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Search results for: CD156

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#33973283   2021/05/10 To Up

Leptomeningeal and intraventricular myelomatosis manifesting an aggressive form of communicating hydrocephalus.

Leptomeningeal myelomatosis (LMM) is a fatal complication that occurs in < 1% of patients with multiple myeloma. Many patients with LMM present with neurologic symptoms referable to cranial neuropathies, while the manifestation of communicating hydrocephalus has been underrecognized. A Japanese man with Bence Jones protein-κ multiple myeloma developed fever and headache at age 54 years. He then became somnolent and went into a coma. Neuroimaging analyses identified rapidly progressive communicating hydrocephalus due to meningitis. He died 83 days after the onset of headache without any response to treatment at age 55 years. No symptoms or signs associated with cranial nerves were found during the course of illness. Postmortem examination revealed hydrocephalus and diffuse infiltration of myeloma cells into the subarachnoid space of the cerebrum, cerebellum, and brainstem. In addition, the interstitial tissue of the choroid plexuses was filled with myeloma cells. These myeloma cells were positive for CD156 and light chain κ. The Ki-67 labeling index in myeloma cells of the central nervous system (CNS) was 30-40%. Histopathological examination further revealed many myeloma cells on the surface of the lateral, third and fourth ventricles and at the area postrema of the medulla oblongata. Patients with LMM can develop an aggressive form of communicating hydrocephalus. Given that cerebrospinal fluid, produced by epithelial cells in the choroid plexuses of the ventricles, passes into the subarachnoid space through the third and fourth ventricles, myeloma cells may invade the CNS through the choroid plexuses.
Yasuo Miki, Kosuke Kamata, Yui Akemoto, Fumiyasu Tsushima, Hirotake Sakuraba, Kazufumi Yamagata, Akira Kurose, Shinsaku Fukuda, Koichi Wakabayashi

1667 related Products with: Leptomeningeal and intraventricular myelomatosis manifesting an aggressive form of communicating hydrocephalus.

1 mg100μg96 Tests1,000 tests100.00 ul100 mg1000 tests200 100ug100ug500 MG

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#19373511   2009/04/17 To Up

Upregulation of ADAM8 in the airways of mice with allergic bronchial asthma.

Recent microarray analyses revealed that a disintegrin and metalloproteinase (ADAM) 8 (ADAM8; also called CD156) is one of the asthma candidate genes. However, the function of ADAM8 and its localization in the airways are still poorly understood. In the present study, the changes in the expression and localization of ADAM8 in the airways of a mouse model of allergic bronchial asthma were investigated. Male BALB/c mice were sensitized and repeatedly challenged with ovalbumin antigen to induce asthmatic response. After the final antigen challenge, mRNA and protein expressions of ADAM8 were elucidated by quantitative RT-PCR and immunohistochemistry. The mRNA expression of ADAM8 in the airways was significantly increased in this animal model of asthma compared with naive animals. Immunohistochemical examinations revealed that ADAM8 was located in airway epithelia, airway smooth muscles, and infiltrated cells (mainly macrophages) into lung parenchyma. A distinctly stronger immunostaining of ADAM8 was observed in these airway cells of the repeatedly antigen-challenged mice compared with those of the sensitized control animals. An upregulation of ADAM8 in the airways might be involved in the pathogenesis of airway inflammation and/or hyperresponsiveness, characteristic features of allergic bronchial asthma.
Yoshihiko Chiba, Satoshi Onoda, Yoshiyuki Hattori, Yoshie Maitani, Hiroyasu Sakai, Miwa Misawa

1569 related Products with: Upregulation of ADAM8 in the airways of mice with allergic bronchial asthma.

1ml1 5 G

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#19003792   // To Up

ADAM8 is selectively up-regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice.

Endothelial cell (EC) loss and subsequent angiogenesis occur over the first week after spinal cord injury (SCI). To identify molecular mechanisms that could be targeted with intravenous (i.v.) treatments, we determined whether transmembrane "a disintegrin and metalloprotease" (ADAM) proteins are expressed in ECs of the injured spinal cord. ADAMs bind to integrins, which are important for EC survival and angiogenesis. Female adult C57Bl/6 mice with a spinal cord contusion had progressively more ADAM8 (CD156) immunostaining in blood vessels and individual ECs between 1 and 28 days following injury. Uninjured spinal cords had little ADAM8 staining. The increase in ADAM8 mRNA and protein was confirmed in spinal cord lysates, and ADAM8 mRNA was present in FACS-enriched ECs. ADAM8 colocalized extensively and exclusively with the EC marker PECAM and also with i.v.-injected lectins. Intravenous isolectin B4 (IB4) labels a subpopulation of blood vessels at and within the injury epicenter 3-7 days after injury, coincident with angiogenesis. Both ADAM8 and the proliferation marker Ki-67 were present in IB4-positive microvessels. ADAM8-positive proliferating cells were seen at the leading end of IB4-positive blood vessels. Angiogenesis was confirmed by BrdU incorporation, binding of i.v.-injected nucleolin antibodies, and MT1-MMP immunostaining in a subset of blood vessels. These data suggest that ADAM8 is vascular selective and plays a role in proliferation and/or migration of ECs during angiogenesis following SCI.
Edward T Mahoney, Richard L Benton, Melissa A Maddie, Scott R Whittemore, Theo Hagg

