Search results for: Meltrin
Error loading info... Pleas try again later.
#23324579 // To Up
ADAM 12: a putative marker of oligodendrogliomas?ADAM 12 (meltrin alpha) belongs to a large family of molecules, consisting of members with both disintegrin and metalloproteinase properties. ADAMs have been implicated in several cell physiological processes including cell adhesion, cell fusion, proteolysis and signalling. ADAM 12 is widely expressed, including skeletal muscle, testis, bone, intestine, heart and kidney. In addition, a variety of tumours show elevated expression of ADAM12; among them being breast-, colon-, gastric- and lung-carcinoma. As to the brain, ADAM 12 has been shown previously to be expressed in rat and human oligodendrocytes. However, little is known about the expression of this protease in brain tumours. This study demonstrates the presence of ADAM 12 in non-neoplastic oligodendroglial cells of normal human brain as well as in neoplastic oligodendroglia and minigemistocytes arising from four pure oligodendrogliomas and three mixed oligoastrocytomas. Double stainings revealed a notable preference of ADAM 12 for the oligodendroglial over astroglial components. The results of immunohistochemistry are in accordance with the results obtained from the RT-PCR, which further demonstrated a mild difference concerning the mRNA concentration of ADAM 12 between similar grades of eight astrocytomas and eight oligodendrogliomas (namely four astrocytomas grade II versus four oligodendrogliomas grade II and four astrocytomas grade III versus four oligodendrogliomas grade III). Both cellular immunostaining for ADAM 12 and ADAM 12 mRNA content decrease with higher histologic grade of the tumour. Surprisingly, the latter parameter (ADAM12 mRNA) showed a significant opposite correlation to the degree of histologic tumour malignancy. From our data showing that ADAM 12 is highly expressed in, but not restricted to, oligodendrogliomas, we conclude that ADAM 12 immunohistochemistry may be a helpful tool in the diagnosis of brain tumours.
Dimitrios Kanakis, Uwe Lendeckel, Paraskevi Theodosiou, Henrik Dobrowolny, Christian Mawrin, Gerburg Keilhoff, Alicia Bukowska, Knut Dietzmann, Bernhard Bogerts, Hans-Gert Bernstein100ug100μg100ug100ug100ul100μg100ug100ug2.5 mg100ul10
#21492148 // To Up
Regional expression of ADAM19 during chicken embryonic development.ADAM19 (also named meltrin Î²) is a member of the ADAM (a disintegrin and metalloprotease) family of metalloproteases and is involved in morphogenesis and tissue formation during embryonic development. In the present study, chicken ADAM19 is cloned by reverse transcription-polymerase chain reaction and identified by sequencing. Its expression patterns in different parts of the developing chicken embryo are investigated by Western blot analysis and immunohistochemistry. Results show that ADAM19 protein is widely expressed in chicken embryos. It is detectable in the central nervous system, including the brain, spinal cord, cochlea, and retina. Furthermore, ADAM19 protein is also found in other tissues and organs such as digestive organs, the thymus, the lung bud, the dorsal aorta, the kidney, the gonad, muscles, and in the feather buds. All these data suggest that ADAM19 plays an important role in the embryonic development of chicken.
Xin Yan, Juntang Lin, Annett Markus, Arndt Rolfs, Jiankai Luo300 units96T100ug Lyophilized5050ml100 ul100 Tests200 100ug Lyophilized1mg
#20882308 2010/09/30 To Up
Molecules and signaling pathways involved in the expression of OC-STAMP during osteoclastogenesis.The receptor activator of nuclear factor-ÎºB ligand (RANKL) is a key factor in regulating osteoclastogenesis and in maintaining the survival of mature osteoclasts. We screened differentially expressed genes in RAW264.7 cells in response to RANKL and found osteoclast stimulatory transmembrane protein (OC-STAMP) as one of the RANKL-induced genes of interest. Recently, OC-STAMP has been identified as the RANKL-induced protein that promotes osteoclast differentiation, but the mechanism that regulates its expression is not understood. Therefore, the tissue distribution of OC-STAMP and the signaling pathways that regulate its expression were studied here. Similar to osteoclasts, OC-STAMP was expressed in most tissues, suggesting its involvement in the function of other tissues. Interestingly, OC-STAMP was downregulated by 17Î²-estradiol at high concentrations, suggesting the potential relationship between OC-STAMP and estrogen. Importantly, the knockdown of OC-STAMP at the transcript level resulted in the inhibition of multinucleated osteoclast formation and the decreased expression of genes including transcription factor (such as c-Jun), receptors (such as RANK and c-Fms), a signaling molecule (such as TRAF6), and a cell fusion-related molecule (such as meltrin-Î±), suggesting that the osteoclast differentiation needs the coordinated expression of OC-STAMP with several molecules required for transcription, signaling transduction, and cell fusion. Additionally, the treatment of its specific antibody inhibited the formation and bone resorptive activity of mature osteoclasts, suggesting its involvement in the function of mature osteoclasts. Furthermore, studies with pharmacological inhibitors suggested PKCÎ² or Akt might be the major signaling molecules to regulate the expression of OC-STAMP during osteoclastogenesis.
