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<title>Disintegrine</title>

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<h1 id="firstHeading" class="firstHeading mw-first-heading">Disintegrine</h1>

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Disintegrine sind <a href="Peptid#Polypeptid" title="Peptid">Polypeptide</a>, die erstmals aus dem <a href="Schlangengift" title="Schlangengift">Gift</a> verschiedener <a href="Vipern" title="Vipern">Vipern</a> (Viperidae) isoliert wurden. Die Sequenz findet sich aber auch als Disintegrin-Domäne in einer Reihe humaner Enzyme, den <a href="ADAM-Metalloproteasen" title="ADAM-Metalloproteasen">ADAM-Metalloproteasen</a>. Bisher sind über 25 verschiedene Disintegrine aus Schlangengift isoliert worden.

<div class="mw-heading mw-heading2"><h2 id="Aufbau">Aufbau</h2></div>

Disintegrine sind wasserlösliche <a href="Cystein" title="Cystein">cysteinreiche</a> nicht-<a href="Enzym" title="Enzym">enzymatische</a> Peptide, die in Schlangengift aus 41 bis 84 <a href="Aminos%C3%A4uren" title="Aminosäuren">Aminosäuren</a> bestehen. In den ADAM-Proteasen besteht die <a href="Aminos%C3%A4uresequenz" title="Aminosäuresequenz">Sequenz</a> der Disintegrin-Domäne meist aus ungefähr 90 Aminosäuren. Fast alle Disintegrine und Disintegrin-Domänen, so beispielsweise auch ADAM15, enthalten die <a href="RGD-Sequenz" title="RGD-Sequenz">RGD-Sequenz</a> (Arg-Gly-Asp), die beispielsweise an αvβ3-<a href="Integrine" title="Integrine">Integrine</a> bindet.<a href="#cite_note-PMID12514095-1">[1]</a> Andere Disintegrine der ADAMs können an andere Integrine binden. ADAM28 bindet an α4β1<a href="#cite_note-PMID11724793-2">[2]</a>

Im Schlangengift bewirken die Disintegrine eine verminderte Blutgerinnung durch die Bindung an den <a href="Fibrinogen" title="Fibrinogen">Fibrinogen</a>-Bindungsrezeptor – das Integrin αIIbβ3 – der <a href="Thrombozyt" title="Thrombozyt">Thrombozyten</a>.<a href="#cite_note-PMID11415436-3">[3]</a>

Die RGD-Sequenz, oder wie im Fall von Obtustatin die KTS-Sequenz, wird am Ende einer Schleifenstruktur des Peptids dem jeweiligen Rezeptor präsentiert.<a href="#cite_note-PMID15642483-4">[4]</a>

<div class="mw-heading mw-heading2"><h2 id="Anwendung">Anwendung</h2></div>

Die hochspezifische Bindung an verschiedene Rezeptoren machen die Disintegrine zu potenziellen Wirkstoffen zur Behandlung einer Reihe von Erkrankungen. Die <a href="Antikoagulation" title="Antikoagulation">antikoagulative</a> Wirkung kann beispielsweise zur Vorbeugung vor <a href="Thrombus" title="Thrombus">Thromben</a> genutzt werden.<a href="#cite_note-stocker-5">[5]</a>

Weltweit werden die Disintegrine für die Therapie von <a href="Krebs_(Medizin)" title="Krebs (Medizin)">Krebs</a>, <a href="Asthma" class="mw-redirect" title="Asthma">Asthma</a> und <a href="Osteopenie" title="Osteopenie">Osteopenie</a> erprobt.<a href="#cite_note-PMID18508683-6">[6]</a>

Speziell die hohe Affinität zu bestimmten Integrinen, die beim Tumorwachstum wichtig für die Neubildung von Blutgefäßen (<a href="Angiogenese" title="Angiogenese">Angiogenese</a>) sind (beispielsweise αvβ3), ist dabei von Interesse.<a href="#cite_note-PMID17979731-7">[7]</a>

<div class="mw-heading mw-heading2"><h2 id="Beispiele">Beispiele</h2></div>

Auswahl einiger Schlangen-Disintegrine.