1553 related Products with: ADAM8 is selectively up-regulated in endothelial cells and is associated with angiogenesis after spinal cord injury in adult mice.

100 μg100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#15978851   // To Up

Transposition of MINE, a composite retrotransposon, in the avirulence gene ACE1 of the rice blast fungus Magnaporthe grisea.

The ACE1 avirulence gene allele from the rice blast fungus Magnaporthe grisea was characterized in virulent isolate 2/0/3, revealing the insertion of a 1.9 kb MINE retrotransposon in the last ACE1 exon. MINE is a novel chimeric element composed of a transcribed non-coding sequence of 1.1 kb (WEIRD) fused to a 5'-truncated MGL retrotransposon. MINEs were found in high copy number in M. grisea isolates from rice (68 copies) and as a single copy in isolate CD156 from Eleusine. MINEs vary in size (1.3-6.7 kb) with conserved 5' WEIRD sequences and variable 3' MGL sequences. MGLs fused to WEIRDs correspond to different 5'-truncated MGLs with conserved 3' ends. The organization and diversity of MINEs suggest that these retrotransposons result from independent fusions between WEIRD and 5'-truncated MGLs. Such chimera could be formed during MGL reverse transcription as proposed for human U6-LINE1 chimeric retrotransposons and integrated into M. grisea genome using MGL machinery.
Isabelle Fudal, Heidi U Böhnert, Didier Tharreau, Marc-Henri Lebrun

1725 related Products with: Transposition of MINE, a composite retrotransposon, in the avirulence gene ACE1 of the rice blast fungus Magnaporthe grisea.

1100.00 ul1 ml 100ul

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#12415192   // To Up

CD156 transgenic mice. Different responses between inflammatory types.

CD156 (ADAM8) is part of the ADAM family of proteins with the catalytic site consensus sequence of metalloprotease and disintegrins. To examine the role of CD156 in vivo, we generated mutant CD156 (eCD156) transgenic mice expressing the ectodomain of CD156 under the control of the alpha1-antitrypsin (AT) promoter. One of the transgenic mice designated ATMS2-TG18 expressed a 1.84 kb mRNA which was predicted to be a truncated CD156. The expression of the transgenic CD156 mRNA in ATMS2-TG18 mice was abundant in the liver and slight in kidney. Turpentine oil (TO) and lipopolysaccharide (LPS) markedly upregulated the expression. Soluble CD156 (sCD156) was produced constitutively, and increased after the treatment with TO. Casein-induced peritoneal leukocyte infiltration was significantly less extensive in ATMS2-TG18 than non-transgenic mice. The expression of L-selectin in neutrophils (PMN) from peripheral blood leukocytes (PBL) was more strongly downregulated in ATMS2-TG18 than non-transgenic mice, suggesting that L-selectin in PMN from ATMS2-TG18 mice was shed by sCD156. In contrast, oxazolone (Ox)-induced contact hypersensitivity reactions (CHR) were more marked in ATMS2-TG18 than non-transgenic mice. The expression of E-selectin mRNA was detected in inflammatory skin sites from ATMS2-TG18, but not non-transgenic mice, suggesting that sCD156 may activate the endothelial cells and lead to the upregulation of E-selectin. These results suggest that CD156 regulates leukocyte infiltration directly or indirectly.
Yasunori Higuchi, Atsushi Yasui, Keiko Matsuura, Shunsuke Yamamoto

1300 related Products with: CD156 transgenic mice. Different responses between inflammatory types.

251 mg1mg0.15 mg50 ug100ug Lyophilized5ug

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#12135759   // To Up

The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs.

