scholarly journals Two Different Heparin-binding Domains in the Triple-helical Domain of ColQ, the Collagen Tail Subunit of Synaptic Acetylcholinesterase

2003 ◽  
Vol 278 (26) ◽  
pp. 23233-23242 ◽  
Author(s):  
Paola Deprez ◽  
Nibaldo C. Inestrosa ◽  
Eric Krejci
Keyword(s):  
Heparin Binding ◽  
Helical Domain ◽  
Binding Domains ◽  
Triple Helical Domain

scholarly journals Pseudomonas aeruginosa uses multiple receptors for adherence to laminin during infection of the respiratory tract and skin wounds

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Magnus Paulsson ◽  
Yu-Ching Su ◽  
Tamara Ringwood ◽  
Fabian Uddén ◽  
Kristian Riesbeck
Keyword(s):  
Cystic Fibrosis ◽  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Heparin Binding ◽  
Surface Receptors ◽  
Binding Domains ◽  
Laminin Receptors ◽  
Multiple Receptors ◽  
Main Component ◽  
Tract Infections

AbstractPseudomonas aeruginosa efficiently adheres to human tissues, including the lungs and skin, causing infections that are difficult to treat. Laminin is a main component of the extracellular matrix, and in this study we defined bacterial laminin receptors on P. aeruginosa. Persistent clinical P. aeruginosa isolates from patients with cystic fibrosis, wounds or catheter-related urinary tract infections bound more laminin compared to blood isolates. Laminin receptors in the outer membrane were revealed by 2D-immunblotting, and the specificities of interactions were confirmed with ELISA and biolayer interferometry. Four new high-affinity laminin receptors were identified in the outer membrane; EstA, OprD, OprG and PA3923. Mutated bacteria devoid of these receptors adhered poorly to immobilized laminin. All bacterial receptors bound to the heparin-binding domains on LG4 and LG5 of the laminin alpha chain as assessed with truncated laminin fragments, transmission electron microscopy and inhibition by heparin. In conclusion, P. aeruginosa binds laminin via multiple surface receptors, and isolates from lungs of cystic fibrosis patients bound significantly more laminin compared to bacteria isolated from the skin and urine. Since laminin is abundant in both the lungs and skin, we suggest that laminin binding is an important mechanism in P. aeruginosa pathogenesis.

The fibril structure of type V collagen triple-helical domain

Micron ◽  
2001 ◽  
Vol 32 (3) ◽  
pp. 317-323 ◽  
Author(s):  
K Mizuno ◽  
E Adachi ◽  
Y Imamura ◽  
O Katsumata ◽  
T Hayashi
Keyword(s):  
Type V Collagen ◽  
Helical Domain ◽  
Fibril Structure ◽  
Triple Helical Domain ◽  
Type V

scholarly journals Proteolytic modification of the heparin-binding affinity of extracellular superoxide dismutase

1993 ◽  
Vol 290 (2) ◽  
pp. 623-626 ◽  
Author(s):  
K Karlsson ◽  
A Edlund ◽  
J Sandström ◽  
S L Marklund
Keyword(s):  
Superoxide Dismutase ◽  
Binding Affinity ◽  
Heparan Sulphate ◽  
Limited Proteolysis ◽  
Size Exclusion ◽  
Extracellular Superoxide Dismutase ◽  
Heparin Binding ◽  
Binding Domains ◽  
Heparin Affinity

The heparin-binding affinity of the tetrameric extracellular superoxide dismutase (EC-SOD) is a result of the cooperative effect of the heparin-binding domains of the subunits, located in the hydrophilic, strongly positively charged C-terminal ends. EC-SOD C, the high-heparin-affinity type, exposed to immobilized trypsin and plasmin was found to rapidly lose its affinity for heparin, without any loss of enzymic activity or major change in molecular mass as judged by size-exclusion chromatography. Heparin and dextran sulphate 5000 inhibited the proteolysis, suggesting that EC-SOD C sequestered by heparan sulphate proteoglycan in vivo is partially protected against proteolysis. The loss of heparin-affinity occurred with the stepwise formation of intermediates, and the pattern upon chromatography on heparin-Sepharose and subsequent immunoblotting was compatible with the notion that the changes are due to sequential truncations of heparin-binding domains from subunits composing the EC-SOD tetramers. A similar pattern with intermediates and apparent truncations has previously been found with EC-SOD of human plasma. The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.

scholarly journals Identification of novel heparin-binding domains of vitronectin

FEBS Letters ◽  
1997 ◽  
Vol 407 (2) ◽  
pp. 169-172 ◽  
Author(s):  
Olin D Liang ◽  
Sylvia Rosenblatt ◽  
Gursharan S Chhatwal ◽  
Klaus T Preissner
Keyword(s):  
Heparin Binding ◽  
Binding Domains

Adhesion of lymphoid cells to the carboxyl-terminal heparin-binding domains of fibronectin

1989 ◽  
Vol 181 (2) ◽  
pp. 348-361 ◽  
Author(s):  
Nan-Shih Liao ◽  
Joni St. John ◽  
James B. McCarthy ◽  
Leo T. Furcht ◽  
H.Tak Cheung
Keyword(s):  
Lymphoid Cells ◽  
Heparin Binding ◽  
Binding Domains ◽  
Carboxyl Terminal

Collagen XXII binds to collagen-binding integrins via the novel motifs GLQGER and GFKGER

2014 ◽  
Vol 459 (1) ◽  
pp. 217-227 ◽  
Author(s):  
Daniela Zwolanek ◽  
Guido Veit ◽  
Johannes A. Eble ◽  
Donald Gullberg ◽  
Florence Ruggiero ◽  
...  
Keyword(s):  
Cell Attachment ◽  
Hacat Cells ◽  
The Novel ◽  
Collagen Binding ◽  
Binding Motifs ◽  
Helical Domain ◽  
Triple Helical Domain

Cell attachment to collagens is mediated by integrins. In the present study, we define two new integrin-binding motifs, GLQGER and GFKGER, within the collagen XXII triple helical domain. Mutation of the two motifs in collagen XXII abolishes the binding to HaCaT cells completely.

scholarly journals Large Deletions Targeting the Triple-Helical Domain of Collagen VII Lead to Mild Acral Dominant Dystrophic Epidermolysis Bullosa

2018 ◽  
Vol 138 (4) ◽  
pp. 987-991 ◽  
Author(s):  
Nadja Chmel ◽  
Olivier Bornert ◽  
Ingrid Hausser ◽  
Gabriele Grüninger ◽  
Wiktor Borozkin ◽  
...  
Keyword(s):  
Epidermolysis Bullosa ◽  
Dystrophic Epidermolysis Bullosa ◽  
Helical Domain ◽  
Large Deletions ◽  
Triple Helical Domain ◽  
Collagen Vii
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