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Article ; Online: Platelet glycoprotein VI as a mediator of metastasis.

Farndale, R W

Journal of thrombosis and haemostasis : JTH

2009 Volume 7, Issue 10, Page(s) 1711–1712

MeSH term(s)	Animals ; Blood Platelets/metabolism ; Blood Platelets/physiology ; Cell Communication ; Cell-Derived Microparticles/physiology ; Drug Delivery Systems ; Humans ; Mice ; Models, Biological ; Neoplasm Metastasis/physiopathology ; Neoplastic Cells, Circulating ; Neovascularization, Pathologic/physiopathology ; Organ Specificity ; Platelet Activation ; Platelet Membrane Glycoproteins/physiology
Chemical Substances	Platelet Membrane Glycoproteins ; platelet membrane glycoprotein VI
Language	English
Publishing date	2009-08-11
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/j.1538-7836.2009.03566.x
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Article ; Online: The voltage-gated K

Wright, Joy R / Jones, Sarah / Parvathy, Sasikumar / Kaczmarek, Leonard K / Forsythe, Ian / Farndale, Richard W / Gibbins, Jonathan M / Mahaut-Smith, Martyn P

Platelets

2021 Volume 33, Issue 3, Page(s) 451–461

Abstract: Kv1.3 is a voltage-gated ... ...

Abstract	Kv1.3 is a voltage-gated K
MeSH term(s)	Blood Platelets/metabolism ; Collagen/metabolism ; Humans ; Integrin alpha2beta1/metabolism ; Platelet Adhesiveness/physiology ; Platelet Aggregation/physiology ; Potassium Channels, Voltage-Gated/metabolism
Chemical Substances	Integrin alpha2beta1 ; Potassium Channels, Voltage-Gated ; Collagen (9007-34-5)
Language	English
Publishing date	2021-08-04
Publishing country	England
Document type	Journal Article
ZDB-ID	1034283-7
ISSN	1369-1635 ; 0953-7104
ISSN (online)	1369-1635
ISSN	0953-7104
DOI	10.1080/09537104.2021.1942818
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Article ; Online: Tyrosine-sulfated dermatopontin shares multiple binding sites and recognition determinants on triple-helical collagens with proteins implicated in cell adhesion and collagen folding, fibrillogenesis, cross-linking, and degradation.

Jensen, Morten M / Bonna, Arkadiusz / Frederiksen, Sigurd J / Hamaia, Samir W / Højrup, Peter / Farndale, Richard W / Karring, Henrik

Biochimica et biophysica acta. Proteins and proteomics

2022 Volume 1870, Issue 5, Page(s) 140771

Abstract: ... of the Collagen Toolkit II peptides. Substituting any of the three arginine residues (R) with alanine ...

