Guilty by Association: Some Collagen II Mutants Alter the Formation of ECM as a Result of Atypical Interaction with Fibronectin

Ito, Hidetoshi; Rucker, Eileen; Steplewski, Andrzej; McAdams, Erin; Brittingham, Raymond; Alabyeva, Tatiana; Fertala, Andrzej

doi:10.1016/j.jmb.2005.07.019

Cited by 34 publications

(67 citation statements)

References 47 publications

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“…Mutations in type II collagen result in abnormal deposition of both type II collagen and fibronectin. In this study, impaired fibronectin assembly was attributed to alterations in fibronectin interactions caused by its binding to thermally labile collagen II mutant (38). It is not known why cells lacking type I collagen are defective in fibronectin matrix deposition (23), whereas disruption of fibronectin-collagen binding due to a mutation in fibronectin or the presence of blocking peptides does not disrupt fibronectin matrix deposition or stability (Figs.…”

Section: Discussionmentioning

confidence: 74%

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

158

178

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munication between cells and the extracellular matrix (ECM) is critical for regulation of cell growth, survival, migration, and differentiation. Remodeling of the ECM can occur under normal physiological conditions, as a result of tissue injury, and in certain pathological conditions. ECM remodeling leads to alterations in ECM composition and organization that can alter many aspects of cell behavior, including cell migration. The cell migratory response varies depending on the type, amount, and organization of ECM molecules present, as well as the integrin and proteoglycan repertoire of the cells. We and others have shown that the deposition of several ECM molecules, including collagen types I and III, depends on the presence and stability of ECM fibronectin. Hence, the effect of fibronectin and fibronectin matrix on cell function may partially depend on its ability to direct the deposition of collagen in the ECM. In this study, we used collagen-binding fibronectin mutants and recombinant peptides that interfere with fibronectin-collagen binding to show that fibronectindependent collagen I deposition regulates the cell migratory response to fibronectin. These data show that the ability of fibronectin to organize other proteins in the ECM is an important aspect of fibronectin function and highlight the importance of understanding how interactions between ECM proteins influence cell behavior. extracellular matrix; contractility CELL FATE DECISIONS involving cell growth, differentiation, and survival rely on the ability of cells to coordinate diverse input from cytokines, growth factors, and extracellular matrix (ECM) molecules (3,89,94). The effects of ECM molecules on cell behavior are particularly complicated, since they depend on the mixture of ECM molecules that are present, the way the ECM proteins are organized and presented to cells, and the presence of proteases, protease inhibitors, and endocytic mechanisms that can alter the levels of ECM proteins and ECM degradation products. Understanding how ECM proteins act in concert to elicit biological effects is key to understanding how cell-ECM interactions maintain normal tissue function and influence the cell response to tissue injury.There is much data showing that mixtures of different ECM molecules can have effects distinct from that of a single ECM molecule. For example, coating dishes with a combination of tenascin C and fibronectin results in altered expression of matrix metalloproteinases (MMPs) (86), whereas addition of tenascin C to dishes coated with fibrin and fibronectin results in altered cytoskeletal organization (90) compared with cells seeded in the absence of tenascin C. The ability of fibronectin null cells to produce a fibronectin matrix is also dependent on the combination of matrix proteins present on the substrate (4). Furthermore, mixed collagen and fibronectin substrates have been shown to alter the response of endothelial cells to shear stress compared with their response to fibronectin alone (59). Similarly, addition of soluble matric...

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Section: Discussionmentioning

confidence: 74%

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Sottile

Shi²,

Rublyevska³

et al. 2007

American Journal of Physiology-Cell Physiology

158

178

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“…In brief, procollagen I at a concentration 230 g/ml was digested with Lys-C (1 g/ml) for 0.5 h at 25°C, experimental conditions in which formation of collagen fibrils does not occur (21). After initial incubation, a possible enzymatic digestion of Lys-C-sensitive antibodies was inhibited by N␣-p-tosyl-L-lysine chloromethyl ketone (TPCK, Sigma-Aldrich) added to a final concentration of 1 mM (19,22). Subsequently, the anti-␣2Ct antibody was added to the Lys-C-processed collagen samples at concentrations of 180 or 10 g/ml to achieve collagen/antibody molar ratios of about 1:2 or 10:1, respectively.…”