<td>Name

</td>

<td>nAminosäuren

</td>

<td>nCystein

</td>

<td>Spezies

</td></tr>

<tr>

<td>Albolabrin<a href="#cite_note-PMID2036389-8">[8]</a>

</td>

<td>73

</td>

<td>12

</td>

<td><a href="Wei%C3%9Flippen-Bambusotter" title="Weißlippen-Bambusotter">Weißlippen-Bambusotter</a> (Trimeresurus albolabris)

</td></tr>

<tr>

<td>Rhodostomin<a href="#cite_note-PMID11415436-3">[3]</a>

</td>

<td>68

</td>

<td>12

</td>

<td><a href="Malayische_Mokassinotter" title="Malayische Mokassinotter">Malayische Mokassinotter</a> (Calloselasma rhodostoma)

</td></tr>

<tr>

<td>Trigramin<a href="#cite_note-PMID3680247-9">[9]</a>

</td>

<td>72

</td>

<td>12

</td>

<td><a href="Gr%C3%BCne_Bambusotter" title="Grüne Bambusotter">Grüne Bambusotter</a> (Trimeresurus gramineus)

</td></tr>

<tr>

<td>Batroxostatin<a href="#cite_note-PMID2207176-10">[10]</a>

</td>

<td>71

</td>

<td>12

</td>

<td><a href="Gew%C3%B6hnliche_Lanzenotter" title="Gewöhnliche Lanzenotter">Gewöhnliche Lanzenotter</a> (Bothrops atrox)

</td></tr>

<tr>

<td>Elegantin<a href="#cite_note-PMID2191722-11">[11]</a><a href="#cite_note-PMID8920980-12">[12]</a>

</td>

<td>73

</td>

<td>12

</td>

<td>Trimeresurus elegans

</td></tr>

<tr>

<td>Applagin<a href="#cite_note-PMID2036389-8">[8]</a>

</td>

<td>71

</td>

<td>12

</td>

<td><a href="Wassermokassinotter" title="Wassermokassinotter">Wassermokassinotter</a> (Agkistrodon piscivorus)

</td></tr>

<tr>

<td>Barbourin<a href="#cite_note-PMID10815769-13">[13]</a><a href="#cite_note-PMID2033037-14">[14]</a>

</td>

<td>73

</td>

<td>12

</td>

<td><a href="Zwergklapperschlange" title="Zwergklapperschlange">Zwergklapperschlange</a> (Sistrurus m. barbouri)

</td></tr>

<tr>

<td>Bitistatin<a href="#cite_note-PMID15642483-4">[4]</a><a href="#cite_note-PMID9369214-15">[15]</a>

</td>

<td>83

</td>

<td>14

</td>

<td><a href="Puffotter" title="Puffotter">Puffotter</a> (Bitis arietans)

</td></tr>

<tr>

<td>Obtustatin<a href="#cite_note-PMID12727812-16">[16]</a>

</td>

<td>41

</td>

<td>8

</td>

<td><a href="Levanteotter" title="Levanteotter">Levanteotter</a> (Macrovipera lebetina)

</td></tr>

<tr>

<td>Echistatin<a href="#cite_note-PMID12727812-16">[16]</a><a href="#cite_note-PMID3198653-17">[17]</a>

</td>

<td>49

</td>

<td>8

</td>

<td><a href="Gemeine_Sandrasselotter" title="Gemeine Sandrasselotter">Gemeine Sandrasselotter</a> (Echis carinatus)

</td></tr>

<tr>

<td>Eristostatin<a href="#cite_note-PMID12727812-16">[16]</a><a href="#cite_note-PMID17316731-18">[18]</a>

</td>

<td>49

</td>

<td>8

</td>

<td><a href="MacMahon-Viper" title="MacMahon-Viper">MacMahon-Viper</a> (Eristicophis macmahoni)

</td></tr>

<tr>

<td>Halysin<a href="#cite_note-PMID8772651-19">[19]</a><a href="#cite_note-PMID1888330-20">[20]</a>

</td>

<td>71

</td>

<td>12

</td>

<td><a href="Halysotter" title="Halysotter">Halysotter</a> (Gloydius halys)

</td></tr>

<tr>

<td>Kistrin<a href="#cite_note-PMID8772651-19">[19]</a><a href="#cite_note-PMID1900221-21">[21]</a>

</td>

<td>68

</td>

<td>12

</td>

<td><a href="Malayische_Mokassinotter" title="Malayische Mokassinotter">Malayische Mokassinotter</a> (Calloselasma rhodostoma)

</td></tr>

<tr>

<td>Mambin<a href="#cite_note-PMID8772651-19">[19]</a><a href="#cite_note-PMID1591238-22">[22]</a>

</td>

<td>59

</td>

<td>8

</td>

<td><a href="Jamesons_Mamba" title="Jamesons Mamba">Jamesons Mamba</a> (Dendroaspis jamesoni)