Abstract	Dermatopontin (DPT), a small extracellular matrix protein that stimulates collagen fibrillogenesis, contains sulfotyrosine residues but neither its level of sulfation nor its binding sites on fibrillar collagens are known. Here, we discovered that DPT is present in a relatively high mass concentration (~ 0.02%) in porcine corneal stroma, from which we purified five DPT charge variants (A-E) containing up to six sulfations. The major variant (C), containing four sulfotyrosine residues, was used to locate binding sites for DPT on triple-helical collagens II and III using the Collagen Toolkits. DPT-binding loci included the triple helix crosslinking sites and collagenase cleavage site. We find that strong DPT-binding sites on triple-helical collagen comprise an arginine-rich, positively-charged sequence that also contains hydrophobic residues. This collagen-binding signature of DPT is similar to that of the chaperone HSP47. Thus, we propose that DPT assumes the role of HSP47 as a collagen chaperone during and after the secretion. Peptide II-44, harbouring the conserved collagenase cleavage site, shows the strongest DPT-binding of the Collagen Toolkit II peptides. Substituting any of the three arginine residues (R) with alanine in the sequence GLAGQRGIVGLOGQRGER of II-44 resulted in almost complete loss of DPT binding. Since osteogenesis imperfecta, spondyloepiphyseal dysplasia, and spondyloepimetaphyseal dysplasia congenita are associated with missense mutations that substitute the corresponding arginine residues in collagens alpha-1(I) and alpha-1(II), we suggest that disrupted DPT binding to fibrillar collagens may contribute to these connective tissue disorders. In conclusion, the present work provides a cornerstone for further elucidation of the role of DPT.
MeSH term(s)	Animals ; Arginine ; Binding Sites ; Cell Adhesion ; Collagen/chemistry ; Collagen/metabolism ; Collagen Type I ; Fibrillar Collagens/chemistry ; Fibrillar Collagens/metabolism ; Peptides/chemistry ; Swine ; Tyrosine/analogs & derivatives
Chemical Substances	Collagen Type I ; Fibrillar Collagens ; Peptides ; tyrosine O-sulfate (29166358BF) ; Tyrosine (42HK56048U) ; Collagen (9007-34-5) ; Arginine (94ZLA3W45F)
Language	English
Publishing date	2022-03-16
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2918798-9
ISSN	1878-1454 ; 1570-9639
ISSN (online)	1878-1454
ISSN	1570-9639
DOI	10.1016/j.bbapap.2022.140771
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Article: Integrin recognition motifs in the human collagens.

Hamaia, Samir / Farndale, Richard W

Advances in experimental medicine and biology

2014 Volume 819, Page(s) 127–142

Abstract: ... hydroxyproline) and x'' is often R). Here, we review the variations within such sequences that support integrin ...

Abstract	The best-known (fibrillar) collagens support cellular adhesion primarily through a subset of collagen-binding integrins, α1β1, α2β1, α10β1 and α11β1, which have been shown to recognise a series of similar sequences. These contain Gxx'GEx''motifs (where x is a hydrophobic residue, x' is usually O (hydroxyproline) and x'' is often R). Here, we review the variations within such sequences that support integrin reactivity, and their distribution across the 28 human collagens. The main basis for our understanding is the use of triple-helical, homotrimeric collagen peptides, but this work is far from exhaustive, and there is good evidence that heterotrimeric collagens where the sequence of interest occurs in two or even just a single chain may still support integrin binding. The fibrillar collagens I, II and III are rich in GxOGER motifs, whereas GxOGEK is more widely distributed, and less frequent in these three archetypal fibrillar collagens.
MeSH term(s)	Amino Acid Motifs ; Collagen/chemistry ; Collagen/metabolism ; Humans ; Integrins/metabolism ; Protein Engineering ; Protein Structure, Tertiary
Chemical Substances	Integrins ; Collagen (9007-34-5)
Language	English
Publishing date	2014-07-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	2214-8019 ; 0065-2598
ISSN (online)	2214-8019
ISSN	0065-2598
DOI	10.1007/978-94-017-9153-3_9
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Article ; Online: Structural studies of the MMP-3 interaction with triple-helical collagen introduce new roles for the enzyme in tissue remodelling

Szymon W. Manka / Dominique Bihan / Richard W. Farndale

Scientific Reports, Vol 9, Iss 1, Pp 1-

2019 Volume 14

Abstract: Abstract Matrix metalloproteinase-3 (MMP-3) participates in normal extracellular matrix turnover during embryonic development, organ morphogenesis and wound healing, and in tissue-destruction associated with aneurysm, cancer, arthritis and heart failure. ...