The ADAM family of proteases are type I transmembrane proteins with both metalloproteinase and disintegrin containing extracellular domains. ADAMs are implicated in the proteolytic processing of membrane-bound precursors and involved in modulating cell-cell and cell-matrix interactions. ADAM8 (MS2, CD156) has been identified in myeloid and B cells. In this report we demonstrate that soluble ADAM8 is an active metalloprotease in vitro and is able to hydrolyse myelin basic protein and a variety of peptide substrates based on the cleavage sites of membrane-bound cytokines, growth factors and receptors which are known to be processed by metalloproteinases. Interestingly, although ADAM8 was inhibited by a number of peptide analogue hydroxamate inhibitors, it was not inhibited by the tissue inhibitors of metalloproteinases (TIMPs). We also demonstrate that the activity of recombinant soluble ADAM9 (meltrin-gamma, MDC9) lacks inhibition by the TIMPs, but can be inhibited by hydroxamate inhibitors. The lack of TIMP inhibition of ADAM8 and 9 contrasts with other membrane-associated metalloproteinases characterised to date in this respect (ADAM10, 12, 17, and the membrane-type metalloproteinases) which have been implicated in protein processing at the cell surface.
Augustin Amour, C Graham Knight, William R English, Ailsa Webster, Patrick M Slocombe, Vera Knäuper, Andrew J P Docherty, J David Becherer, Carl P Blobel, Gillian Murphy

2962 related Products with: The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs.

100 assays0.1ml (1mg/ml)0.1ml (1mg/ml)100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100 ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#10354553   // To Up

ADAM family proteins in the immune system.

CD156 is a member of a family proteins characterized by a disintegrin and a metalloprotease domain (ADAM). These molecules are phylogenically conserved but have individual roles in a variety of cells. Here, Shunsuke Yamamoto and colleagues discuss data suggesting that ADAM family proteins have important roles in the immune system.
S Yamamoto, Y Higuchi, K Yoshiyama, E Shimizu, M Kataoka, N Hijiya, K Matsuura

2220 related Products with: ADAM family proteins in the immune system.

2 Pieces/Box1020 1 mg21000101mg101002

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#9218457   // To Up

Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location.

The murine cell surface antigen mCD156 is a glycoprotein that is expressed in monocytic cell lines and consists of a metalloprotease domain, a disintegrin domain, a cysteine-rich domain, and an epidermal growth factor-like domain in the extracellular region. The mCD156 gene is composed of 24 exons and 23 introns and spans approximately 14 kilobases. The first exon encodes most of the signal peptide sequence, and the transmembrane region is encoded by a single exon (19). In contrast, the other regions are composed of multiple exons. Of these, exons 7-12 and 12-15 encode a metalloprotease domain and a disintegrin domain, respectively. Sequence analysis of the 5'-flanking DNA revealed many potential regulatory motifs. Chloramphenicol acetyltransferase analysis demonstrated that nucleotides at positions -183, -334, and -623 contained cis-acting enhancing elements in a mouse monocytic cell line, aHINS-B3. Nucleotides at positions -183 and -390 contained elements responsible for lipopolysaccharide (LPS) inducibility, although several other 5'-flanking regions were also involved in LPS responsiveness. Regions -202, -507, and -659 play a role in interferon-gamma inducibility. Some of the potential regulatory motifs and other unknown cis elements may be involved in the constitutive expression, and LPS and interferon-gamma inducibilities. The mCD156 gene was mapped to chromosome 7, region F3-F4.
M Kataoka, K Yoshiyama, K Matsuura, N Hijiya, Y Higuchi, S Yamamoto

2388 related Products with: Structure of the murine CD156 gene, characterization of its promoter, and chromosomal location.

5 G50 ug100 μg50 ug1 mg100 μg50 mg50 ug50 ug10 ug10

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#9126482   // To Up

CD156 (human ADAM8): expression, primary amino acid sequence, and gene location.

The murine cell-surface antigen MS2 [ADAM 8; mouse CD156 (mCD156)] is a transmembrane glycoprotein that is highly expressed in monocytic lineages. mCD156 consists of a long exterior region containing domains strikingly similar to those of hemorrhagic snake venom proteins. cDNA for human CD156 was isolated from cDNA libraries from the human macrophage cell line THP-1 and from human granulocytes. The CD156 cDNA detected mRNA from human macrophage cell lines, granulocytes, monocytes, and B cell but not T cell lines. The nucleotide sequence of the CD156 cDNA showed 65.6% homology with that of mCD156, and its amino acid sequence had high homology with hemorrhagic snake venom proteins and other related mammalian proteins. The CD156 gene was mapped to human chromosome 10q26.3.
K Yoshiyama, Y Higuchi, M Kataoka, K Matsuura, S Yamamoto

2561 related Products with: CD156 (human ADAM8): expression, primary amino acid sequence, and gene location.

100ug5 x 50 ug10 50 ug10 mg1 g100 1 mg.5 μg1 g100 mg10 mg

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