Eintrag weiter verarbeiten
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1
Gespeichert in:
| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , , , |
| In: | European Journal of Biochemistry, 215, 1993, 1, S. 151-159 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus |
|---|---|
| author |
KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus |
| spellingShingle |
KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus European Journal of Biochemistry Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 Biochemistry |
| author_sort |
kern, andreas |
| spelling |
KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1993.tb18017.x <jats:p>The triple‐helical cyanogen‐bromide‐derived fragment CB3[IV] of collagen IV, located 100 nm from the N‐terminus of the molecule, contains the binding sites for the integrins α1β1 and α2β1. To investigate the interaction of these integrins and collagen IV, we performed solid‐phase and inhibition assays using as receptor isolated α1β1 and α2β1. The ligands used were the binding‐site‐bearing trimeric peptide CB3[IV] and its shorter tryptic fragments F1–F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for α1β1 and α2β1 were in different but adjacent areas of CB3[IV]. Triple‐helical conformation and distinct primary structures were required for the interaction. Dissociation constants (<jats:italic>K</jats:italic><jats:sub>a</jats:sub>), for the affinity of integrins for collagen IV, were determined in the 1‐nM range in the presence of Mn<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup>. In the absence of Mn<jats:sup>2+</jats:sup>, the <jats:italic>K</jats:italic><jats:sub>d</jats:sub> values indicated a 30–60‐fold decrease in the affinities, which for α2β1 was further reduced by adding Ca<jats:sup>2+</jats:sup>. In the presence of Ca<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup> the affinity of collagen IV for α1β1 was four‐times higher than for α2β1.</jats:p> Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 European Journal of Biochemistry |
| doi_str_mv |
10.1111/j.1432-1033.1993.tb18017.x |
| facet_avail |
Online Free |
| finc_class_facet |
Chemie und Pharmazie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTkzLnRiMTgwMTcueA |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTkzLnRiMTgwMTcueA |
| institution |
DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 |
| imprint |
Wiley, 1993 |
| imprint_str_mv |
Wiley, 1993 |
| issn |
0014-2956 1432-1033 |
| issn_str_mv |
0014-2956 1432-1033 |
| language |
English |
| mega_collection |
Wiley (CrossRef) |
| match_str |
kern1993interactionoftypeivcollagenwiththeisolatedintegrinsa1b1anda2b1 |
| publishDateSort |
1993 |
| publisher |
Wiley |
| recordtype |
ai |
| record_format |
ai |
| series |
European Journal of Biochemistry |
| source_id |
49 |
| title |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_unstemmed |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_full |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_fullStr |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_full_unstemmed |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_short |
Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_sort |
interaction of type iv collagen with the isolated integrins α1β1 and α2β1 |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1993.tb18017.x |
| publishDate |
1993 |
| physical |
151-159 |
| description |
<jats:p>The triple‐helical cyanogen‐bromide‐derived fragment CB3[IV] of collagen IV, located 100 nm from the N‐terminus of the molecule, contains the binding sites for the integrins α1β1 and α2β1. To investigate the interaction of these integrins and collagen IV, we performed solid‐phase and inhibition assays using as receptor isolated α1β1 and α2β1. The ligands used were the binding‐site‐bearing trimeric peptide CB3[IV] and its shorter tryptic fragments F1–F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for α1β1 and α2β1 were in different but adjacent areas of CB3[IV]. Triple‐helical conformation and distinct primary structures were required for the interaction. Dissociation constants (<jats:italic>K</jats:italic><jats:sub>a</jats:sub>), for the affinity of integrins for collagen IV, were determined in the 1‐nM range in the presence of Mn<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup>. In the absence of Mn<jats:sup>2+</jats:sup>, the <jats:italic>K</jats:italic><jats:sub>d</jats:sub> values indicated a 30–60‐fold decrease in the affinities, which for α2β1 was further reduced by adding Ca<jats:sup>2+</jats:sup>. In the presence of Ca<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup> the affinity of collagen IV for α1β1 was four‐times higher than for α2β1.</jats:p> |
| container_issue |
1 |
| container_start_page |
151 |
| container_title |
European Journal of Biochemistry |
| container_volume |