Abstract	Abstract Matrix metalloproteinase-3 (MMP-3) participates in normal extracellular matrix turnover during embryonic development, organ morphogenesis and wound healing, and in tissue-destruction associated with aneurysm, cancer, arthritis and heart failure. Despite its inability to cleave triple-helical collagens, MMP-3 can still bind to them, but the mechanism, location and role of binding are not known. We used the Collagen Toolkits, libraries of triple-helical peptides that embrace the entire helical domains of collagens II and III, to map MMP-3 interaction sites. The enzyme recognises five sites on collagen II and three sites on collagen III. They share a glycine-phenylalanine-hydroxyproline/alanine (GFO/A) motif that is recognised by the enzyme in a context-dependent manner. Neither MMP-3 zymogen (proMMP-3) nor the individual catalytic (Cat) and hemopexin (Hpx) domains of MMP-3 interact with the peptides, revealing cooperative binding of both domains to the triple helix. The Toolkit binding data combined with molecular modelling enabled us to deduce the putative collagen-binding mode of MMP-3, where all three collagen chains make contacts with the enzyme in the valley running across both Cat and Hpx domains. The observed binding pattern casts light on how MMP-3 could regulate collagen turnover and compete with various collagen-binding proteins regulating cell adhesion and proliferation.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2019-12-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
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Article ; Online: Covalent Capture of a Heterotrimeric Collagen Helix.

Li, I-Che / Hulgan, Sarah A H / Walker, Douglas R / Farndale, Richard W / Hartgerink, Jeffrey D / Jalan, Abhishek A

Organic letters

2019 Volume 21, Issue 14, Page(s) 5480–5484

Abstract: Stabilizing the three-dimensional structure of supramolecular materials can be accomplished through covalent capture of the assembled system. The lysine-aspartate charge pairs designed to direct the self-assembly of a collagen triple helix were ... ...

Abstract	Stabilizing the three-dimensional structure of supramolecular materials can be accomplished through covalent capture of the assembled system. The lysine-aspartate charge pairs designed to direct the self-assembly of a collagen triple helix were subsequently used to covalently capture the helix through proximity-directed amide bond formation using EDC/HOBT activation. The triple helix thus stabilized maintains its folded structure and can now be used for applications previously inaccessible due to problematic folding equilibria.
MeSH term(s)	Amino Acid Sequence ; Collagen/chemistry ; Models, Molecular ; Protein Conformation, alpha-Helical ; Protein Multimerization
Chemical Substances	Collagen (9007-34-5)
Language	English
Publishing date	2019-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1523-7052
ISSN (online)	1523-7052
DOI	10.1021/acs.orglett.9b01771
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Article: Collagen scaffolds functionalized with triple-helical peptides support 3D HUVEC culture.

Malcor, Jean-Daniel / Hunter, Emma J / Davidenko, Natalia / Bax, Daniel V / Cameron, Ruth / Best, Serena / Sinha, Sanjay / Farndale, Richard W

Regenerative biomaterials

2020 Volume 7, Issue 5, Page(s) 471–482

Abstract: Porous biomaterials which provide a structural and biological support for cells have immense potential in tissue engineering and cell-based therapies for tissue repair. Collagen biomaterials that can host endothelial cells represent promising tools for ... ...

Abstract	Porous biomaterials which provide a structural and biological support for cells have immense potential in tissue engineering and cell-based therapies for tissue repair. Collagen biomaterials that can host endothelial cells represent promising tools for the vascularization of engineered tissues. Three-dimensional collagen scaffolds possessing controlled architecture and mechanical stiffness are obtained through freeze-drying of collagen suspensions, followed by chemical cross-linking which maintains their stability. However, cross-linking scaffolds renders their biological activity suboptimal for many cell types, including human umbilical vein endothelial cells (HUVECs), by inhibiting cell-collagen interactions. Here, we have improved crucial HUVEC interactions with such cross-linked collagen biomaterials by covalently coupling combinations of triple-helical peptides (THPs). These are ligands for collagen-binding cell-surface receptors (integrins or discoidin domain receptors) or secreted proteins (SPARC and von Willebrand factor). THPs enhanced HUVEC adhesion, spreading and proliferation on 2D collagen films. THPs grafted to 3D-cross-linked collagen scaffolds promoted cell survival over seven days. This study demonstrates that THP-functionalized collagen scaffolds are promising candidates for hosting endothelial cells with potential for the production of vascularized engineered tissues in regenerative medicine applications.
Language	English
Publishing date	2020-08-18
Publishing country	England
Document type	Journal Article
ZDB-ID	2799042-4
ISSN	2056-3426 ; 2056-3418
ISSN (online)	2056-3426
ISSN	2056-3418
DOI	10.1093/rb/rbaa025
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Article ; Online: Modified platelet deposition on matrix metalloproteinase 13 digested collagen I.

