. Positive reactivity was demonstrated on various histologic types of human tumor tissues: primary melanoma (10/10), metastatic melanoma (4/4), nevus (10/10), lung cancer (3/6), breast cancer (2/6), and colon cancer (1/1). Adjacent normal tissues were unstained. Control experiments included the cell-binding assay with L612 alone, 18C6 alone. L612 + unrelated mouse IgG, and unrelated IgM HuMAb (L72) + 18C6; but biotinylated anti-mouse IgG did not react with these control preparations. The results indicate that anti-id 18C6 is a highly specific probe to assess the expression of the ganglioside antigenic epitope recognized by the L612 HuMAb on biopsied human tumor tissues.
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PMID:Murine monoclonal anti-idiotype antibody (alpha) as a probe to detect human monoclonal antibody bound to human tumor tissues. 223 Jan 46

A retrograde tracing study in the mole using wheat germ-agglutinated horseradish peroxidase (WGA-HRP) indicated that the medial superior olivary nucleus (MSO) projects to the inferior colliculus (IC) bilaterally. Considering the strict ipsilateral projections from the MSO to the IC in all other eutherian species ever reported, the bilateral projection in the mole is quite unique. This may reflect specializations of the peripheral auditory apparatus of the underground dwellers and/or primitiveness of the insectivorous brains.
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PMID:Bilateral projections from the medial superior olivary nucleus to the inferior colliculus in the mole (Mogera robusta). 246 89

To study tumor-associated antigens that are immunogenic to humans, we have generated human monoclonal antibodies by fusing lymph node lymphocytes of a melanoma patient with a mouse myeloma cell line. We examined in detail the reactivity of one IgG antibody, termed 2-139-1. Immunostaining was performed with purified antibody conjugated to biotin. Binding was visualized by the avidin-biotin-peroxidase complex. With cultured cells, 2-139-1 stained 12 of 12 melanomas and 12 of 16 carcinomas. Reactivity was not detectable in seven neural crest tumors, six sarcomas, and 45 lymphomas and leukemias. This spectrum of reactivity was confirmed with sections of human tissues. The human monoclonal antibody 2-139-1 reacted against melanomas and not banal nevi. While the antibody reacted strongly to adenocarcinomas of the colon, prostate, rectum, and pancreas, it did not stain all the carcinomas tested. Furthermore, reactivity was not seen against sarcomas. Interestingly, 2-139-1 did not bind to the majority of the cells in normal tissues, including fetal tissues. The reactivity of 2-139-1 may be representative of the humoral immune response found in the regional lymph nodes of cancer patients. The distribution of this epitope in various tumors was fairly limited and appeared to be associated with malignant transformation.
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PMID:Tumor-reactive human immunoglobulin G monoclonal antibody from a melanoma patient. 247 81

A light microscopic analysis of lectin receptors in normal placenta and trophoblastic disease was performed utilizing biotinylated Concanavalin-A (Con-A), wheat germ agglutinin (WGA), and peanut agglutinin (PNA), in conjunction with an avidin-biotin peroxidase complex. Hydatidiform mole, invasive mole and choriocarcinoma exhibited increased receptors to Con-A and WGA compared to normal placenta. Increased reactivity to Con-A and WGA was associated merely with increased growth and proliferation of trophoblasts rather than a malignant transformation. Normal placenta, partial and complete mole generally showed moderate to strong binding with PNA after neuraminidase treatment, while invasive mole and choriocarcinoma (11 of 15 cases) generally showed minimal to absent reaction with PNA. Heterogeneity of PNA binding in choriocarcinoma was manifested by the presence of PNA reactivity in the trophoblast membrane in 2 cases wherein no prior neuraminidase treatment was given. This suggests that in some malignant trophoblasts, there is absence of sialic acid in the terminal cell surface carbohydrate groups resulting in the exposure of N-acetylgalactoseamine.
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PMID:Lectin binding in tissues from hydatidiform mole, invasive mole and choriocarcinoma to concanavalin-A, wheat germ agglutinin and peanut agglutinin. 256 Mar 69


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