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<StructureSection load='1li1' size='340' side='right'caption='[[1li1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1li1' size='340' side='right'caption='[[1li1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1li1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LI1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1li1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LI1 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1li1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li1 OCA], [http://pdbe.org/1li1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1li1 RCSB], [http://www.ebi.ac.uk/pdbsum/1li1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1li1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1li1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1li1 OCA], [https://pdbe.org/1li1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1li1 RCSB], [https://www.ebi.ac.uk/pdbsum/1li1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1li1 ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CO4A1_HUMAN CO4A1_HUMAN]] Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage (BSVDH) [MIM:[http://omim.org/entry/607595 607595]]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.<ref>PMID:16598045</ref> <ref>PMID:17696175</ref> <ref>PMID:17379824</ref> <ref>PMID:20385946</ref> <ref>PMID:19477666</ref>  Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:[http://omim.org/entry/611773 611773]]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.<ref>PMID:18160688</ref> <ref>PMID:20818663</ref>  Defects in COL4A1 are a cause of familial porencephaly (POREN1) [MIM:[http://omim.org/entry/175780 175780]]. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect or arrest in the development of the cerebral ventricles.<ref>PMID:15905400</ref> <ref>PMID:16107487</ref> <ref>PMID:19194877</ref>  [[http://www.uniprot.org/uniprot/CO4A2_HUMAN CO4A2_HUMAN]] Defects in COL4A2 are the cause of porencephaly type 2 (POREN2) [MIM:[http://omim.org/entry/614483 614483]]. POREN2 is a neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles.<ref>PMID:22209246</ref>  Defects in COL4A2 are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[http://omim.org/entry/614519 614519]]. ICH is a pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:22209247</ref>   
[[https://www.uniprot.org/uniprot/CO4A1_HUMAN CO4A1_HUMAN]] Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage (BSVDH) [MIM:[https://omim.org/entry/607595 607595]]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.<ref>PMID:16598045</ref> <ref>PMID:17696175</ref> <ref>PMID:17379824</ref> <ref>PMID:20385946</ref> <ref>PMID:19477666</ref>  Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:[https://omim.org/entry/611773 611773]]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.<ref>PMID:18160688</ref> <ref>PMID:20818663</ref>  Defects in COL4A1 are a cause of familial porencephaly (POREN1) [MIM:[https://omim.org/entry/175780 175780]]. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect or arrest in the development of the cerebral ventricles.<ref>PMID:15905400</ref> <ref>PMID:16107487</ref> <ref>PMID:19194877</ref>  [[https://www.uniprot.org/uniprot/CO4A2_HUMAN CO4A2_HUMAN]] Defects in COL4A2 are the cause of porencephaly type 2 (POREN2) [MIM:[https://omim.org/entry/614483 614483]]. POREN2 is a neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles.<ref>PMID:22209246</ref>  Defects in COL4A2 are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:[https://omim.org/entry/614519 614519]]. ICH is a pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.<ref>PMID:22209247</ref>   
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CO4A1_HUMAN CO4A1_HUMAN]] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.<ref>PMID:10811134</ref> <ref>PMID:16481288</ref> <ref>PMID:16151532</ref> <ref>PMID:18775695</ref>  Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.<ref>PMID:10811134</ref> <ref>PMID:16481288</ref> <ref>PMID:16151532</ref> <ref>PMID:18775695</ref>  [[http://www.uniprot.org/uniprot/CO4A2_HUMAN CO4A2_HUMAN]] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.<ref>PMID:10625665</ref> <ref>PMID:12876280</ref> <ref>PMID:15899827</ref>  Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.<ref>PMID:10625665</ref> <ref>PMID:12876280</ref> <ref>PMID:15899827</ref>   
[[https://www.uniprot.org/uniprot/CO4A1_HUMAN CO4A1_HUMAN]] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.<ref>PMID:10811134</ref> <ref>PMID:16481288</ref> <ref>PMID:16151532</ref> <ref>PMID:18775695</ref>  Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.<ref>PMID:10811134</ref> <ref>PMID:16481288</ref> <ref>PMID:16151532</ref> <ref>PMID:18775695</ref>  [[https://www.uniprot.org/uniprot/CO4A2_HUMAN CO4A2_HUMAN]] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.<ref>PMID:10625665</ref> <ref>PMID:12876280</ref> <ref>PMID:15899827</ref>  Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.<ref>PMID:10625665</ref> <ref>PMID:12876280</ref> <ref>PMID:15899827</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 09:45, 18 August 2021

The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-linkThe 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link