Howes, J-M / Pugh, N / Knäuper, V / Farndale, R W

Journal of thrombosis and haemostasis : JTH

2015 Volume 13, Issue 12, Page(s) 2253–2259

Abstract: Background: Atherothrombosis underlies acute coronary syndromes, including unstable angina and acute myocardial infarction. Within the unstable plaque, monocytes express collagenolytic matrix metalloproteinases (MMPs), including MMP-13, which degrades ... ...

Abstract	Background: Atherothrombosis underlies acute coronary syndromes, including unstable angina and acute myocardial infarction. Within the unstable plaque, monocytes express collagenolytic matrix metalloproteinases (MMPs), including MMP-13, which degrades fibrous collagen. Following rupture, vessel wall components including degraded collagen are exposed to circulating platelets. Platelet receptors then mediate the recruitment and activation of platelets to form a thrombus, blocking blood flow and resulting in myocardial infarction and sudden death. Objectives: Here we aim to provide information on the effects of collagen degradation on platelet adhesion and thrombus formation. Methods: Using increasing concentrations of MMP-13, we induced progressive degradation of fibrous and monomeric collagen I, visualized by electrophoresis, and then investigated the capacity of the resulting fragments to support static platelet adhesion and thrombus formation in whole flowing blood. Results: Both integrin and glycoprotein VI-dependent interactions with fibrous collagen underpin high levels of platelet adhesion under both conditions, with little obvious effect of MMP-13 treatment. Static platelet adhesion to monomeric collagen was strongly α2β1-dependent regardless of degradation status. Under flow conditions, partially degraded monomeric collagen supported increased thrombus deposition at 10 μg mL(-1) MMP-13, falling close to background when collagen degradation was complete (100 μg mL(-1) MMP-13). Conclusions: New binding activities come into play after partial digestion of collagen monomers, and net platelet-reactivity through all axes is abolished as degradation becomes more complete.
MeSH term(s)	Blood Platelets/metabolism ; Collagen Type I/metabolism ; Electrophoresis, Polyacrylamide Gel ; Humans ; Integrin alpha2beta1/metabolism ; Matrix Metalloproteinase 13/metabolism ; Platelet Adhesiveness ; Proteolysis ; Thrombosis/blood ; Thrombosis/enzymology ; Thrombosis/metabolism
Chemical Substances	Collagen Type I ; Integrin alpha2beta1 ; MMP13 protein, human (EC 3.4.24.-) ; Matrix Metalloproteinase 13 (EC 3.4.24.-)
Language	English
Publishing date	2015-11-30
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2112661-6
ISSN	1538-7836 ; 1538-7933
ISSN (online)	1538-7836
ISSN	1538-7933
DOI	10.1111/jth.13166
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Article ; Online: Chain alignment of collagen I deciphered using computationally designed heterotrimers.

Jalan, Abhishek A / Sammon, Douglas / Hartgerink, Jeffrey D / Brear, Paul / Stott, Katherine / Hamaia, Samir W / Hunter, Emma J / Walker, Douglas R / Leitinger, Birgit / Farndale, Richard W

Nature chemical biology

2020 Volume 16, Issue 4, Page(s) 423–429

Abstract: The most abundant member of the collagen protein family, collagen I (also known as type I collagen; COL1), is composed of one unique (chain B) and two similar (chain A) polypeptides that self-assemble with one amino acid offset into a heterotrimeric ... ...