215 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792343625291530246 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T16:54:40.398Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Interaction+of+type+IV+collagen+with+the+isolated+integrins+%CE%B11%CE%B21+and+%CE%B12%CE%B21&rft.date=1993-07-01&genre=article&issn=1432-1033&volume=215&issue=1&spage=151&epage=159&pages=151-159&jtitle=European+Journal+of+Biochemistry&atitle=Interaction+of+type+IV+collagen+with+the+isolated+integrins+%CE%B11%CE%B21+and+%CE%B12%CE%B21&aulast=K%C3%9CHN&aufirst=Klaus&rft_id=info%3Adoi%2F10.1111%2Fj.1432-1033.1993.tb18017.x&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792343625291530246 |
| author | KERN, Andreas, EBLE, Johannes, GOLBIK, Ralph, KÜHN, Klaus |
| author_facet | KERN, Andreas, EBLE, Johannes, GOLBIK, Ralph, KÜHN, Klaus, KERN, Andreas, EBLE, Johannes, GOLBIK, Ralph, KÜHN, Klaus |
| author_sort | kern, andreas |
| container_issue | 1 |
| container_start_page | 151 |
| container_title | European Journal of Biochemistry |
| container_volume | 215 |
| description | <jats:p>The triple‐helical cyanogen‐bromide‐derived fragment CB3[IV] of collagen IV, located 100 nm from the N‐terminus of the molecule, contains the binding sites for the integrins α1β1 and α2β1. To investigate the interaction of these integrins and collagen IV, we performed solid‐phase and inhibition assays using as receptor isolated α1β1 and α2β1. The ligands used were the binding‐site‐bearing trimeric peptide CB3[IV] and its shorter tryptic fragments F1–F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for α1β1 and α2β1 were in different but adjacent areas of CB3[IV]. Triple‐helical conformation and distinct primary structures were required for the interaction. Dissociation constants (<jats:italic>K</jats:italic><jats:sub>a</jats:sub>), for the affinity of integrins for collagen IV, were determined in the 1‐nM range in the presence of Mn<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup>. In the absence of Mn<jats:sup>2+</jats:sup>, the <jats:italic>K</jats:italic><jats:sub>d</jats:sub> values indicated a 30–60‐fold decrease in the affinities, which for α2β1 was further reduced by adding Ca<jats:sup>2+</jats:sup>. In the presence of Ca<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup> the affinity of collagen IV for α1β1 was four‐times higher than for α2β1.</jats:p> |
| doi_str_mv | 10.1111/j.1432-1033.1993.tb18017.x |
| facet_avail | Online, Free |
| finc_class_facet | Chemie und Pharmazie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTExMS9qLjE0MzItMTAzMy4xOTkzLnRiMTgwMTcueA |
| imprint | Wiley, 1993 |
| imprint_str_mv | Wiley, 1993 |
| institution | DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1 |
| issn | 0014-2956, 1432-1033 |
| issn_str_mv | 0014-2956, 1432-1033 |
| language | English |
| last_indexed | 2024-03-01T16:54:40.398Z |
| match_str | kern1993interactionoftypeivcollagenwiththeisolatedintegrinsa1b1anda2b1 |
| mega_collection | Wiley (CrossRef) |
| physical | 151-159 |
| publishDate | 1993 |
| publishDateSort | 1993 |
| publisher | Wiley |
| record_format | ai |
| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | KERN, Andreas EBLE, Johannes GOLBIK, Ralph KÜHN, Klaus 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1993.tb18017.x <jats:p>The triple‐helical cyanogen‐bromide‐derived fragment CB3[IV] of collagen IV, located 100 nm from the N‐terminus of the molecule, contains the binding sites for the integrins α1β1 and α2β1. To investigate the interaction of these integrins and collagen IV, we performed solid‐phase and inhibition assays using as receptor isolated α1β1 and α2β1. The ligands used were the binding‐site‐bearing trimeric peptide CB3[IV] and its shorter tryptic fragments F1–F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for α1β1 and α2β1 were in different but adjacent areas of CB3[IV]. Triple‐helical conformation and distinct primary structures were required for the interaction. Dissociation constants (<jats:italic>K</jats:italic><jats:sub>a</jats:sub>), for the affinity of integrins for collagen IV, were determined in the 1‐nM range in the presence of Mn<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup>. In the absence of Mn<jats:sup>2+</jats:sup>, the <jats:italic>K</jats:italic><jats:sub>d</jats:sub> values indicated a 30–60‐fold decrease in the affinities, which for α2β1 was further reduced by adding Ca<jats:sup>2+</jats:sup>. In the presence of Ca<jats:sup>2+</jats:sup> and Mg<jats:sup>2+</jats:sup> the affinity of collagen IV for α1β1 was four‐times higher than for α2β1.</jats:p> Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 European Journal of Biochemistry |
| spellingShingle | KERN, Andreas, EBLE, Johannes, GOLBIK, Ralph, KÜHN, Klaus, European Journal of Biochemistry, Interaction of type IV collagen with the isolated integrins α1β1 and α2β1, Biochemistry |
| title | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_full | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_fullStr | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_full_unstemmed | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_short | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| title_sort | interaction of type iv collagen with the isolated integrins α1β1 and α2β1 |
| title_unstemmed | Interaction of type IV collagen with the isolated integrins α1β1 and α2β1 |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1993.tb18017.x |