Structural highlights

1li1 is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CO4A1_HUMAN] Defects in COL4A1 are a cause of brain small vessel disease with hemorrhage (BSVDH) [MIM:607595]. Brain small vessel diseases underlie 20 to 30 percent of ischemic strokes and a larger proportion of intracerebral hemorrhages. Inheritance is autosomal dominant.[1] [2] [3] [4] [5] Defects in COL4A1 are the cause of hereditary angiopathy with nephropathy aneurysms and muscle cramps (HANAC) [MIM:611773]. The clinical renal manifestations include hematuria and bilateral large cysts. Histologic analysis revealed complex basement membrane defects in kidney and skin. The systemic angiopathy appears to affect both small vessels and large arteries.[6] [7] Defects in COL4A1 are a cause of familial porencephaly (POREN1) [MIM:175780]. Porencephaly is a term used for any cavitation or cerebrospinal fluid-filled cyst in the brain. Porencephaly type 1 is usually unilateral and results from focal destructive lesions such as fetal vascular occlusion or birth trauma. Type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect or arrest in the development of the cerebral ventricles.[8] [9] [10] [CO4A2_HUMAN] Defects in COL4A2 are the cause of porencephaly type 2 (POREN2) [MIM:614483]. POREN2 is a neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles.[11] Defects in COL4A2 are a cause of susceptibility to intracerebral hemorrhage (ICH) [MIM:614519]. ICH is a pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.[12]

Function

[CO4A1_HUMAN] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.[13] [14] [15] [16] Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. Inhibits expression of hypoxia-inducible factor 1alpha and ERK1/2 and p38 MAPK activation. Ligand for alpha1/beta1 integrin.[17] [18] [19] [20] [CO4A2_HUMAN] Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.[21] [22] [23] Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.[24] [25] [26]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Triple-helical collagen IV protomers associate through their N- and C-termini forming a three-dimensional network, which provides basement membranes with an anchoring scaffold and mechanical strength. The noncollagenous (NC1) domain of the C-terminal junction between two adjacent collagen IV protomers from human placenta was crystallized and its 1.9-A structure was solved by multiple anomalous diffraction (MAD) phasing. This hexameric NC1 particle is composed of two trimeric caps, which interact through a large planar interface. Each cap is formed by two alpha 1 fragments and one alpha 2 fragment with a similar previously uncharacterized fold, segmentally arranged around an axial tunnel. Each monomer chain folds into two structurally very similar subdomains, which each contain a finger-like hairpin loop that inserts into a six-stranded beta-sheet of the neighboring subdomain of the same or the adjacent chain. Thus each trimer forms a quite regular, but nonclassical, sixfold propeller. The trimer-trimer interaction is further stabilized by a previously uncharacterized type of covalent cross-link between the side chains of a Met and a Lys residue of the alpha 1 and alpha 2 chains from opposite trimers, explaining previous findings of nonreducible cross-links in NC1. This structure provides insights into NC1-related diseases such as Goodpasture and Alport syndromes.

