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Journal articles on the topic 'Adam, Adam'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Dreymueller, Daniela, Stefan Uhlig, and Andreas Ludwig. "ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets." American Journal of Physiology-Lung Cellular and Molecular Physiology 308, no. 4 (2015): L325—L343. http://dx.doi.org/10.1152/ajplung.00294.2014.

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Acute and chronic lung inflammation is driven and controlled by several endogenous mediators that undergo proteolytic conversion from surface-expressed proteins to soluble variants by a disintegrin and metalloproteinase (ADAM)-family members. TNF and epidermal growth factor receptor ligands are just some of the many substrates by which these proteases regulate inflammatory or regenerative processes in the lung. ADAM10 and ADAM17 are the most prominent members of this protease family. They are constitutively expressed in most lung cells and, as recent research has shown, are the pivotal sheddin

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2

Charrier, Laetitia, Yutao Yan, Adel Driss, Christian L. Laboisse, Shanthi V. Sitaraman, and Didier Merlin. "ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 2 (2005): G346—G353. http://dx.doi.org/10.1152/ajpgi.00262.2004.

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The disintegrin metalloproteases (or ADAMs) are membrane-anchored glycoproteins that have been implicated in cell-cell or cell-matrix interactions and in proteolysis of molecules on the cell surface. The expression and/or the pathophysiological implications of ADAMs are not known in intestinal epithelial cells. Therefore, our aim was to investigate the expression and the role of ADAMs in intestinal epithelial cells. Expression of ADAMs was assessed by RT-PCR, Western blot analysis, and immunufluorescence experiments. Wound-healing experiments were performed by using the electric cell substrate

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3

Łukaszewicz-Zając, Marta, Maciej Dulewicz, and Barbara Mroczko. "A Disintegrin and Metalloproteinase (ADAM) Family: Their Significance in Malignant Tumors of the Central Nervous System (CNS)." International Journal of Molecular Sciences 22, no. 19 (2021): 10378. http://dx.doi.org/10.3390/ijms221910378.

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Despite the considerable advances in diagnostic methods in medicine, central nervous system (CNS) tumors, particularly the most common ones—gliomas—remain incurable, with similar incidence rates and mortality. A growing body of literature has revealed that degradation of the extracellular matrix by matrix metalloproteinases (MMPs) might be involved in the pathogenesis of CNS tumors. However, the subfamily of MMPs, known as disintegrin and metalloproteinase (ADAM) proteins are unique due to both adhesive and proteolytic activities. The objective of our review is to present the role of ADAMs in

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4

van der Vorst, Emiel, Christian Weber, and Marjo Donners. "A Disintegrin and Metalloproteases (ADAMs) in Cardiovascular, Metabolic and Inflammatory Diseases: Aspects for Theranostic Approaches." Thrombosis and Haemostasis 118, no. 07 (2018): 1167–75. http://dx.doi.org/10.1055/s-0038-1660479.

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AbstractA disintegrin and metalloproteases (ADAMs) are membrane-bound enzymes responsible for the shedding or cleavage of various cell surface molecules, such as adhesion molecules, cytokines/chemokines and growth factors. This shedding can result in the release of soluble proteins that can exert agonistic or antagonistic functions. Additionally, ADAM-mediated cleavage can render these membrane proteins inactive. This review will describe the role and association of ADAMs in various pathologies with a main focus on ADAM10 and ADAM17 in atherosclerosis, including a brief overview of atheroscler

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5

BRIDGES, Lance C., Dean SHEPPARD та Ron D. BOWDITCH. "ADAM disintegrin-like domain recognition by the lymphocyte integrins α4β1 and α4β7". Biochemical Journal 387, № 1 (2005): 101–8. http://dx.doi.org/10.1042/bj20041444.

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The ADAM (adisintegrin and metalloprotease) family of proteins possess both proteolytic and adhesive domains. We have established previously that the disintegrin domain of ADAM28, an ADAM expressed by human lymphocytes, is recognized by the integrin α4β1. The present study characterizes the integrin binding properties of the disintegrin-like domains of human ADAM7, ADAM28 and ADAM33 with the integrins α4β1, α4β7 and α9β1. Cell-adhesion assays demonstrated that, similar to ADAM28, the ADAM7 disintegrin domain supported α4β1-dependent Jurkat cell adhesion, whereas the ADAM33 disintegrin domain d

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Däuker, Helmut. "Der melancholische Vampir." »Gibt es ein Entkommen? Lebenslinien im Brennpunkt der Geschichte« 30, no. 1 (2018): 93–99. http://dx.doi.org/10.30820/8240.05.