</td></tr>

<tr>

<td>Tergeminin<a href="#cite_note-PMID2033037-14">[14]</a>

</td>

<td>73

</td>

<td>12

</td>

<td><a href="Massassauga" title="Massassauga">Westliche Massassauga</a> (Sistrurus catenatus tergeminus)

</td></tr>

<tr>

<td>Triflavin<a href="#cite_note-PMID1859363-23">[23]</a>

</td>

<td>70

</td>

<td>12

</td>

<td><a href="Habu-Schlange" class="mw-redirect" title="Habu-Schlange">Habu-Schlange</a> (Trimeresurus flavoviridis)

</td></tr></tbody></table>

<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>

<li id="cite_note-PMID12514095-1"><a href="#cite_ref-PMID12514095_1-0">↑</a> D. F. Seals und S. A. Courtneidge: <a rel="nofollow" class="external text" href="http://genesdev.cshlp.org/content/17/1/7.long">The ADAMs family of metalloproteases: multidomain proteins with multiple functions.</a> In: Genes Dev 17, 2003, S. 7–30. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/12514095?dopt=Abstract">PMID 12514095</a> (Review)

</li>

<li id="cite_note-PMID11724793-2"><a href="#cite_ref-PMID11724793_2-0">↑</a> L. C. Bridges u. a.: <style data-mw-deduplicate="TemplateStyles:r261891140">

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</style><a rel="nofollow" class="external text" href="https://web.archive.org/web/20080528103748/http://www.jbc.org/cgi/content/full/277/5/3784">The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin α4β1.</a> (<a href="Webarchivierung#Begrifflichkeiten" title="Webarchivierung">Memento</a> vom 28. Mai 2008 im <a href="Internet_Archive" title="Internet Archive">Internet Archive</a>) In: <a href="J_Biol_Chem" class="mw-redirect" title="J Biol Chem">J Biol Chem</a> 277, 2002, S. 3784–3792. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/11724793?dopt=Abstract">PMID 11724793</a>

</li>

<li id="cite_note-PMID11415436-3">↑ <a href="#cite_ref-PMID11415436_3-0">a</a> <a href="#cite_ref-PMID11415436_3-1">b</a> C. P. Chang u. a.: Positional importance of Pro53 adjacent to the Arg49-Gly50-Asp51 sequence of rhodostomin in binding to integrin alphaIIbbeta3. In: <a href="Biochem_J" class="mw-redirect" title="Biochem J">Biochem J</a> 357, 2001, S. 57–64. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/11415436?dopt=Abstract">PMID 11415436</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221928/">PMC 1221928</a> (freier Volltext)

</li>

<li id="cite_note-PMID15642483-4">↑ <a href="#cite_ref-PMID15642483_4-0">a</a> <a href="#cite_ref-PMID15642483_4-1">b</a> L. C. Knight und J. E. Romano: Functional expression of bitistatin, a disintegrin with potential use in molecular imaging of thromboembolic disease. In: Protein Expr Purif 39, 2005, S. 307–319. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/15642483?dopt=Abstract">PMID 15642483</a>

</li>

<li id="cite_note-stocker-5"><a href="#cite_ref-stocker_5-0">↑</a> K. Stocker: <a rel="nofollow" class="external text" href="https://web.archive.org/web/20151211092315/http://www.smw.ch/docs/pdf/1999_06/1999-06-366.PDF">Anwendung von Schlangengiftproteinen in der Medizin.</a> (<a href="Webarchivierung#Begrifflichkeiten" title="Webarchivierung">Memento</a> vom 11. Dezember 2015 im <a href="Internet_Archive" title="Internet Archive">Internet Archive</a>) (PDF; 182 kB) In: Schweiz Med Wochenschr 129, 1999, S. 205–216.

</li>

<li id="cite_note-PMID18508683-6"><a href="#cite_ref-PMID18508683_6-0">↑</a> M. A. McLane u. a.: Disintegrins in health and disease. In: Front Biosci 13, 2008, S. 6617–6637. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/18508683?dopt=Abstract">PMID 18508683</a> (Review)

</li>

<li id="cite_note-PMID17979731-7"><a href="#cite_ref-PMID17979731_7-0">↑</a> S. Swenson u. a.: Anti-angiogenesis and RGD-containing snake venom disintegrins. In: <a href="Curr_Pharm_Des" class="mw-redirect" title="Curr Pharm Des">Curr Pharm Des</a> 13, 2007, S. 2860–2871. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/17979731?dopt=Abstract">PMID 17979731</a> (Review)