The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link.,Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W Proc Natl Acad Sci U S A. 2002 May 14;99(10):6607-12. PMID:12011424[27]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Gould DB, Phalan FC, van Mil SE, Sundberg JP, Vahedi K, Massin P, Bousser MG, Heutink P, Miner JH, Tournier-Lasserve E, John SW. Role of COL4A1 in small-vessel disease and hemorrhagic stroke. N Engl J Med. 2006 Apr 6;354(14):1489-96. PMID:16598045 doi:10.1056/NEJMoa053727
  2. ↑ Sibon I, Coupry I, Menegon P, Bouchet JP, Gorry P, Burgelin I, Calvas P, Orignac I, Dousset V, Lacombe D, Orgogozo JM, Arveiler B, Goizet C. COL4A1 mutation in Axenfeld-Rieger anomaly with leukoencephalopathy and stroke. Ann Neurol. 2007 Aug;62(2):177-84. PMID:17696175 doi:10.1002/ana.21191
  3. ↑ Vahedi K, Kubis N, Boukobza M, Arnoult M, Massin P, Tournier-Lasserve E, Bousser MG. COL4A1 mutation in a patient with sporadic, recurrent intracerebral hemorrhage. Stroke. 2007 May;38(5):1461-4. Epub 2007 Mar 22. PMID:17379824 doi:10.1161/STROKEAHA.106.475194
  4. ↑ Coupry I, Sibon I, Mortemousque B, Rouanet F, Mine M, Goizet C. Ophthalmological features associated with COL4A1 mutations. Arch Ophthalmol. 2010 Apr;128(4):483-9. doi: 10.1001/archophthalmol.2010.42. PMID:20385946 doi:10.1001/archophthalmol.2010.42
  5. ↑ Shah S, Kumar Y, McLean B, Churchill A, Stoodley N, Rankin J, Rizzu P, van der Knaap M, Jardine P. A dominantly inherited mutation in collagen IV A1 (COL4A1) causing childhood onset stroke without porencephaly. Eur J Paediatr Neurol. 2010 Mar;14(2):182-7. doi: 10.1016/j.ejpn.2009.04.010., Epub 2009 May 28. PMID:19477666 doi:10.1016/j.ejpn.2009.04.010
  6. ↑ Plaisier E, Gribouval O, Alamowitch S, Mougenot B, Prost C, Verpont MC, Marro B, Desmettre T, Cohen SY, Roullet E, Dracon M, Fardeau M, Van Agtmael T, Kerjaschki D, Antignac C, Ronco P. COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms, and muscle cramps. N Engl J Med. 2007 Dec 27;357(26):2687-95. PMID:18160688 doi:10.1056/NEJMoa071906
  7. ↑ Plaisier E, Chen Z, Gekeler F, Benhassine S, Dahan K, Marro B, Alamowitch S, Paques M, Ronco P. Novel COL4A1 mutations associated with HANAC syndrome: a role for the triple helical CB3[IV] domain. Am J Med Genet A. 2010 Oct;152A(10):2550-5. doi: 10.1002/ajmg.a.33659. PMID:20818663 doi:10.1002/ajmg.a.33659
  8. ↑ Gould DB, Phalan FC, Breedveld GJ, van Mil SE, Smith RS, Schimenti JC, Aguglia U, van der Knaap MS, Heutink P, John SW. Mutations in Col4a1 cause perinatal cerebral hemorrhage and porencephaly. Science. 2005 May 20;308(5725):1167-71. PMID:15905400 doi:10.1126/science.1109418
  9. ↑ Breedveld G, de Coo IF, Lequin MH, Arts WF, Heutink P, Gould DB, John SW, Oostra B, Mancini GM. Novel mutations in three families confirm a major role of COL4A1 in hereditary porencephaly. J Med Genet. 2006 Jun;43(6):490-5. Epub 2005 Aug 17. PMID:16107487 doi:10.1136/jmg.2005.035584
  10. ↑ de Vries LS, Koopman C, Groenendaal F, Van Schooneveld M, Verheijen FW, Verbeek E, Witkamp TD, van der Worp HB, Mancini G. COL4A1 mutation in two preterm siblings with antenatal onset of parenchymal hemorrhage. Ann Neurol. 2009 Jan;65(1):12-8. doi: 10.1002/ana.21525. PMID:19194877 doi:10.1002/ana.21525
  11. ↑ Yoneda Y, Haginoya K, Arai H, Yamaoka S, Tsurusaki Y, Doi H, Miyake N, Yokochi K, Osaka H, Kato M, Matsumoto N, Saitsu H. De novo and inherited mutations in COL4A2, encoding the type IV collagen alpha2 chain cause porencephaly. Am J Hum Genet. 2012 Jan 13;90(1):86-90. doi: 10.1016/j.ajhg.2011.11.016. Epub, 2011 Dec 29. PMID:22209246 doi:10.1016/j.ajhg.2011.11.016
  12. ↑ Jeanne M, Labelle-Dumais C, Jorgensen J, Kauffman WB, Mancini GM, Favor J, Valant V, Greenberg SM, Rosand J, Gould DB. COL4A2 mutations impair COL4A1 and COL4A2 secretion and cause hemorrhagic stroke. Am J Hum Genet. 2012 Jan 13;90(1):91-101. doi: 10.1016/j.ajhg.2011.11.022. Epub, 2011 Dec 29. PMID:22209247 doi:10.1016/j.ajhg.2011.11.022
  13. ↑ Colorado PC, Torre A, Kamphaus G, Maeshima Y, Hopfer H, Takahashi K, Volk R, Zamborsky ED, Herman S, Sarkar PK, Ericksen MB, Dhanabal M, Simons M, Post M, Kufe DW, Weichselbaum RR, Sukhatme VP, Kalluri R. Anti-angiogenic cues from vascular basement membrane collagen. Cancer Res. 2000 May 1;60(9):2520-6. PMID:10811134
