scholarly journals Binding of soluble type I collagen to fibroblasts: effects of thermal activation of ligand, ligand concentration, pinocytosis, and cytoskeletal modifiers.

1982 ◽  
Vol 95 (3) ◽  
pp. 747-751 ◽  
Author(s):  
B D Goldberg
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Thermal Activation ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Binding ◽  
Bacterial Collagenase ◽  
Ligand Interactions ◽  
Organizing Center ◽  
High Ligand

Efficient binding of native, soluble 125I-labeled type I rat collagen to mouse 3T3 fibroblast monolayers requires prior warming of the ligand to 35-37 degrees C for 10-30 min. Decreased binding at high ligand concentrations is ascribed to ligand-ligand interactions rather than to negative cooperativity. Addition of bacterial collagenase to monolayers labeled with the 125I-ligand releases a constant fraction (80%) of the bound ligand over a 2-h interval at 37 degrees C, indicating that little of the ligand becomes inaccessible by pinocytosis. Colchicine (10(-7) M) and vinblastine (5 X 10(-8) M) do not inhibit binding by morphologically intact monolayers. Cytochalasins and concanavalin A show dose-related inhibition of binding by intact monolayers that is due to a reduction in the number of available binding sites rather than to a change in binding site affinity. The collagen binding site on the fibroblast surface is proposed as an organizing center for the assembly of periodic type I collagen fibrils.

scholarly journals Inhibition of MMP-2 gelatinolysis by targeting exodomain–substrate interactions

2007 ◽  
Vol 406 (1) ◽  
pp. 147-155 ◽  
Author(s):  
Xiaoping Xu ◽  
Zhihua Chen ◽  
Yao Wang ◽  
Lynda Bonewald ◽  
Bjorn Steffensen
Keyword(s):  
Binding Site ◽  
Type I Collagen ◽  
Matrix Metalloproteinase 2 ◽  
Type I ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Collagen Binding ◽  
Collagen Peptides ◽  
Collagen Chain ◽  
Hydrolysis Of

MMP-2 (matrix metalloproteinase 2) contains a CBD (collagen-binding domain), which is essential for positioning gelatin substrate molecules relative to the catalytic site for cleavage. Deletion of the CBD or disruption of CBD-mediated gelatin binding inhibits gelatinolysis by MMP-2. To identify CBD-binding sites on type I collagen and collagen peptides with the capacity to compete CBD binding of gelatin and thereby inhibit gelatinolysis by MMP-2, we screened a one-bead one-peptide combinatorial peptide library with recombinant CBD as bait. Analyses of sequences from the CBD-binding peptides pointed to residues 715–721 in human α1(I) collagen chain as a binding site for CBD. A peptide (P713) including this collagen segment was synthesized for analyses. In SPR (surface plasmon resonance) assays, the CBD and MMP-2E404A, a catalytically inactive MMP-2 mutant, both bound immobilized P713 in a concentration-dependent manner, but not a scrambled control peptide. Furthermore, P713 competed gelatin binding by the CBD and MMP-2E404A. In control assays, neither of the non-collagen binding alkylated CBD or MMP-2 with deletion of CBD (MMP-2ΔCBD) bound P713. Consistent with the exodomain functions of the CBD, P713 inhibited ∼90% of the MMP-2 gelatin cleavage, but less than 20% of the MMP-2 activity on a peptide substrate (NFF-1) which does not require the CBD for cleavage. Confirming the specificity of the inhibition, P713 did not alter MMP-2ΔCBD or MMP-8 activities. These experiments identified a CBD-binding site on type I collagen and demonstrated that a corresponding synthetic peptide can inhibit hydrolysis of type I and IV collagens by competing CBD-mediated gelatin binding to MMP-2.

scholarly journals Mapping the Type I Collagen-binding Site on Pigment Epithelium-derived Factor

2002 ◽  
Vol 277 (47) ◽  
pp. 45400-45407 ◽  
Author(s):  
Christina Meyer ◽  
Luigi Notari ◽  
S. Patricia Becerra
Keyword(s):  
Binding Site ◽  
Type I Collagen ◽  
Pigment Epithelium ◽  
Type I ◽  
Collagen Binding ◽  
Pigment Epithelium Derived Factor

scholarly journals Mapping the heparin-binding sites on type I collagen monomers and fibrils.

