|
|
char = T;code = 84
char = r;code = 114
char = o;code = 111
char = p;code = 112
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char = O;code = 79
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result sql = Tropoelastin interacts with cell-surface glycosaminoglycans via its COOH-terminal domain.
Tropoelastin interacts with cell-surface glycosaminoglycans via its COOH-terminal domain.char = U;code = 85
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char = O;code = 79
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char = ;code = 32
char = T;code = 84
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char = r;code = 114
char = o;code = 111
char = u;code = 117
char = g;code = 103
char = h;code = 104
char = ;code = 32
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char = h;code = 104
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char = s;code = 115
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char = s;code = 115
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char = e;code = 101
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char = t;code = 116
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char = 1;code = 49
char = 7;code = 55
char = ;code = 32
char = a;code = 97
char = m;code = 109
char = i;code = 105
char = n;code = 110
char = o;code = 111
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char = c;code = 99
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char = d;code = 100
char = s;code = 115
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char = a;code = 97
char = s;code = 115
char = ;code = 32
char = t;code = 116
char = h;code = 104
char = e;code = 101
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char = s;code = 115
char = e;code = 101
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char = e;code = 101
char = l;code = 108
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char = ;code = 32
char = t;code = 116
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char = e;code = 101
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char = a;code = 97
char = r;code = 114
char = b;code = 98
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char = n;code = 110
char = u;code = 117
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char = t;code = 116
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char = p;code = 112
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char = t;code = 116
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char = r;code = 114
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char = s;code = 115
char = p;code = 112
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char = s;code = 115
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char = l;code = 108
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char = f;code = 102
char = o;code = 111
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char = e;code = 101
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char = d;code = 100
char = h;code = 104
char = e;code = 101
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char = <;code = 60
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char = r;code = 114
char = /;code = 47
char = >;code = 62
result sql = Using a biochemical and cell biological approach, we have identified a cell interaction site at the carboxyl terminus of tropoelastin. Cell interactions with the COOH-terminal sequence are not through the elastin-binding protein (EBP67) because neither VGVAPG-like peptides nor galactoside sugars altered adhesion. Our results also show that cell adhesion to tropoelastin is not promoted by integrins. Through the use of mutant Chinese hamster ovary cell lines defective in glycosaminoglycan biosynthesis, as well as competition studies and enzymatic removal of specific cell-surface glycosaminoglycans, the tropoelastin-binding moieties on the cell surface were identified as heparan and chondroitin sulfate-containing glycosaminoglycans, with heparan sulfate being greatly preferred. Heparin affinity chromatography combined with cell adhesion assays identified the last 17 amino acids as the sequence element at the carboxyl terminus of tropoelastin responsible for the adhesive activity.
char = r;code = 114
char = o;code = 111
char = p;code = 112
char = o;code = 111
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char = t;code = 116
char = i;code = 105
char = n;code = 110
char = ;code = 32
char = i;code = 105
char = n;code = 110
char = t;code = 116
char = e;code = 101
char = r;code = 114
char = a;code = 97
char = c;code = 99
char = t;code = 116
char = s;code = 115
char = ;code = 32
char = w;code = 119
char = i;code = 105
char = t;code = 116
char = h;code = 104
char = ;code = 32
char = c;code = 99
char = e;code = 101
char = l;code = 108
char = l;code = 108
char = -;code = 45
char = s;code = 115
char = u;code = 117
char = r;code = 114
char = f;code = 102
char = a;code = 97
char = c;code = 99
char = e;code = 101
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char = g;code = 103
char = l;code = 108
char = y;code = 121
char = c;code = 99
char = o;code = 111
char = s;code = 115
char = a;code = 97
char = m;code = 109
char = i;code = 105
char = n;code = 110
char = o;code = 111
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char = l;code = 108
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char = c;code = 99
char = a;code = 97
char = n;code = 110
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char = i;code = 105
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char = C;code = 67
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char = O;code = 79
char = H;code = 72
char = -;code = 45
char = t;code = 116
char = e;code = 101
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char = d;code = 100
char = o;code = 111
char = m;code = 109
char = a;code = 97
char = i;code = 105
char = n;code = 110
char = .;code = 46
result sql = Tropoelastin interacts with cell-surface glycosaminoglycans via its COOH-terminal domain.
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char = l;code = 108
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char = t;code = 116
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char = h;code = 104
char = ;code = 32
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char = e;code = 101
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char = O;code = 79
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result sql = Using a biochemical and cell biological approach, we have identified a cell interaction site at the carboxyl terminus of tropoelastin. Cell interactions with the COOH-terminal sequence are not through the elastin-binding protein (EBP67) because neither VGVAPG-like peptides nor galactoside sugars altered adhesion. Our results also show that cell adhesion to tropoelastin is not promoted by integrins. Through the use of mutant Chinese hamster ovary cell lines defective in glycosaminoglycan biosynthesis, as well as competition studies and enzymatic removal of specific cell-surface glycosaminoglycans, the tropoelastin-binding moieties on the cell surface were identified as heparan and chondroitin sulfate-containing glycosaminoglycans, with heparan sulfate being greatly preferred. Heparin affinity chromatography combined with cell adhesion assays identified the last 17 amino acids as the sequence element at the carboxyl terminus of tropoelastin responsible for the adhesive activity.
Publication: J. Biol. Chem. 2005 Dec 9 ;280(49)::40939-47.
Publication Date: 2005 Dec 9
Study Author(s): Broekelmann, Thomas J;Kozel, Beth A;Ishibashi, Hideaki;Werneck, Claudio C;Keeley, Fred W;Zhang, Lijuan;Mecham, Robert P;
Institution: Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Shortcut link to this study:
Publication Date: 2005 Dec 9
Study Author(s): Broekelmann, Thomas J;Kozel, Beth A;Ishibashi, Hideaki;Werneck, Claudio C;Keeley, Fred W;Zhang, Lijuan;Mecham, Robert P;
Institution: Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Shortcut link to this study:
Using a biochemical and cell biological approach, we have identified a cell interaction site at the carboxyl terminus of tropoelastin. Cell interactions with the COOH-terminal sequence are not through the elastin-binding protein (EBP67) because neither VGVAPG-like peptides nor galactoside sugars altered adhesion. Our results also show that cell adhesion to tropoelastin is not promoted by integrins. Through the use of mutant Chinese hamster ovary cell lines defective in glycosaminoglycan biosynthesis, as well as competition studies and enzymatic removal of specific cell-surface glycosaminoglycans, the tropoelastin-binding moieties on the cell surface were identified as heparan and chondroitin sulfate-containing glycosaminoglycans, with heparan sulfate being greatly preferred. Heparin affinity chromatography combined with cell adhesion assays identified the last 17 amino acids as the sequence element at the carboxyl terminus of tropoelastin responsible for the adhesive activity.
PMID: 16192266
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