</li>

<li id="cite_note-PMID2036389-8">↑ <a href="#cite_ref-PMID2036389_8-0">a</a> <a href="#cite_ref-PMID2036389_8-1">b</a> J. J. Calvette u. a.: Identification of the disulfide bond pattern in albolabrin, an RGD-containing peptide from the venom of Trimeresurus albolabris: significance for the expression of platelet aggregation inhibitory activity. In: <a href="Biochemistry" title="Biochemistry">Biochemistry</a> 30, 1991, S. 5225–5229. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2036389?dopt=Abstract">PMID 2036389</a>

</li>

<li id="cite_note-PMID3680247-9"><a href="#cite_ref-PMID3680247_9-0">↑</a> T. F. Huang, J. C. Holt, H. Lukasiewicz, S. Niewiarowski: <cite style="font-style:italic">Trigramin. A low molecular weight peptide inhibiting fibrinogen interaction with platelet receptors expressed on glycoprotein IIb-IIIa complex</cite>. In: <cite style="font-style:italic">The Journal of Biological Chemistry</cite>. Band 262, Nr. 33, 1987, S. 16157–16163, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/3680247?dopt=Abstract">PMID 3680247</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Disintegrine&rft.atitle=Trigramin.+A+low+molecular+weight+peptide+inhibiting+fibrinogen+interaction+with+platelet+receptors+expressed+on+glycoprotein+IIb-IIIa+complex&rft.au=T.+F.+Huang%2C+J.+C.+Holt%2C+H.+Lukasiewicz%2C+...&rft.date=1987&rft.genre=journal&rft.issue=33&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.pages=16157-16163&rft.pmid=3680247&rft.volume=262" style="display:none">

</li>

<li id="cite_note-PMID2207176-10"><a href="#cite_ref-PMID2207176_10-0">↑</a> B. Rucinski u. a.: Batroxostatin, an Arg-Gly-Asp-containing peptide from Bothrops atrox, is a potent inhibitor of platelet aggregation and cell interaction with fibronectin. In: <a href="Biochim_Biophys_Acta" class="mw-redirect" title="Biochim Biophys Acta">Biochim Biophys Acta</a> 1054, 1990, S. 257–262. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2207176?dopt=Abstract">PMID 2207176</a>

</li>

<li id="cite_note-PMID2191722-11"><a href="#cite_ref-PMID2191722_11-0">↑</a> J. Williams u. a.: Elegantin and albolabrin purified peptides from viper venoms: homologies with the RGDS domain of fibrinogen and von Willebrand factor. In: Biochim Biophys Acta 1039, 1990, S. 81–89. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2191722?dopt=Abstract">PMID 2191722</a>

</li>

<li id="cite_note-PMID8920980-12"><a href="#cite_ref-PMID8920980_12-0">↑</a> A. Scaloni u. a.: Amino acid sequence and molecular modelling of glycoprotein IIb-IIIa and fibronectin receptor iso-antagonists from Trimeresurus elegans venom. In: Biochem J 319, 1996, S. 775–782. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8920980?dopt=Abstract">PMID 8920980</a>

</li>

<li id="cite_note-PMID10815769-13"><a href="#cite_ref-PMID10815769_13-0">↑</a> H. Minoux u. a.: Structural analysis of the KGD sequence loop of barbourin, an alphaIIbbeta3-specific disintegrin. In; J Comput Aided Mol Des 14, 2000, S. 317–327. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/10815769?dopt=Abstract">PMID 10815769</a>

</li>

<li id="cite_note-PMID2033037-14">↑ <a href="#cite_ref-PMID2033037_14-0">a</a> <a href="#cite_ref-PMID2033037_14-1">b</a> R. M. Scarborough, J. W. Rose, M. A. Hsu, D. R. Phillips, V. A. Fried, A. M. Campbell, L. Nannizzi, I. F. Charo: <cite style="font-style:italic">Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri</cite>. In: <cite style="font-style:italic">The Journal of Biological Chemistry</cite>. Band 266, Nr. 15, 1991, S. 9359–9362, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2033037?dopt=Abstract">PMID 2033037</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Disintegrine&rft.atitle=Barbourin.+A+GPIIb-IIIa-specific+integrin+antagonist+from+the+venom+of+Sistrurus+m.+barbouri&rft.au=R.+M.+Scarborough%2C+J.+W.+Rose%2C+M.+A.+Hsu%2C+...&rft.date=1991&rft.genre=journal&rft.issue=15&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.pages=9359-9362&rft.pmid=2033037&rft.volume=266" style="display:none">