Abstract	The most abundant member of the collagen protein family, collagen I (also known as type I collagen; COL1), is composed of one unique (chain B) and two similar (chain A) polypeptides that self-assemble with one amino acid offset into a heterotrimeric triple helix. Given the offset, chain B can occupy either the leading (BAA), middle (ABA) or trailing (AAB) position of the triple helix, yielding three isomeric biomacromolecules with different protein recognition properties. Despite five decades of intensive research, there is no consensus on the position of chain B in COL1. Here, three triple-helical heterotrimers that each contain a putative von Willebrand factor (VWF) and discoidin domain receptor (DDR) recognition sequence from COL1 were designed with chain B permutated in all three positions. AAB demonstrated a strong preference for both VWF and DDR, and also induced higher levels of cellular DDR phosphorylation. Thus, we resolve this long-standing mystery and show that COL1 adopts an AAB register.
MeSH term(s)	Amino Acid Sequence ; Amino Acids ; Collagen/chemistry ; Collagen/metabolism ; Collagen Type I/chemistry ; Collagen Type I/metabolism ; Computational Biology/methods ; Humans ; Models, Molecular ; Peptides/chemistry ; Protein Conformation
Chemical Substances	Amino Acids ; Collagen Type I ; Peptides ; Collagen (9007-34-5)
Language	English
Publishing date	2020-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2202962-X
ISSN	1552-4469 ; 1552-4450
ISSN (online)	1552-4469
ISSN	1552-4450
DOI	10.1038/s41589-019-0435-y
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Zs.A 6251: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
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Article: Tyrosine-sulfated dermatopontin shares multiple binding sites and recognition determinants on triple-helical collagens with proteins implicated in cell adhesion and collagen folding, fibrillogenesis, cross-linking, and degradation

Jensen, Morten M. / Bonna, Arkadiusz / Frederiksen, Sigurd J. / Hamaia, Samir W. / Højrup, Peter / Farndale, Richard W. / Karring, Henrik

Biochimica et biophysica acta. 2022 Mar. 13,

2022

Abstract: ... of the Collagen Toolkit II peptides. Substituting any of the three arginine residues (R) with alanine ...

Abstract	Dermatopontin (DPT), a small extracellular matrix protein that stimulates collagen fibrillogenesis, contains sulfotyrosine residues but neither its level of sulfation nor its binding sites on fibrillar collagens are known. Here, we discovered that DPT is present in a relatively high mass concentration (~ 0.02%) in porcine corneal stroma, from which we purified five DPT charge variants (A-E) containing up to six sulfations. The major variant (C), containing four sulfotyrosine residues, was used to locate binding sites for DPT on triple-helical collagens II and III using the Collagen Toolkits. DPT-binding loci included the triple helix crosslinking sites and collagenase cleavage site. We find that strong DPT-binding sites on triple-helical collagen comprise an arginine-rich, positively-charged sequence that also contains hydrophobic residues. This collagen-binding signature of DPT is similar to that of the chaperone HSP47. Thus, we propose that DPT assumes the role of HSP47 as a collagen chaperone during and after the secretion. Peptide II-44, harbouring the conserved collagenase cleavage site, shows the strongest DPT-binding of the Collagen Toolkit II peptides. Substituting any of the three arginine residues (R) with alanine in the sequence GLAGQRGIVGLOGQRGER of II-44 resulted in almost complete loss of DPT binding. Since osteogenesis imperfecta, spondyloepiphyseal dysplasia, and spondyloepimetaphyseal dysplasia congenita are associated with missense mutations that substitute the corresponding arginine residues in collagens alpha-1(I) and alpha-1(II), we suggest that disrupted DPT binding to fibrillar collagens may contribute to these connective tissue disorders. In conclusion, the present work provides a cornerstone for further elucidation of the role of DPT.
Keywords	alanine ; arginine ; bone formation ; cell adhesion ; collagen ; collagenase ; cornea ; crosslinking ; extracellular matrix ; hydrophobicity ; peptides ; secretion ; swine
Language	English
Dates of publication	2022-0313
Publishing place	Elsevier B.V.
Document type	Article
Note	Pre-press version
ZDB-ID	2918798-9
ISSN	1878-1454 ; 1570-9639
ISSN (online)	1878-1454
ISSN	1570-9639
DOI	10.1016/j.bbapap.2022.140771
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