Section: Methodsmentioning

confidence: 99%

Collagen Fibril Formation

Chung

Steplewski

Chung

et al. 2008

Journal of Biological Chemistry

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We present a concept for reducing formation of fibrotic deposits by inhibiting self-assembly of collagen molecules into fibrils, a main component of fibrotic lesions. Employing monoclonal antibodies that bind to the telopeptide region of a collagen molecule, we found that blocking telopeptide-mediated collagen/collagen interactions reduces the amount of collagen fibrils accumulated in vitro and in keloid-like organotypic constructs. We conclude that inhibiting extracellular steps of the fibrotic process provides a novel approach to limit fibrosis in a number of tissues and organs.Collagen I is the most abundant structural protein of connective tissues such as skin, bone, and tendon. This protein is first synthesized as a precursor molecule, procollagen, that is characterized by the presence of a rod-like central triple-helical domain flanked by short linear telopeptides and globular N-terminal and C-terminal propeptides (1). Single procollagen molecules are the building blocks for the biologically and mechanically relevant collagen fibrils. Formation of collagen fibrils is initiated by enzymatic cleavage of the N-terminal and the C-terminal propeptides. The N-terminal propeptides are cleaved by a group of enzymes that includes a disintegrin and metalloprotease with thrombospondin motifs (ADAMTS)-2, -3, and -14, whereas the C-terminal propeptides are cleaved by the metalloprotease bone morphogenetic protein 1 (BMP-1) 2 and by the other members of a closely related family of mammalian tolloid-like metalloproteases (2-4). Such a removal of procollagen propeptides exposes telopeptides, which by engaging in site-specific intermolecular interactions drive collagen self-assembly.In native tissues a precise balance between the processes of biosynthesis and degradation maintains the physiological homeostasis of tissue collagens. At the same time, accelerated biosynthesis is required for proper wound healing, whereas excessive accumulation of collagen is the hallmark of a number of localized fibrotic diseases, such as keloids and hypertrophic scars, and systemic fibrosis, such as systemic scleroderma.Localized fibrotic reactions are quite common and frequently develop as a consequence of surgical procedures. For instance, after surgery of the abdomen, the formation of excessive scar tissue around abdominal organs, such as the intestines, can interfere with the functionality of such organs and may cause severe pain and even death. Another situation where excessive scar formation presents a major complication is in the eye after glaucoma surgery performed to create a pressuremaintenance valve. Frequently, however, excessive scar formation closes this pressure-reducing valve, thereby forcing the intraocular pressure to rise (5). Moreover, excessive scarring of the vocal folds may severely alter their ability to vibrate, thereby causing a number of voice disorders (6).At present, several biological processes critical for development of fibrotic lesions are considered potential targets for inhibitors of fibrosis. These inhibit...

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“…[3] Any alterations of FN conformation caused by binding of FN ligand/s, and/or by posttranslation modifications, including its fragmentation by proteases, [11−13] has been reported to disturb FN domain arrangement, can alter tissue architecture, affecting biological activities and cellular communication, and can lead in turn to tissue dysfunctions. [2,4−6] FN has an ability to form crosslinked high-molecular complexes with FN fragments, [11−13] various extracellular matrix, [14] and some blood plasma components including fibrin. [15,16] During blood clotting transglutaminase XIII a catalyzes cross-linking of plasma FN to the fibrin clot via an isopeptide bond.…”

Section: Identification Of Soluble Supramolecular Fn-fibrin Complexesmentioning

confidence: 99%

Identification of Soluble Supramolecular FN-fibrin Complexes in Human Plasma

Krzyżanowska-Gołąb

Lemańska-Perek

Pupek

et al. 2014

Journal of Immunoassay and Immunochemistry

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SDS-agarose FN immunoblotting of 257 normal and pathological human plasma samples revealed the ladder pattern of multiple plasma FN bands which corresponded to FN monomer and dimer, and 5 FN-fibrin bands with increasing molecular masses. The FN-fibrin bands of about 750 kDa, 1000 kDa, 1300 kDa, 1600 kDa, and 1900 kDa appeared more frequently and in significantly higher relative amounts in the pathological samples (P < 0.000) than in relatively healthy individuals. The revealing of high-molecular FN-fibrin complexes by SDS-agarose FN immunobloting might have the potential to become a laboratory biomarker of some diseases in which the coagulation system is triggered.

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Guilty by Association: Some Collagen II Mutants Alter the Formation of ECM as a Result of Atypical Interaction with Fibronectin

Cited by 34 publications

References 47 publications

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Fibronectin-dependent collagen I deposition modulates the cell response to fibronectin

Collagen Fibril Formation

Identification of Soluble Supramolecular FN-fibrin Complexes in Human Plasma

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