Generation of collagenase-resistant collagen by site-directed mutagenesis of murine pro alpha 1(I) collagen gene.

Wu, Hong; Byrne, Michael H.; Stacey, Alex; Goldring, Mary B.; Birkhead, James R.; Jaenisch, Rudolf; Krane, Stephen M.

doi:10.1073/pnas.87.15.5888

Cited by 120 publications

(121 citation statements)

References 34 publications

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“…However, for specific cleavage at residue 775, the collagens must be present in a triple-helical structure (15). To ensure definite cleavage products, we did not digest the smaller collagen fragments with mammalian collage- Figure 3).…”

Section: Resultsmentioning

confidence: 99%

Characterization of the binding region for the yersinia enterocolitica adhesin yada on types i and ii collagen

Schulze‐Koops

Burkhardt

Heesemann

et al. 1995

Arthritis & Rheumatism

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Objective. The plasmid-encoded adhesin YadA confers pathogenic functions on Yersinia enterocolitica, a microorganism associated with reactive arthritis. While emerging evidence has indicated that the persistence of the bacteria in individuals with reactive arthritis is a prerequisite for the development of the disease, the tissue specificity of this immunologic disease sequela remains elusive. The present study was undertaken to investigate YadA-mediated binding of Y enterocolitica to the most abundant collagens in joints, types I and I1 collagen.Methods. Binding studies were performed with recombinant Y enterocoliticu strains and highly purified type I1 collagen and the d ( I ) chain of type I collagen, or fragments of these collagens generated by various enzymatic and nonenzymatic cleavage procedures. Interactions of bacteria with the proteins were determined in binding assays with radiolabeled proteins.Results. Binding regions for YadA were identified at the 181-amino acid fragment d(I)78CBN of type I collagen and the CBlO fragment of type I1 collagen. From binding and blocking experiments with al(1) fragments, cyanogen bromide-derived or mammalian collagenasderived type I1 collagen fragments, and synthetic peptides with collagen-like structures, it was ~~~

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Section: Resultsmentioning

confidence: 99%

Characterization of the binding region for the yersinia enterocolitica adhesin yada on types i and ii collagen

Schulze‐Koops

Burkhardt

Heesemann

et al. 1995

Arthritis & Rheumatism

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“…The investigation on the action of MMPs on collagen has been carried out for a long time, and preliminary measurements have been carried out on the activation energy of the catalysis employing porcine collagenases and gelatinases (16). In addition, previous experiments have been reported on the cleavage of native and site-directed mutants of murine collagen by MMP-1, outlining crucial aspects of the recognition mechanism (17). Very recently, proteolysis of single collagen I molecules has been followed by atomic force microscopy (18), confirming that the process follows a simple Michaelis-Menten mechanism and outlining that the results on bulk solution are compatible with those observed on single collagen molecules.…”

Section: Matrix Metalloproteinases (Mmp)mentioning

confidence: 99%

“…4), which is closely similar to the natural substrate of MMP-8. It envisages a very complex interplay among different portions of the enzyme molecule in the substrate recognition and/or processing, as also suggested by the processing of collagen by MMP-1 (17). Therefore, such a investigation indeed may represent a first basis for the comprehension of molecules, which efficiently interfere at different levels with the cleavage of physiological substrates by MMP-8 as well as by other collagenases.…”