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Adam und Eve sind ein Vampirpaar, leben aber an getrennten Orten, Adam in Detroit, Eve in Tanger. Beide führen ein für Vampire ungewöhnliches ›Leben‹, indem sie sich hauptsächlich kulturellen Tätigkeiten hingeben und sich ausschließlich von Blutkonserven ernähren. Eve ist beunruhigt durch Adams suizidale Stimmung und besucht ihn in Detroit. Als Ava, Eve’s kleine Schwester hinzustößt, gerät das beschaulich-aristokratisch anmutende Leben der beiden Älteren etwas aus den Fugen, u.a., weil Ava gegen die Regeln Adams Kollegen Ian aussaugt. Dieser überlebt dies nicht, Adam und Eve müssen den Leichna

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7

Han, Cecil, Eunyoung Choi, Inju Park, et al. "Comprehensive Analysis of Reproductive ADAMs: Relationship of ADAM4 and ADAM6 with an ADAM Complex Required for Fertilization in Mice1." Biology of Reproduction 80, no. 5 (2009): 1001–8. http://dx.doi.org/10.1095/biolreprod.108.073700.

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Schlomann, Uwe, Kristina Dorzweiler, Elisa Nuti, Tiziano Tuccinardi, Armando Rossello, and Jörg W. Bartsch. "Metalloprotease inhibitor profiles of human ADAM8 in vitro and in cell-based assays." Biological Chemistry 400, no. 6 (2019): 801–10. http://dx.doi.org/10.1515/hsz-2018-0396.

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AbstractADAM8 as a membrane-anchored metalloproteinase-disintegrin is upregulated under pathological conditions such as inflammation and cancer. As active sheddase, ADAM8 can cleave several membrane proteins, among them the low-affinity receptor FcεRII CD23. Hydroxamate-based inhibitors are routinely used to define relevant proteinases involved in ectodomain shedding of membrane proteins. However, for ADAM proteinases, common hydroxamates have variable profiles in their inhibition properties, commonly known for ADAM proteinases 9, 10 and 17. Here, we determined the inhibitor profile of human A

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9

Donizy, Piotr, Marcin Zietek, Marek Leskiewicz, Agnieszka Halon, and Rafal Matkowski. "High Percentage of ADAM-10 Positive Melanoma Cells Correlates with Paucity of Tumor-Infiltrating Lymphocytes but Does Not Predict Prognosis in Cutaneous Melanoma Patients." Analytical Cellular Pathology 2015 (2015): 1–7. http://dx.doi.org/10.1155/2015/975436.

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ADAM-10 (CDw156, CD156c, and kuzbanian) is a protein belonging to a superfamily of metalloproteases, enzymes capable of degrading the extracellular matrix. ADAMs have also been shown to be primarily involved in ectodomain cleavage. The aim of the study was to assess the expression and intracellular location of ADAM-10 in 104 primary skin melanomas and 16 metastatic lesions from regional lymph nodes. Also, prognostic significance of ADAM-10 expression in primary tumor cells and metastatic lesion cells was evaluated during 5-year observation. It was revealed that high expression of ADAM-10 posit

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Takahashi, Yuji, Dora Bigler, Yasuhiko Ito та Judith M. White. "Sequence-Specific Interaction between the Disintegrin Domain of Mouse ADAM 3 and Murine Eggs: Role of β1 Integrin-associated Proteins CD9, CD81, and CD98". Molecular Biology of the Cell 12, № 4 (2001): 809–20. http://dx.doi.org/10.1091/mbc.12.4.809.

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ADAM 3 is a sperm surface glycoprotein that has been implicated in sperm-egg adhesion. Because little is known about the adhesive activity of ADAMs, we investigated the interaction of ADAM 3 disintegrin domains, made in bacteria and in insect cells, with murine eggs. Both recombinant proteins inhibited sperm-egg binding and fusion with potencies similar to that which we recently reported for the ADAM 2 disintegrin domain. Alanine scanning mutagenesis revealed a critical importance for the glutamine at position 7 of the disintegrin loop. Fluorescent beads coated with the ADAM 3 disintegrin doma

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Ohtsu, Haruhiko, Peter J. Dempsey, and Satoru Eguchi. "ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors." American Journal of Physiology-Cell Physiology 291, no. 1 (2006): C1—C10. http://dx.doi.org/10.1152/ajpcell.00620.2005.

