Type I collagen shows a specific binding affinity for bovine dentin phosphophoryn

1986 ◽  
Vol 38 (3) ◽  
pp. 135-141 ◽  
Author(s):  
W. G. Stetler-Stevenson ◽  
Arthur Veis
Keyword(s):  
Binding Affinity ◽  
Type I Collagen ◽  
Specific Binding ◽  
Type I

‘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.

scholarly journals Characterization of sequence specific binding of LARP6 to the 5’ stem-loop of type I collagen mRNAs and implications for rational design of antifibrotic drugs

2020 ◽  
Author(s):  
Lela Stefanovic ◽  
Blaine H. Gordon ◽  
Robert Silvers ◽  
Branko Stefanovic
Keyword(s):  
Rational Design ◽  
Type I Collagen ◽  
Specific Binding ◽  
High Rate ◽  
Stable Complex ◽  
Type I ◽  
Stem Loop ◽  
Rrm Domain ◽  
Α Helix ◽  
Antifibrotic Drugs

AbstractExcessive synthesis of type I collagen characterizes fibrotic diseases. Binding of LARP6 to the 5’ stem-loop (5’SL) of collagen mRNAs regulates their translation and the high rate of biosynthesis in fibrosis. LARP6 needs two domains to form stable complex with 5’SL RNA, the La-domain and the juxtaposed RRM domain (jointly called the La-module). We describe that the La-domain of LARP6 is necessary and sufficient for recognition of 5’SL in sequence specific manner. The three amino acid motif, RNK, located in the flexible loop which connects the second α-helix to the β-sheet of the La domain is critical for binding. Mutation of any of these three amino acids abolishes the binding of La-domain to 5’SL. The major site of crosslinking of LARP6 to 5’SL RNA was mapped to this motif. The RNK motif is not found in other LARPs, which can not bind 5’SL. Presence of RRM increases the stability of complex between La-domain and 5’SL RNA and RRM domain does not make extensive contacts with 5’SL RNA. We propose a model in which the initial recognition of 5’SL by LARP6 is mediated by the RNK epitope and further stabilized by the RRM domain. This discovery suggests that the interaction between LARP6 and collagen mRNAs can be blocked by small molecules that target the RNK epitope and will help rational design of the LARP6 binding inhibitors as specific antifibrotic drugs.

Isolation And Purification Of Collagen And α1 Receptor From Platelet Membrane

1981 ◽  
Author(s):  
T M Chiang ◽  
A H Kang
Keyword(s):  
Affinity Chromatography ◽  
Binding Site ◽  
Gel Electrophoresis ◽  
Type I Collagen ◽  
Specific Binding ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Type I ◽  
Isolation And Purification ◽  
Platelet Membranes

We have previously demonstrated that chick skin type I collagen and the α1(I) chain mediate platelet aggregation. Aggregation is associated with specific binding of these substances by platelet membranes. We now describe the isolation and purification of the receptor. Platelet membranes were prepared as described previously and isolated membranes were solubilized in 0.5% Triton. The receptor was then purified by a combination of gel filtration, affinity chromatography on α1(I)-sepharose or type I collagen-sepharose and preparative polyacrylamide gel electrophoresis. The receptor activity was assayed either directly by a binding assay using (14C)-glycine-labeled α1(I) or indirectly by an adhesion inhibition assay on Sepharose 2B with (14C)-sero- tinin-labeled platelets.The results show that the α1(I) receptor can be purified to a single band on SDS-gel electrophoresis with a recovery of 2.5%. Its activity is destroyed by preincubation with trypsin or pronase indicating it is a protein. The apparent molecular weight as estimated by gel filtration and SDS-gel electrophoresis is 95,000 daltons. The binding of (14C)- labeled α1(I) is specifically displaced by unlabeled α1(I), and the bound radioactivity can be removed by treatment with purified bacterial collagenase. The binding of (14C)- labeled α1(I) by the purified α1(I) receptor can also be inhibited by the receptor isolated from collagen-sepharose affinity chromatography. These data suggest that the α1(I) binding site is identical to the collagen binding site.

scholarly journals Three-dimensional printed hydroxyapatite bone tissue engineering scaffold with antibacterial and osteogenic ability

2021 ◽  
Vol 15 (1) ◽  
Author(s):  
Liu Zhongxing ◽  
Wu Shaohong ◽  
Li Jinlong ◽  
Zhang Limin ◽  
Wang Yuanzheng ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Bone Defect ◽  
Type I Collagen ◽  
Porous Scaffold ◽  
Specific Binding ◽  
Three Dimensional ◽  
Protein Translation ◽  
Inhibition Zone ◽  
Bone Morphogenetic Protein 2 ◽  
Type I