  14. ↑ Zheng JP, Tang HY, Chen XJ, Yu BF, Xie J, Wu TC. Construction of recombinant plasmid and prokaryotic expression in E. coli and biological activity analysis of human placenta arresten gene. Hepatobiliary Pancreat Dis Int. 2006 Feb;5(1):74-9. PMID:16481288
  15. ↑ Sudhakar A, Nyberg P, Keshamouni VG, Mannam AP, Li J, Sugimoto H, Cosgrove D, Kalluri R. Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic activity mediated by alpha1beta1 integrin. J Clin Invest. 2005 Oct;115(10):2801-10. Epub 2005 Sep 8. PMID:16151532 doi:10.1172/JCI24813
  16. ↑ Nyberg P, Xie L, Sugimoto H, Colorado P, Sund M, Holthaus K, Sudhakar A, Salo T, Kalluri R. Characterization of the anti-angiogenic properties of arresten, an alpha1beta1 integrin-dependent collagen-derived tumor suppressor. Exp Cell Res. 2008 Nov 1;314(18):3292-305. doi: 10.1016/j.yexcr.2008.08.011. Epub, 2008 Aug 26. PMID:18775695 doi:10.1016/j.yexcr.2008.08.011
  17. ↑ Colorado PC, Torre A, Kamphaus G, Maeshima Y, Hopfer H, Takahashi K, Volk R, Zamborsky ED, Herman S, Sarkar PK, Ericksen MB, Dhanabal M, Simons M, Post M, Kufe DW, Weichselbaum RR, Sukhatme VP, Kalluri R. Anti-angiogenic cues from vascular basement membrane collagen. Cancer Res. 2000 May 1;60(9):2520-6. PMID:10811134
  18. ↑ Zheng JP, Tang HY, Chen XJ, Yu BF, Xie J, Wu TC. Construction of recombinant plasmid and prokaryotic expression in E. coli and biological activity analysis of human placenta arresten gene. Hepatobiliary Pancreat Dis Int. 2006 Feb;5(1):74-9. PMID:16481288
  19. ↑ Sudhakar A, Nyberg P, Keshamouni VG, Mannam AP, Li J, Sugimoto H, Cosgrove D, Kalluri R. Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic activity mediated by alpha1beta1 integrin. J Clin Invest. 2005 Oct;115(10):2801-10. Epub 2005 Sep 8. PMID:16151532 doi:10.1172/JCI24813
  20. ↑ Nyberg P, Xie L, Sugimoto H, Colorado P, Sund M, Holthaus K, Sudhakar A, Salo T, Kalluri R. Characterization of the anti-angiogenic properties of arresten, an alpha1beta1 integrin-dependent collagen-derived tumor suppressor. Exp Cell Res. 2008 Nov 1;314(18):3292-305. doi: 10.1016/j.yexcr.2008.08.011. Epub, 2008 Aug 26. PMID:18775695 doi:10.1016/j.yexcr.2008.08.011
  21. ↑ Kamphaus GD, Colorado PC, Panka DJ, Hopfer H, Ramchandran R, Torre A, Maeshima Y, Mier JW, Sukhatme VP, Kalluri R. Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor growth. J Biol Chem. 2000 Jan 14;275(2):1209-15. PMID:10625665
  22. ↑ Panka DJ, Mier JW. Canstatin inhibits Akt activation and induces Fas-dependent apoptosis in endothelial cells. J Biol Chem. 2003 Sep 26;278(39):37632-6. Epub 2003 Jul 22. PMID:12876280 doi:10.1074/jbc.M307339200
  23. ↑ Magnon C, Galaup A, Mullan B, Rouffiac V, Bouquet C, Bidart JM, Griscelli F, Opolon P, Perricaudet M. Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with alphavbeta3 and alphavbeta5 integrins. Cancer Res. 2005 May 15;65(10):4353-61. PMID:15899827 doi:10.1158/0008-5472.CAN-04-3536
  24. ↑ Kamphaus GD, Colorado PC, Panka DJ, Hopfer H, Ramchandran R, Torre A, Maeshima Y, Mier JW, Sukhatme VP, Kalluri R. Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor growth. J Biol Chem. 2000 Jan 14;275(2):1209-15. PMID:10625665
  25. ↑ Panka DJ, Mier JW. Canstatin inhibits Akt activation and induces Fas-dependent apoptosis in endothelial cells. J Biol Chem. 2003 Sep 26;278(39):37632-6. Epub 2003 Jul 22. PMID:12876280 doi:10.1074/jbc.M307339200
  26. ↑ Magnon C, Galaup A, Mullan B, Rouffiac V, Bouquet C, Bidart JM, Griscelli F, Opolon P, Perricaudet M. Canstatin acts on endothelial and tumor cells via mitochondrial damage initiated through interaction with alphavbeta3 and alphavbeta5 integrins. Cancer Res. 2005 May 15;65(10):4353-61. PMID:15899827 doi:10.1158/0008-5472.CAN-04-3536
  27. ↑ Than ME, Henrich S, Huber R, Ries A, Mann K, Kuhn K, Timpl R, Bourenkov GP, Bartunik HD, Bode W. The 1.9-A crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proc Natl Acad Sci U S A. 2002 May 14;99(10):6607-12. PMID:12011424 doi:10.1073/pnas.062183499

1li1, resolution 1.90Å

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