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A disintegrin and metalloprotease (ADAM) is a membrane-anchored metalloprotease implicated in the ectodomain shedding of cell surface proteins, including the ligands for epidermal growth factor (EGF) receptors (EGFR)/ErbB. It has been well documented that the transactivation of the EGFR plays critical roles for many cellular functions, such as proliferation and migration mediated through multiple G protein-coupled receptors (GPCRs). Recent accumulating evidence has suggested that ADAMs are the key metalloproteases activated by several GPCR agonists to produce a mature EGFR ligand leading to th

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12

Moss, Marcia L., and Millard H. Lambert. "Shedding of membrane proteins by ADAM family proteases." Essays in Biochemistry 38 (October 1, 2002): 141–53. http://dx.doi.org/10.1042/bse0380141.

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Many membrane-bound proteins undergo proteolytic release from the membrane, a process known as 'shedding'. Some of the processing events are carried out by enzymes of the ADAM (a disintegrin and metalloproteinase) family, which are also membrane bound. One of the most well known ADAM family members is TACE (tumour necrosis factor-alpha-converting enzyme. TACE was the first ADAM family member to have a known physiological substrate, namely, precursor tumour necrosis factor-alpha. Inhibitors of TACE block the release of the soluble form of this inflammatory cytokine, and are currently being stud

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13

Kanakis, Dimitrios, Uwe Lendeckel, Paraskevi Theodosiou, et al. "ADAM 12: A Putative Marker of Oligodendrogliomas?" Disease Markers 34, no. 2 (2013): 81–91. http://dx.doi.org/10.1155/2013/823025.

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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 oligodend

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14

Ramanujam, Sunitha, and Miriam A. M. Capretz. "ADAM." International Journal of Intelligent Information Technologies 1, no. 3 (2005): 14–33. http://dx.doi.org/10.4018/jiit.2005070102.

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15

Terras, Rita, and Ulla Berkéwicz. "Adam." World Literature Today 62, no. 3 (1988): 456. http://dx.doi.org/10.2307/40144354.

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16

Sisson, Matthew S. "Adam." English Journal 93, no. 1 (2003): 119. http://dx.doi.org/10.2307/3650592.

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17

Ganesan, Dharmalingam, and Mikael Lindvall. "ADAM." ACM Transactions on Software Engineering and Methodology 23, no. 2 (2014): 1–51. http://dx.doi.org/10.1145/2529998.

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18

Barbará, Daniel, Julia Couto, Sushil Jajodia, and Ningning Wu. "ADAM." ACM SIGMOD Record 30, no. 4 (2001): 15–24. http://dx.doi.org/10.1145/604264.604268.

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19

GOLD, SUSAN DILLON. "Adam." Nursing 31, no. 11 (2001): 46–48. http://dx.doi.org/10.1097/00152193-200131110-00017.

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20

Trébucq, Stéphane, and Elisabetta Magnaghi. "ADAM." Recherche et Cas en Sciences de Gestion N° 17, no. 1 (2021): 79–117. http://dx.doi.org/10.3917/rcsg.017.0079.

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21

Huang, Jing, Lance C. Bridges, and Judith M. White. "Selective Modulation of Integrin-mediated Cell Migration by Distinct ADAM Family Members." Molecular Biology of the Cell 16, no. 10 (2005): 4982–91. http://dx.doi.org/10.1091/mbc.e05-03-0258.

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A disintegrin and a metalloprotease (ADAM) family members have been implicated in many biological processes. Although it is recognized that recombinant ADAM disintegrin domains can interact with integrins, little is known about ADAM-integrin interactions in cellular context. Here, we tested whether ADAMs can selectively regulate integrin-mediated cell migration. ADAMs were expressed in Chinese hamster ovary cells that express defined integrins (α4β1, α5β1, or both), and cell migration on full-length fibronectin or on its α4β1 or α5β1 binding fragments was studied. We found that ADAMs inhibit i

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22

Litwa, M. David. "Behold Adam: A Reading of John 19:5." Horizons in Biblical Theology 32, no. 2 (2010): 129–43. http://dx.doi.org/10.1163/187122010x529462.