1994 ◽  
Vol 125 (5) ◽  
pp. 1179-1188 ◽  
Author(s):  
J D San Antonio ◽  
A D Lander ◽  
M J Karnovsky ◽  
H S Slayter
Keyword(s):  
Electron Microscopy ◽  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Heparan Sulfate ◽  
Binding Site ◽  
Binding Sites ◽  
Type I Collagen ◽  
Type I ◽  
Heparin Binding ◽  
Heparin Binding Site

The glycosaminoglycan chains of cell surface heparan sulfate proteoglycans are believed to regulate cell adhesion, proliferation, and extracellular matrix assembly, through their interactions with heparin-binding proteins (for review see Ruoslahti, E. 1988. Annu. Rev. Cell Biol. 4:229-255; and Bernfield, M., R. Kokenyesi, M. Kato, M. T. Hinkes, J. Spring, R. L. Gallo, and E. J. Lose. 1992. Annu. Rev. Cell Biol. 8:365-393). Heparin-binding sites on many extracellular matrix proteins have been described; however, the heparin-binding site on type I collagen, a ubiquitous heparin-binding protein of the extracellular matrix, remains undescribed. Here we used heparin, a structural and functional analogue of heparan sulfate, as a probe to study the nature of the heparan sulfate proteoglycan-binding site on type I collagen. We used affinity coelectrophoresis to study the binding of heparin to various forms of type I collagen, and electron microscopy to visualize the site(s) of interaction of heparin with type I collagen monomers and fibrils. Using affinity coelectrophoresis it was found that heparin has similar affinities for both procollagen and collagen fibrils (Kd's approximately 60-80 nM), suggesting that functionally similar heparin-binding sites exist in type I collagen independent of its aggregation state. Complexes of heparin-albumin-gold particles and procollagen were visualized by rotary shadowing and electron microscopy, and a preferred site of heparin binding was observed near the NH2 terminus of procollagen. Native or reconstituted type I collagen fibrils showed one region of significant heparin-gold binding within each 67-nm period, present near the division between the overlap and gap zones, within the "a" bands region. According to an accepted model of collagen fibril structure, our data are consistent with the presence of a single preferred heparin-binding site near the NH2 terminus of the collagen monomer. Correlating these data with known type I collagen sequences, we suggest that the heparin-binding site in type I collagen may consist of a highly basic triple helical domain, including several amino acids known sometimes to function as disaccharide acceptor sites. We propose that the heparin-binding site of type I collagen may play a key role in cell adhesion and migration within connective tissues, or in the cell-directed assembly or restructuring of the collagenous extracellular matrix.

scholarly journals Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans

2007 ◽  
Vol 28 (3) ◽  
pp. 209-221 ◽  
Author(s):  
Joan C. Marini ◽  
Antonella Forlino ◽  
Wayne A. Cabral ◽  
Aileen M. Barnes ◽  
James D. San Antonio ◽  
...  
Keyword(s):  
Osteogenesis Imperfecta ◽  
Binding Sites ◽  
Type I Collagen ◽  
Type I ◽  
Collagen Binding ◽  
Lethal Mutations ◽  
Helical Domain

Identification of Bilirubin Binding Site in Type I Collagen

2013 ◽  
Vol 19 (4) ◽  
pp. 357-364 ◽  
Author(s):  
Nagarajan Usharani ◽  
Gladstone Christopher Jayakumar ◽  
Swarna V. Kanth ◽  
Jonnalagadda Raghava Rao ◽  
Bangaru Chandrasekaran ◽  
...  
Keyword(s):  
Binding Site ◽  
Type I Collagen ◽  
Type I ◽  
Bilirubin Binding

The C-terminus type I collagen is a major binding site for heparin

1986 ◽  
Vol 882 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Katharyn M. Keller ◽  
John M. Keller ◽  
Klaus Kühn
Keyword(s):  
Binding Site ◽  
Type I Collagen ◽  
Type I ◽  
C Terminus

scholarly journals A study of the interaction in vitro between type I collagen and a small dermatan sulphate proteoglycan

1988 ◽  
Vol 251 (3) ◽  
pp. 643-648 ◽  
Author(s):  
N Uldbjerg ◽  
C C Danielsen
Keyword(s):  
Steady State ◽  
Binding Sites ◽  
Type I Collagen ◽  
Enzyme Linked Immunosorbent Assay ◽  
Side Chains ◽  
Type I ◽  
Dermatan Sulphate ◽  
Collagen Fibrillogenesis ◽  
High Affinity ◽  
Sulphate Proteoglycan

The interaction between a small dermatan sulphate proteoglycan isolated from human uterine cervix and collagen type I from human and rat skin was investigated by collagen-fibrillogenesis experiments. Collagen fibrillogenesis was initiated by elevation of temperature and pH after addition of proteoglycan, chondroitinase-digested proteoglycan or isolated side chains, and monitored by turbidimetry. Collagen-associated and unbound proteoglycan was determined by enzyme-linked immunosorbent assay after aggregation was complete. (1) The binding of proteoglycan to collagen could be explained by the presence of two mutually non-interacting binding sites, with Ka1 = 1.3 x 10(8) M-1 and Ka2 = 1.3 x 10(6) M-1. The number of binding sites per tropocollagen molecule was n1 = 0.11 and n2 = 1.1. The 0.1 high-affinity binding site per tropocollagen molecule indicates that the strong interaction between proteoglycan and collagen results from a concerted action of tropocollagen molecules in fibrils. Digestion of the proteoglycan with chondroitinase ABC did not affect these binding characteristics. (2) Proteoglycan did not affect the rate of fibrillogenesis, but increased the steady-state A400 by up to 90%. This increase was directly proportional to the saturation of the high-affinity type of binding sites. Neither isolated core protein nor isolated side chains induced a similar high increase in steady-state A400. (3) Electron micrographs showed that the fibril diameter was affected only to a minor extent, if at all, by the proteoglycan, whereas bundles of laterally aligned fibrils were common in the presence of proteoglycan. (4) Results obtained with human and rat collagen were similar.