Myung Hee Kim, Mikyung Park, Seung-Hwa Baek, Hye Joo Kim, Seong Hwan Kim
1165 related Products with: Molecules and signaling pathways involved in the expression of OC-STAMP during osteoclastogenesis.96 wells8 inhibitors2 Pieces/Box2 Pieces/Box14 inhibitors2 Pieces/Box2 Pieces/Box300 units
#20705134 2010/08/10 To Up
The disintegrin and metalloprotease Meltrin from Drosophila forms oligomers via its protein binding domain and is regulated by the homeobox protein VND during embryonic development.A Disintegrin And Metalloprotease (ADAM) proteins belong to the metzincin superfamily of metalloproteases that are known to play important roles in several physiological and developmental processes including myoblast fusion, tumor necrosis factor-Î± release or fertilization. They are characterized by a typical domain structure with a proteolytically active domain and the protein binding domains both facing the extracellular space. Regulatory mechanisms are largely unknown. Here we report on the potential of the Drosophila ADAM Meltrin to form oligomers via its substrate binding domain. Significantly, oligomerization occurs apparently in a redox-dependent manner. Further analysis revealed that the ACR domain is responsible for aggregation while the disintegrin-like and EGF-like domains are not capable of oligomer formation. Stage dependent transcript analysis revealed a constant expression of three different splice variants, two of which were characterized by sequencing. Like many other ADAM proteins, Meltrin shows a highly restricted expression pattern during embryogenesis with at least two of the respective transcripts being present in a subpopulation of neuronal cells in the embryonic central nervous system. Finally, we report on the identification of the first regulator of meltrin: the homeobox protein ventral nervous system defective specifically excludes Meltrin expression from the embryonic ventral neuroectoderm.
Heiko Meyer, Tonia Von Ohlen, Mareike Panz, Achim Paululat
2081 related Products with: The disintegrin and metalloprotease Meltrin from Drosophila forms oligomers via its protein binding domain and is regulated by the homeobox protein VND during embryonic development.1000 TESTS/0.65ml10 100ul 100ul100 ul2100 ul 100ul100ul1mg100 U100ug Lyophilized
#19601832 // To Up
Targeting ADAM12 in human disease: head, body or tail?ADAM12/meltrin alpha is a type I transmembrane multidomain protein involved in tumor progression and other severe diseases, including osteoarthritis, and as such could be considered as a potential drug target. In addition to protease activity, ADAM12 possesses cell binding and cell signaling properties. This functional trinity is reflected in the structure of ADAM12, which can be divided into head, body, and tail. The head of the protein (consisting of the pro and catalytic domains) mediates processing of growth factors and cytokines and has been implicated in epidermal growth factor (EGF) and insulin-like growth factor receptor signaling. The body of the protein (consisting of the disintegrin, cysteine-rich, and EGF-like domains) is involved in contacts with the extracellular matrix and other cells through interactions with integrins and syndecans. Finally, the tail of the protein (consisting of the cytoplasmic domain) is engaged in interactions with intracellular signaling molecules. In many studies, ADAM12 overexpression has been correlated with disease, and ADAM12 has been shown to promote tumor growth and progression in cancer. On the other hand, protective effects of ADAM12 in disease have also been reported. Future investigations should address the precise mechanisms of ADAM12 in disease and biology in order to counterbalance the benefits from targeting ADAM12 therapeutically with possible side effects. This review describes the biology of ADAM12, its association with disease, and evaluates the possible approaches to targeting ADAM12 in human disease.
J Jacobsen, U M Wewer96 tests96 tests100 μg96 tests96 tests0.1 mg96T100 μg
Error loading info... Pleas try again later.
#19049978 2008/12/02 To Up
Roles of meltrin-beta/ADAM19 in progression of Schwann cell differentiation and myelination during sciatic nerve regeneration.Remyelination is an important aspect of nerve regeneration after nerve injury, but the underlying mechanisms are not fully understood. Here, we show that meltrin-beta (ADAM19), a member of the ADAM (a disintegrin and metalloprotease) family, plays crucial roles in nerve regeneration after a crush injury to the sciatic nerves. The expression of meltrin-beta was up-regulated in neurons after the crush injury. Morphometrical analysis revealed a delay in remyelination in meltrin-beta-deficient nerves, whereas no significant defects were observed in their axon elongation. The activation of Krox-20, an indispensable transcription factor for myelination, was delayed in meltrin-beta-deficient nerves and was accompanied by the retarded expression of myelin-related proteins. Expression of Krox-20 in Schwann cells was mediated by Akt. Phosphorylation of Akt but not that of Erks was reduced in regenerating nerves of meltrin-beta-deficient mice. The cell membrane fraction prepared from meltrin-beta-deficient nerves showed a defective activation of Akt in the membrane-loaded Schwann cells. Meltrin-beta-deficient mice exhibited delayed sciatic functional recovery after the nerve crush. Altogether, these results reveal a role of meltrin-beta in Schwann cell differentiation and re-myelination in nerve regeneration. Moreover, this study suggests that meltrin-beta functions as a modulator of juxtacrine signaling from axons that activate the Akt pathway and the Krox-20 expression, which is the prerequisite for Schwann cell differentiation.