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AbstractThis essay offers a theological interpretation of Pilate’s famous phrase “Behold the man!” (δο νρωπος, John 19:5) in light of two proposed intertextual echoes: Genesis 3:22 and Vita Adae et Evae 13:3. Both texts feature the phrase “Behold the man/Adam.” In each case, the phrase prima facie highlights Adam’s divinity, but ironically underscores the frailty of his humanity. In John 19:5, however, the phrase “Behold the man” functions in the opposite manner. Although on the surface it highlights Jesus’ ridiculousness and misery, it ironically manifests his divine sovereignty. The essay c

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23

Iba, Kousuke, Reidar Albrechtsen, Brent Gilpin та ін. "The Cysteine-Rich Domain of Human Adam 12 Supports Cell Adhesion through Syndecans and Triggers Signaling Events That Lead to β1 Integrin–Dependent Cell Spreading". Journal of Cell Biology 149, № 5 (2000): 1143–56. http://dx.doi.org/10.1083/jcb.149.5.1143.

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The ADAMs (a disintegrin and metalloprotease) family of proteins is involved in a variety of cellular interactions, including cell adhesion and ecto- domain shedding. Here we show that ADAM 12 binds to cell surface syndecans. Three forms of recombinant ADAM 12 were used in these experiments: the cys-teine-rich domain made in Escherichia coli (rADAM 12-cys), the disintegrin-like and cysteine-rich domain made in insect cells (rADAM 12-DC), and full-length human ADAM 12-S tagged with green fluorescent protein made in mammalian cells (rADAM 12-GFP). Mesenchymal cells specifically and in a dose-dep

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24

Conrad, Catharina, Julia Benzel, Kristina Dorzweiler, et al. "ADAM8 in invasive cancers: links to tumor progression, metastasis, and chemoresistance." Clinical Science 133, no. 1 (2019): 83–99. http://dx.doi.org/10.1042/cs20180906.

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Abstract Ectodomain shedding of extracellular and membrane proteins is of fundamental importance for cell–cell communication in neoplasias. A Disintegrin And Metalloproteinase (ADAM) proteases constitute a family of multifunctional, membrane-bound proteins with traditional sheddase functions. Their protumorigenic potential has been attributed to both, essential (ADAM10 and ADAM17) and ‘dispensable’ ADAM proteases (ADAM8, 9, 12, 15, and 19). Of specific interest in this review is the ADAM proteinase ADAM8 that has been identified as a significant player in aggressive malignancies including brea

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25

Bahudhanapati, Harinath, Shashwati Bhattacharya, and Shuo Wei. "Evolution of Vertebrate Adam Genes; Duplication of Testicular Adams from Ancient Adam9/9-like Loci." PLOS ONE 10, no. 8 (2015): e0136281. http://dx.doi.org/10.1371/journal.pone.0136281.

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26

Yuan, Ruiyong, Paul Primakoff, and Diana G. Myles. "A Role for the Disintegrin Domain of Cyritestin, a Sperm Surface Protein Belonging to the ADAM Family, in Mouse Sperm–Egg Plasma Membrane Adhesion and Fusion." Journal of Cell Biology 137, no. 1 (1997): 105–12. http://dx.doi.org/10.1083/jcb.137.1.105.

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Sperm–egg plasma membrane fusion is preceded by sperm adhesion to the egg plasma membrane. Cell–cell adhesion frequently involves multiple adhesion molecules on the adhering cells. One sperm surface protein with a role in sperm–egg plasma membrane adhesion is fertilin, a transmembrane heterodimer (α and β subunits). Fertilin α and β are the first identified members of a new family of membrane proteins that each has the following domains: pro-, metalloprotease, disintegrin, cysteine-rich, EGF-like, transmembrane, and cytoplasmic domain. This protein family has been named ADAM because all member

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27

Barash, David P. "Old Adam, New Adam, We, and Us." Society 48, no. 6 (2011): 471–73. http://dx.doi.org/10.1007/s12115-011-9478-8.

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28

Umeda, Masataka, Nobuya Yoshida, Ryo Hisada та ін. "ADAM9 enhances Th17 cell differentiation and autoimmunity by activating TGF-β1". Proceedings of the National Academy of Sciences 118, № 18 (2021): e2023230118. http://dx.doi.org/10.1073/pnas.2023230118.

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The a disintegrin and metalloproteinase (ADAM) family of proteinases alter the extracellular environment and are involved in the development of T cells and autoimmunity. The role of ADAM family members in Th17 cell differentiation is unknown. We identified ADAM9 to be specifically expressed and to promote Th17 differentiation. Mechanistically, we found that ADAM9 cleaved the latency-associated peptide to produce bioactive transforming growth factor β1, which promoted SMAD2/3 phosphorylation and activation. A transcription factor inducible cAMP early repressor was found to bind directly to the

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29

Lu, Dong, Kian Chung, Min Xia, Mike Scully, Vijay Kakkar, and Xinjie Lu. "Integrin binding characteristics of the disintegrin-like domain of ADAM-15." Thrombosis and Haemostasis 96, no. 11 (2006): 642–51. http://dx.doi.org/10.1160/th06-07-0395.