</li>

<li id="cite_note-PMID9369214-15"><a href="#cite_ref-PMID9369214_15-0">↑</a> J. J. Calvetea u. a.: The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans. In: <a href="FEBS_Letters" title="FEBS Letters">FEBS Letters</a> 416, 1997, S. 197–202. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/9369214?dopt=Abstract">PMID 9369214</a>

</li>

<li id="cite_note-PMID12727812-16">↑ <a href="#cite_ref-PMID12727812_16-0">a</a> <a href="#cite_ref-PMID12727812_16-1">b</a> <a href="#cite_ref-PMID12727812_16-2">c</a> C. Marcinkiewicz u. a.: <a rel="nofollow" class="external text" href="http://cancerres.aacrjournals.org/cgi/content/full/63/9/2020">Obtustatin: a potent selective inhibitor of alpha1beta1 integrin in vitro and angiogenesis in vivo.</a> In: <a href="Cancer_Res" class="mw-redirect" title="Cancer Res">Cancer Res</a> 63, 2003, S. 2020–2023. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/12727812?dopt=Abstract">PMID 12727812</a>

</li>

<li id="cite_note-PMID3198653-17"><a href="#cite_ref-PMID3198653_17-0">↑</a> Z. R. Gan, R. J. Gould, J. W. Jacobs, P. A. Friedman, M. A. Polokoff: <cite style="font-style:italic">Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus</cite>. In: <cite style="font-style:italic">The Journal of Biological Chemistry</cite>. Band 263, Nr. 36, 1988, S. 19827–19832, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/3198653?dopt=Abstract">PMID 3198653</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Disintegrine&rft.atitle=Echistatin.+A+potent+platelet+aggregation+inhibitor+from+the+venom+of+the+viper%2C+Echis+carinatus&rft.au=Z.+R.+Gan%2C+R.+J.+Gould%2C+J.+W.+Jacobs%2C+...&rft.date=1988&rft.genre=journal&rft.issue=36&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.pages=19827-19832&rft.pmid=3198653&rft.volume=263" style="display:none">

</li>

<li id="cite_note-PMID17316731-18"><a href="#cite_ref-PMID17316731_18-0">↑</a> J. Tian u. a.: Inhibition of melanoma cell motility by the snake venom disintegrin eristostatin. In: <a href="Toxicon" title="Toxicon">Toxicon</a> 49, 2007, S. 899–908. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/17316731?dopt=Abstract">PMID 17316731</a>

</li>

<li id="cite_note-PMID8772651-19">↑ <a href="#cite_ref-PMID8772651_19-0">a</a> <a href="#cite_ref-PMID8772651_19-1">b</a> <a href="#cite_ref-PMID8772651_19-2">c</a> L. C. Knight u. a.: <a rel="nofollow" class="external text" href="http://jnm.snmjournals.org/cgi/reprint/37/3/476">Comparison of iodine-123-disintegrins for imaging thrombi and emboli in a canine model.</a> In: J Nucl Med 37, 1996, S. 476–482. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8772651?dopt=Abstract">PMID 8772651</a>

</li>

<li id="cite_note-PMID1888330-20"><a href="#cite_ref-PMID1888330_20-0">↑</a> T. F. Huang u. a.: Halysin, an antiplatelet Arg-Gly-Asp-containing snake venom peptide, as fibrinogen receptor antagonist. In: <a href="Biochem_Pharmacol" class="mw-redirect" title="Biochem Pharmacol">Biochem Pharmacol</a> 42, 1991, S. 1209–1219. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1888330?dopt=Abstract">PMID 1888330</a>

</li>

<li id="cite_note-PMID1900221-21"><a href="#cite_ref-PMID1900221_21-0">↑</a> T. Yasuda u. a.: <a rel="nofollow" class="external text" href="http://circ.ahajournals.org/cgi/content/abstract/83/3/1038">Kistrin, a polypeptide platelet GPIIb/IIIa receptor antagonist, enhances and sustains coronary arterial thrombolysis with recombinant tissue-type plasminogen activator in a canine preparation.</a> In: Circulation 83, 1991, S. 1038–1047. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1900221?dopt=Abstract">PMID 1900221</a>

</li>

<li id="cite_note-PMID1591238-22"><a href="#cite_ref-PMID1591238_22-0">↑</a> R. S. McDowell u. a.: Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. In: Biochemistry 31, 1992, S. 4766–4772. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1591238?dopt=Abstract">PMID 1591238</a>