Shuji Wakatsuki, Norihiro Yumoto, Koji Komatsu, Toshiyuki Araki, Atsuko Sehara-Fujisawa
1618 related Products with: Roles of meltrin-beta/ADAM19 in progression of Schwann cell differentiation and myelination during sciatic nerve regeneration.100 μg10 ug100ug Lyophilized2ug96 samples96 wells100ug1.00 flask
#19027850 2008/11/06 To Up
Xenopus ADAM19 is involved in neural, neural crest and muscle development.ADAM19 is a member of the meltrin subfamily of ADAM metalloproteases. In Xenopus, ADAM19 is present as a maternal transcript. Zygotic expression starts during gastrulation and is apparent in the dorsal blastopore lip. ADAM19 expression through neurulation and tailbud formation becomes enriched in dorsal structures such as the neural tube, the notochord and the somites. Using morpholino knock-down, we show that a reduction of ADAM19 protein in gastrula stage embryos results in a decrease of Brachyury expression in the notochord concomitant with an increase in the dorsal markers, Goosecoid and Chordin. These changes in gene expression are accompanied by a decrease in phosphorylated AKT, a downstream target of the EGF signaling pathway, and occur while the blastopore closes at the same rate as the control embryos. During neurulation and tailbud formation, ADAM19 knock-down induces a reduction of the neural markers N-tubulin and NRP1 but not Sox2. In the somitic mesoderm, the expression of MLC is also decreased while MyoD is not. ADAM19 knockdown also reduces neural crest markers prior to cell migration. Neural crest induction is also decreased in embryos treated with an EGF receptor inhibitor suggesting that this pathway is necessary for neural crest cell induction. Using targeted knock-down of ADAM19 we show that the reduction of neural and neural crest markers is cell autonomous and that the migration if the cranial neural crest is perturbed. We further show that ADAM19 protein reduction affects somite organization, reduces 12-101 expression and perturbs fibronectin localization at the intersomitic boundary.
Russell Neuner, HÃ©lÃ¨ne Cousin, Catherine McCusker, Michael Coyne, Dominique Alfandari
1487 related Products with: Xenopus ADAM19 is involved in neural, neural crest and muscle development.0.1ml (1mg/ml)100ug Lyophilized100ug Lyophilized10100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized
#18946084 2008/10/22 To Up
Extracellular cleavage of cadherin-11 by ADAM metalloproteases is essential for Xenopus cranial neural crest cell migration.Cell adhesion molecules such as cadherins alternate their expression throughout cranial neural crest (CNC) development, yet our understanding of the role of these molecules during CNC migration remains incomplete. The "mesenchymal" cadherin-11 is expressed in the CNC during migration yet prevents migration when overexpressed in the embryo, suggesting that a defined level of cadherin-11-mediated cell adhesion is required for migration. Here we show that members of the meltrin subfamily of ADAM metalloproteases cleave the extracellular domain of cadherin-11 during CNC migration. We show that a fragment corresponding to the putative shed form of cadherin-11 retains biological activity by promoting CNC migration in vivo, in a non-cell-autonomous manner. Additionally, cleavage of cadherin-11 does not affect binding to beta-catenin and downstream signaling events. We propose that ADAM cleavage of cadherin-11 promotes migration by modifying its ability to support cell-cell adhesion while maintaining the membrane-bound pool of beta-catenin associated with the cadherin-11 cytoplasmic domain.
Catherine McCusker, HÃ©lÃ¨ne Cousin, Russell Neuner, Dominique Alfandari
2857 related Products with: Extracellular cleavage of cadherin-11 by ADAM metalloproteases is essential for Xenopus cranial neural crest cell migration.100 ul100ug Lyophilized1 LITRE10 mg96 samples100ug Lyophilized100ug100ug Lyophilized100 TESTS0.1ml (1mg/ml)100ug Lyophilized
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45 Fax 0032 16 50 90 45
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50 Fax 01 43 25 01 60
52062 Aachen Deutschland
Tel 0241 40 08 90 86 Fax 0241 55 91 05 36
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
Schweiz Züri +41435006251
Česká republika Praha +420246019719
Ireland Dublin +35316526556
Norge Oslo +4721031366
Finland Helsset +358942419041
Sverige Stockholm +46852503438
Ελλάς Αθήνα +302111768494
Magyarország Budapest +3619980547
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
Tel 058 710 33 44
Fax 058 710 33 48
GENTAUR Nederland BV
5521 DG Eersel Nederland
Tel 0208-080893 Fax 0497-517897
Piazza Giacomo Matteotti, 6, 24122 Bergamo
Tel 02 36 00 65 93 Fax 02 36 00 65 94
53 Iskar Str. 1191 Kokalyane, Sofia