Structural basis of carbohydrate binding in domain C of a type I pullulanase from Paenibacillus barengoltzii

2020 ◽  
Vol 76 (5) ◽  
pp. 447-457
Author(s):  
Ping Huang ◽  
Shiwang Wu ◽  
Shaoqing Yang ◽  
Qiaojuan Yan ◽  
Zhengqiang Jiang
Keyword(s):  
Binding Site ◽  
Binding Sites ◽  
Structural Basis ◽  
Carbohydrate Binding ◽  
Type I ◽  
Debranching Enzyme ◽  
Crystal Forms ◽  
Aromatic Residues ◽  
Starch Debranching Enzyme ◽  
Paenibacillus Barengoltzii

Pullulanase (EC 3.2.1.41) is a well known starch-debranching enzyme that catalyzes the cleavage of α-1,6-glycosidic linkages in α-glucans such as starch and pullulan. Crystal structures of a type I pullulanase from Paenibacillus barengoltzii (PbPulA) and of PbPulA in complex with maltopentaose (G5), maltohexaose (G6)/α-cyclodextrin (α-CD) and β-cyclodextrin (β-CD) were determined in order to better understand substrate binding to this enzyme. PbPulA belongs to glycoside hydrolase (GH) family 13 subfamily 14 and is composed of three domains (CBM48, A and C). Three carbohydrate-binding sites identified in PbPulA were located in CBM48, near the active site and in domain C, respectively. The binding site in CBM48 was specific for β-CD, while that in domain C has not been reported for other pullulanases. The domain C binding site had higher affinity for α-CD than for G6; a small motif (FGGEH) seemed to be one of the major determinants for carbohydrate binding in this domain. Structure-based mutations of several surface-exposed aromatic residues in CBM48 and domain C had a debilitating effect on the activity of the enzyme. These results suggest that both CBM48 and domain C play a role in binding substrates. The crystal forms described contribute to the understanding of pullulanase domain–carbohydrate interactions.

‘Small’-proteoglycan: collagen interactions: Keratan sulphate proteoglycan associates with rabbit corneal collagen fibrils at the ‘a’ and ‘c’ bands

1985 ◽  
Vol 5 (9) ◽  
pp. 765-774 ◽  
Author(s):  
J. E. Scott ◽  
M. Haigh
Keyword(s):  
Binding Sites ◽  
Type I Collagen ◽  
Specific Binding ◽  
Corneal Stroma ◽  
Collagen Fibrils ◽  
Type I ◽  
Keratan Sulphate ◽  
Protein Rich ◽  
Small Proteoglycan ◽  
Corneal Collagen

l. Proteoglycans (PGs) in rabbit corneal stroma and mouse sclera have been stained for electron microscopy with Cupromeronic blue in a critical electrolyte concentration (CEC) mode, with and without prior digestion of the tissue by keratanase or chondroitinase ABC to remove the keratan sulphate (KS) or chondroitin-dermatan sulphates (CS or DS) respectively.2. Two classes of PGs, located orthogonally to the corneal collagen fibrils at either the ‘step’ (band ‘a’ or ‘c’) or gap zone (band ‘d’ or ‘e’) are shown to be KS-PGs or DS-PGs respectively. Four separate and specific PG binding sites on Type I collagen fibrils have thus been identified.3. Rabbit corneal KS and DS PGs each contain two kinds of PG (Gregory JD, Coster L & Damle SP (1982) J. Biol. Chem.257, 6965–6970). We propose that each ‘small’ protein-rich PG is associated with a specific binding site on the collagen fibril.

A nuclear factor 1 binding site mediates the transcriptional activation of a type I collagen promoter by transforming growth factor-β

Cell ◽  
1988 ◽  
Vol 52 (3) ◽  
pp. 405-414 ◽  
Author(s):  
Pellegrino Rossi ◽  
Gerard Karsenty ◽  
Anita B. Roberts ◽  
Nanette S. Roche ◽  
Michael B. Sporn ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Type I Collagen ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Type I ◽  
Nuclear Factor ◽  
Nuclear Factor 1 ◽  
Collagen Promoter
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