</li>

<li id="cite_note-PMID1859363-23"><a href="#cite_ref-PMID1859363_23-0">↑</a> T. F. Huang u. a.: A potent antiplatelet peptide, triflavin, from Trimeresurus flavoviridis snake venom. In: Biochem J 277, 1991, S. 351v357. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1859363?dopt=Abstract">PMID 1859363</a>

</li>

</ol>

<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>

<ul><li>R. J. Gould u. a.: Disintegrins: a family of integrin inhibitory proteins from viper venoms. In: Proc Soc Exp Biol Med 195, 1990, S. 168–171. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2236100?dopt=Abstract">PMID 2236100</a> (Review)</li>

<li>J. A. Williams: Disintegrins: RGD-containing proteins which inhibit cell/matrix interactions (adhesion) and cell/cell interactions (aggregation) via the integrin receptors. In: Pathol Biol (Paris) 40, 1992, S. 813–821. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1484742?dopt=Abstract">PMID 1484742</a> (Review)</li>

<li>S. Niewiarowski u. a.: Disintegrins and other naturally occurring antagonists of platelet fibrinogen receptors. In: Semin Hematol 31, 1994, S. 289–300. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/7831574?dopt=Abstract">PMID 7831574</a> (Review)</li>

<li>T. F. Huang: What have snakes taught us about integrins? In: Cell Mol Life Sci 54, 1998, S. 527–540. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/9676572?dopt=Abstract">PMID 9676572</a> (Review)</li>

<li>R. M. Kini: Anticoagulant proteins from snake venoms: structure, function and mechanism. In: Biochem J 397, 2006, S. 377–387. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16831131?dopt=Abstract">PMID 16831131</a> (Review), <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1533313/">PMC 1533313</a> (freier Volltext)</li>

<li>C. H. Yang: <a rel="nofollow" class="external text" href="http://www.iovs.org/cgi/reprint/37/5/843">Inhibition of retinal pigment epithelial cell-induced tractional retinal detachment by disintegrins, a group of Arg-Gly-Asp-containing peptides from viper venom.</a> In: Invest Ophthalmol Vis Sci 37, 1996, S. 843–854. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8603869?dopt=Abstract">PMID 8603869</a></li>

<li>M. A. McLane u. a.: Disintegrins. In: Curr Drug Targets Cardiovasc Haematol Disord 4, 2004, S. 327–355. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/1557895?dopt=Abstract">PMID 1557895</a> (Review)</li>

<li>X. Lu u. a.: Snake venom metalloproteinase containing a disintegrin-like domain, its structure-activity relationships at interacting with integrins. In: Curr Med Chem Cardiovasc Hematol Agents 3, 2005, S. 249–260. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/15974889?dopt=Abstract">PMID 15974889</a></li>

<li>C. Barja-Fidalgo u. a.: <a rel="nofollow" class="external text" href="http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005001000008&lng=en&nrm=iso&tlng=en">Disintegrins: integrin selective ligands which activate integrin-coupled signaling and modulate leukocyte functions.</a> In: Braz J Med Biol Res 38, 2005, S. 1513–1520. <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16172744?dopt=Abstract">PMID 16172744</a> (Review)</li>

<li>K. Grimm: Induktion der Integrin vermittelten Synthese und Aktivierung von Matrix Metalloproteinasen durch Schlangengift Metalloproteinasen in dermalen Fibroblasten. Dissertation, Universität zu Köln, 2003. <a href="Uniform_Resource_Name" title="Uniform Resource Name">urn</a>:<a rel="nofollow" class="external text" href="https://nbn-resolving.de/urn:nbn:de:hbz:38-13157">nbn:de:hbz:38-13157</a></li></ul>

<div class="mw-heading mw-heading2"><h2 id="Weblinks">Weblinks</h2></div>

<ul><li>T. Wolf: <a rel="nofollow" class="external text" href="https://www.welt.de/welt_print/article1620599/Schlangengift-gegen-Krebs.html">Schlangengift gegen Krebs.</a> In: Die Welt vom 2. Februar 2008</li>

<li>T. Wolf: <a rel="nofollow" class="external text" href="http://www.morgenpost.de/printarchiv/wissen/article162380/Schlangengift_gegen_Krebs_Alzheimer_und_Parkinson.html">Schlangengift gegen Krebs, Alzheimer und Parkinson.</a> In: Berliner Morgenpost vom 3. Februar 2008</li></ul></div><div><div class="zim-footer">

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