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SummaryAlthough discovered as potent inhibitors of αIIbβ3-mediated platelet aggregation, snake venom disintegrins are now known to bind to other integrins according to different degrees of potency and specificity. More recently, homologues of the disintegrinlike loop have been found as a discrete domain in the ADAM family, yet the potency and specificity of each of these domains in terms of integrin binding is relatively unknown. In this present study, we have selected the disintegrin-like domain (dd) of ADAM-15 (designated as ddADAM-15), the only RGD containing domain in the ADAM family, for

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30

GIBBONS, ALISON. "Adam Thirlwell." Contemporary Literature 55, no. 4 (2014): 611–34. http://dx.doi.org/10.3368/cl.55.4.611.

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31

Hague, Richard. "Adam Earth." English Journal 85, no. 4 (1996): 41. http://dx.doi.org/10.2307/819628.

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32

Rolin, Timothée. "Adam - www.adamproject.net." Ligeia N°45-48, no. 1 (2003): 216. http://dx.doi.org/10.3917/lige.045.0216.

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33

SCHOTSMANS, Paul. "Adam Nash." Ethische Perspectieven 10, no. 3 (2000): 182–83. http://dx.doi.org/10.2143/epn.10.3.504060.

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34

Radcliffe, Elizabeth S., and D. D. Raphael. "Adam Smith." Philosophical Review 96, no. 4 (1987): 612. http://dx.doi.org/10.2307/2185403.

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35

Haakonssen, Kund, and D. D. Raphael. "Adam Smith." Economic Journal 96, no. 381 (1986): 230. http://dx.doi.org/10.2307/2233442.

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36

Klink, Joanna. "Adam Sleeping." Antioch Review 55, no. 4 (1997): 456. http://dx.doi.org/10.2307/4613572.

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37

McCalman, Ian. "Adam Westoby." Critique 27, no. 1 (1999): 209–10. http://dx.doi.org/10.1080/03017609908413438.

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38

Studwell, William E. "Adolphe Adam." Music Reference Services Quarterly 3, no. 3 (1995): 37–46. http://dx.doi.org/10.1300/j116v03n03_05.

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39

Xiang, Lusha, and Kathy L. Ryan. "ADAM-17." Journal of Trauma and Acute Care Surgery 82, no. 5 (2017): 976. http://dx.doi.org/10.1097/ta.0000000000001396.

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40

Alvey, James E. "Adam Smith." History of Economics Review 75, no. 1 (2020): 77–78. http://dx.doi.org/10.1080/10370196.2020.1744876.

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41

Pappas, Dennis G. "Adam Politzer." Ear, Nose & Throat Journal 75, no. 2 (1996): 74–76. http://dx.doi.org/10.1177/014556139607500206.

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Fellner, Fritz. "Adam Wandruszka †." Mitteilungen des Instituts für Österreichische Geschichtsforschung 106, JG (1998): 443–50. http://dx.doi.org/10.7767/miog.1998.106.jg.443.

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Walters, Kerry S. "Adam Smith." Teaching Philosophy 10, no. 1 (1987): 76–78. http://dx.doi.org/10.5840/teachphil198710116.

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Liebert, Elisabeth. "Domestic Adam." Milton Studies 53, no. 1 (2012): 41–67. http://dx.doi.org/10.1353/mlt.2012.0004.

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Weinstein, Eric. "After Adam." Colorado Review 37, no. 1 (2010): 145–46. http://dx.doi.org/10.1353/col.2010.0001.

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46

Silver, Larry, and Gottfried Sello. "Adam Elsheimer." Sixteenth Century Journal 21, no. 1 (1990): 123. http://dx.doi.org/10.2307/2541147.

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Maxwell, Harold. "Adam Limentani." Psychiatric Bulletin 18, no. 6 (1994): 346–56. http://dx.doi.org/10.1192/pb.18.6.346.

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48

Evans, Roger. "Adam Kilgarriff." Computational Linguistics 41, no. 4 (2015): 719–21. http://dx.doi.org/10.1162/coli_a_00234.

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James, John. "Other Adam." Massachusetts Review 56, no. 1 (2015): 112–13. http://dx.doi.org/10.1353/mar.2015.0022.

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Sublet, Jacqueline. "Adam Gacek." Arabica 61, no. 1-2 (2014): 174–77. http://dx.doi.org/10.1163/15700585-12341292.

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