mentioning

confidence: 99%

Cleavage of Bovine Collagen I by Neutrophil Collagenase MMP-8

Marini¹,

Fasciglione²,

Sanctis³

et al. 2000

Journal of Biological Chemistry

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The enzymatic processing of bovine collagen I by neutrophil collagenase (MMP-8) has been monitored at 37°C, envisaging the occurrence of multiple intermediate steps, following the initial cleavage, which leads to the formation of 1 ⁄4 and 3 ⁄4 fragments. Further, the first cleavage event has been investigated at 37°C as a function of pH, and catalytic parameters have been obtained through a global analysis of steady-state kinetic data, such as to get an overall consistent picture of k cat /K m , k cat , and K m . These data have been compared with those obtained from the catalysis by MMP-8 of two synthetic fluorogenic substrates under the same experimental conditions. The overall behavior can be accounted for by the existence of five protonating groups, which vary to a different extent their pK a values for the three substrates investigated. The main observation concerns the fact the two of these residues, which play a relevant role in the enzymatic activity of MMP-8, are relatively far from the primary recognition site, and they are coming into action only for large macromolecular substrates, such as bovine collagen I. This finding opens the question of appropriate testing for inhibitors of the enzymatic action of MMP-8, which must take into account, and also of these relevant interactions occurring only with natural substrates. Matrix metalloproteinases (MMP)1 are a class of proteolytic enzymes characterized by the presence of a Zn 2ϩ atom in the active site, which are able to process enzymatically several components of the extracellular matrix, such as interstitial and basement membranes, collagen, fibronectin, and laminin. Because of their crucial role in the extracellular matrix degradation, they are implicated in the tissue remodeling processes associated to the growth and development and in several pathological conditions, such as rheumatoid arthritis and tumor invasion (1-3). Collagenases, such as fibroblast collagenase (MMP-1), neutrophil collagenase (MMP-8), and collagenase-3 (MMP-13), are a class of MMPs that specifically cleave several types of native triple-helical collagen (4 -6), and in particular collagen I, at a specific peptide bond between Gly 775 and the residue in position 776 (which can be either Leu or Ile) (4, 7), leading to the formation of 1 ⁄4 and 3 ⁄4 fragments. This event is a crucial one because of the fairly slow rate of collagen turnover within the cartilage (8), and it is closely related to the occurrence of important physiological and pathological events (9 -11).Collagen I is one of the major constituents of the extracellular matrix for several tissues, such as skin, tendon, blood vessels, cartilage, bones, and basal laminas (12), and its triplehelical structural arrangement has been the object of several recent studies both on the native molecule (Ref. 13 and references quoted therein) and on model peptides (14, 15). The investigation on the action of MMPs on collagen has been carried out for a long time, and preliminary measurements have been carried out on the activation ener...

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“…This latter observation may indicate a possible relationship between KSPG occupancy on the fibril and collagen modification seen in diabetes and aging. The other main region of KSPG binding, to the "a bands" of the fibril, overlaps with the major N-terminal intermolecular cross-link site (48), the heparin/HSPG-binding site (38), a sequence mediating ␣ 2 ␤ 1 integrin binding to denatured collagen (27,28), the sites for vertebrate collagenase cleavage (49), and fibronectin binding (31)(32)(33). Of potential significance to fibril assembly is the fact that this KSPG-binding region (45) also overlaps with all of the domains shown to be important for collagen fibrillogenesis (Fig.…”

Section: Distribution Of Ligand-binding Sites and Functional Domains mentioning

confidence: 99%

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

Lullo¹,

Sweeney²,

Körkkö³

et al. 2002

Journal of Biological Chemistry

817

546

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Type I collagen is the most abundant protein in humans, and it helps to maintain the integrity of many tissues via its interactions with cell surfaces, other extracellular matrix molecules, and growth and differentiation factors. Nearly 50 molecules have been found to interact with type I collagen, and for about half of them, binding sites on this collagen have been elucidated. In addition, over 300 mutations in type I collagen associated with human connective tissue disorders have been described. However, the spatial relationships between the known ligand-binding sites and mutation positions have not been examined. To this end, here we have created a map of type I collagen that includes all of its ligand-binding sites and mutations. The map reveals the existence of several hot spots for ligand interactions on type I collagen and that most of the binding sites locate to its C-terminal half. Moreover, on the collagen fibril some potentially relevant relationships between binding sites were observed including the following: fibronectin-and certain integrin-binding regions are near neighbors, which may mechanistically relate to fibronectin-dependent cell-collagen attachment; proteoglycan binding may potentially impact upon collagen fibrillogenesis, cell-collagen attachment, and collagen glycation seen in diabetes and aging; and mutations associated with osteogenesis imperfecta and other disorders show apparently nonrandom distribution patterns within both the monomer and fibril, implying that mutation positions correlate with disease phenotype. These and other observations presented here may provide novel insights into evaluating type I collagen functions and the relationships between its binding partners and mutations.

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Generation of collagenase-resistant collagen by site-directed mutagenesis of murine pro alpha 1(I) collagen gene.

Cited by 120 publications

References 34 publications

Characterization of the binding region for the yersinia enterocolitica adhesin yada on types i and ii collagen

Characterization of the binding region for the yersinia enterocolitica adhesin yada on types i and ii collagen

Cleavage of Bovine Collagen I by Neutrophil Collagenase MMP-8

Mapping the Ligand-binding Sites and Disease-associated Mutations on the Most Abundant Protein in the Human, Type I Collagen

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