AbstractThe development of an effective scaffold for bone defect repair is an urgent clinical need. However, it is challenging to design a scaffold with efficient osteoinduction and antimicrobial activity for regeneration of bone defect. In this study, we successfully prepared a hydroxyapatite (HA) porous scaffold with a surface-specific binding of peptides during osteoinduction and antimicrobial activity using a three-dimensional (3D) printing technology. The HA binding domain (HABD) was introduced to the C-terminal of bone morphogenetic protein 2 mimetic peptide (BMP2-MP) and antimicrobial peptide of PSI10. The binding capability results showed that BMP2-MP and PSI10-containing HABD were firmly bound to the surface of HA scaffolds. After BMP2-MP and PSI10 were bound to the scaffold surface, no negative effect was observed on cell proliferation and adhesion. The gene expression and protein translation levels of type I collagen (COL-I), osteocalcin (OCN) and Runx2 have been significantly improved in the BMP2-MP/HABP group. The level of alkaline phosphatase significantly increased in the BMP2-MP/HABP group. The inhibition zone test against Staphylococcus aureus and Escherichia coli BL21 prove that the PSI10/HABP@HA scaffold has strong antibacterial ability than another group. These findings suggest that 3D-printed HA scaffolds with efficient osteoinduction and antimicrobial activity represent a promising biomaterial for bone defect reconstruction.

scholarly journals α2β1Integrin Is Not Recognized by Rhodocytin but Is the Specific, High Affinity Target of Rhodocetin, an RGD-independent Disintegrin and Potent Inhibitor of Cell Adhesion to Collagen

2000 ◽  
Vol 276 (15) ◽  
pp. 12274-12284 ◽  
Author(s):  
Johannes A. Eble ◽  
Bernd Beermann ◽  
Hans-Jürgen Hinz ◽  
Alletta Schmidt-Hederich
Keyword(s):  
Cell Adhesion ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Type I Collagen ◽  
Specific Binding ◽  
Soluble Form ◽  
Type I ◽  
Wild Type ◽  
Independent Manner ◽  
High Affinity

We have recombinantly expressed a soluble form of human α2β1integrin that lacks the membrane-anchoring transmembrane domains as well as the cytoplasmic tails of both integrin subunits. This soluble α2β1integrin binds to its collagen ligands the same way as the wild-type α2β1integrin. Furthermore, like the wild-type form, it can be activated by manganese ions and an integrin-activating antibody. However, it does not bind to rhodocytin, a postulated agonist of α2β1integrin from the snake venom ofCalloselasma rhodostoma, which elicits platelet aggregation. Taking advantage of the recombinantly expressed, soluble α2β1integrin, an inhibition assay was established in which samples can be tested for their capability to inhibit binding of soluble α2β1integrin to immobilized collagen. Thus, by scrutinizing theC. rhodostomasnake venom in this protein-protein interaction assay, we found a component of the snake venom that inhibits the interaction of soluble α2β1integrin to type I collagen efficiently. N-terminal sequences identified this inhibitor as rhodocetin, a recently published antagonist of collagen-induced platelet aggregation. We could demonstrate that its inhibitory effect bases on its strong and specific binding to α2β1integrin, proving that rhodocetin is a disintegrin. Standing apart from the growing group of RGD-dependent snake venom disintegrins, rhodocetin interacts with α2β1integrin in an RGD-independent manner. Furthermore, its native conformation, which is stabilized by disulfide bridges, is indispensibly required for its inhibitory activity. Rhodocetin does not contain any major collagenous structure despite its high affinity to α2β1integrin, which binds to collagenous molecules much more avidly than to noncollagenous ligands, such as laminin. Blocking α2β1integrin as the major collagen receptor on platelets, rhodocetin is responsible for hampering collagen-induced, α2β1integrin-mediated platelet activation, leading to hemorrhages and bleeding disorders of the snakebite victim. Moreover, having a widespread tissue distribution, α2β1integrin also mediates cell adhesion, spreading, and migration. We showed that rhodocetin is able to inhibit α2β1integrin-mediated adhesion of fibrosarcoma cells to type I collagen completely.

Proteoglycan-type I collagen fibril interactions in bone and non-calcifying connective tissues

1985 ◽  
Vol 5 (1) ◽  
pp. 71-81 ◽  
Author(s):  
J. E. Scott ◽  
M. Haigh
Keyword(s):  
Biochemical Analysis ◽  
Type I Collagen ◽  
Soft Tissues ◽  
Chondroitin Sulphate ◽  
Specific Binding ◽  
Uranyl Acetate ◽  
Collagen Fibrils ◽  
Type I ◽  
Connective Tissues ◽  
Oriented Parallel

The association of proteogtycans with type I collagen fibrils in skin, tendon, cornea and bone has been determined by electron microscopy using an electrondense dye, Cupromeronic blue, in the critical electrolyte concentration mode, backed up by biochemical analysis and digestion by hyaluronidase or keratanase. A major proteoglycan of the soft tissues, containing dermatan sulphat, is shown to be regularly and orthogonally arranged at the surface of the fibrils. Uranyl acetate counterstaining revealed that the main specific binding site is the ‘d’ band, which previous work indicated is very close to the initial site of calcification of type I collagen fibrils. Bone, deminer-alized by a ‘non-aqueous’ technique which preserves the proteoglycan in the tissue does not contain orthogonal arrays; the interfibrillar proteoglycan filaments are oriented parallel to the fibril axis. The main proteoglycan in bone is chondroitin sulphate-rich. It is suggested that dermatan sulphate proteoglycan plays a role in preventing soft connective tissues from calcifying.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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