Building Collagen Molecules, Fibrils, and Suprafibrillar Structures

Hulmes, David J.S.

doi:10.1006/jsbi.2002.4450

Cited by 489 publications

(338 citation statements)

References 49 publications

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“…The cysteine residues play an important role in this process through formation of intra-and interchain disulfide bonds. 27 Intrachain disulfide bonds are formed between cysteine residues 1393 and 1438 and the cysteine residues 1323 and 1485, respectively. Cysteine residues 1283, 1289, 1306 and 1315 are involved in interchain disulfide bonding.…”

Section: Discussionmentioning

confidence: 99%

“…Truncated chains lacking a substantial part of the C-propeptide are hardly or not incorporated into the collagen trimer. 21,27 Mutations that introduce a new cysteine residue within the C-propeptide may have a similar deleterious effect on chain association and trimer formation. By introducing a cysteine residue in exon 53, close to C1393, the Y1391C mutation may disturb normal intrachain disulfide bond formation.…”

Section: Discussionmentioning

confidence: 99%

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Czech dysplasia metatarsal type: another type II collagen disorder

Hoornaert

Mařík²,

Kozlowski

et al. 2007

Eur J Hum Genet

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Czech dysplasia metatarsal type is an autosomal-dominant disorder characterized by an early-onset, progressive spondyloarthropathy with normal stature. Shortness of third and/or fourth toes is a frequently observed clinical feature. Similarities between individuals with this dysplasia and patients with an R275C mutation in the COL2A1 gene, prompted us to analyze the COL2A1 gene in the original families reported with Czech dysplasia. Targeted sequencing of exon 13 of the COL2A1 gene was performed, followed by sequencing of the remaining exons in case the R275C mutation was not identified. We identified the R275C substitution in two of the original patients reported with Czech dysplasia and three additional patients. All affected individuals had a similar phenotype characterized by normal height, spondyloarthropathy, short postaxial toes and absence of ocular and orofacial anomalies. The R275C mutation was excluded in a third patient reported with Czech dysplasia. However, the identification of the Y1391C mutation in this patient with disproportionate short stature made the diagnosis of spondyloperipheral dysplasia (SPD) more probable. The Y1391C mutation is located in the C-propeptide of the procollagen chain and has been reported before in a patient with the Torrance type of lethal platyspondylic skeletal dysplasia (PLSD-T). Our observation of the same Y1391C mutation in an additional unrelated patient with SPD further supports the evidence that PLSD-T and SPD represent a phenotypic continuum. The R275C mutation in the COL2A1 gene causes a specific type II collagen disorder that was recently delineated as Czech dysplasia.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Czech dysplasia metatarsal type: another type II collagen disorder

Hoornaert

Mařík²,

Kozlowski

et al. 2007

Eur J Hum Genet

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“…Here, we have used SCFS to study early events of integrin-mediated cellular adhesion to a structurally well defined collagen type I matrix. Collagens are a protein family containing Ͼ20 members, which are divided into fibrilforming and nonfibrillar groups (Hulmes, 2002). Fibrillar collagens, such as collagen type I, are the main component of the ECM where they help resisting tensile forces and provide the major biomechanical scaffold for cell attachment (Kadler et al, 1996).…”

mentioning

confidence: 99%

Revealing Early Steps of α₂β₁Integrin-mediated Adhesion to Collagen Type I by Using Single-Cell Force Spectroscopy

Taubenberger

Cisneros

Friedrichs

et al. 2007

MBoC

192

197

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We have characterized early steps of ␣ 2 ␤ 1 integrin-mediated cell adhesion to a collagen type I matrix by using single-cell force spectroscopy. In agreement with the role of ␣ 2 ␤ 1 as a collagen type I receptor, ␣ 2 ␤ 1 -expressing Chinese hamster ovary (CHO)-A2 cells spread rapidly on the matrix, whereas ␣ 2 ␤ 1 -negative CHO wild-type cells adhered poorly. Probing CHO-A2 cell detachment forces over a contact time range of 600 s revealed a nonlinear adhesion response. During the first 60 s, cell adhesion increased slowly, and forces associated with the smallest rupture events were consistent with the breakage of individual integrin-collagen bonds. Above 60 s, a fraction of cells rapidly switched into an activated adhesion state marked by up to 10-fold increased detachment forces. Elevated overall cell adhesion coincided with a rise of the smallest rupture forces above the value required to break a single-integrin-collagen bond, suggesting a change from single to cooperative receptor binding. Transition into the activated adhesion mode and the increase of the smallest rupture forces were both blocked by inhibitors of actomyosin contractility. We therefore propose a two-step mechanism for the establishment of ␣ 2 ␤ 1 -mediated adhesion as weak initial, single-integrin-mediated binding events are superseded by strong adhesive interactions involving receptor cooperativity and actomyosin contractility. INTRODUCTIONIntegrins are a family of ␣/␤-heterodimeric receptors involved in cell-cell adhesion and cell attachment to the extracellular matrix (Hynes, 1992). In adherent cells, integrins are often arranged into highly organized structures, such as focal complexes, focal adhesions, and fibrillar adhesions . In these mature adhesive contacts, integrins are linked to the actin cytoskeleton via their intracellular domains and a multitude of adapter proteins, such as vinculin, talin, and ␣-actinin (Zamir and Geiger, 2001). Whereas the molecular composition of integrin complexes and signaling pathways controlling their macroscopic assembly or disassembly have been analyzed in detail, less is known about the early molecular events leading to the formation of integrin-based adhesion.Generally, integrin-mediated adhesion is thought to be initiated on the cell membrane by the engagement of individual integrin dimers with their respective ligand (Lotz et al., 1989;Gallant and Garcia, 2006). The number of receptorligand pairs may then grow by increasing the cell-substrate contact area and by receptor diffusion within that zone. Subsequent adhesion strengthening occurs through integrin clustering and linkage to the cytoskeleton. In addition, the ligand affinity of the integrins may increase as a result of intracellular regulatory pathways (Hughes and Pfaff, 1998). At a later stage, the assembly of higher-order integrincytoskeletal complexes requires actomyosin-driven contractility under the control of the small guanosine triphosphatase (GTPase) RhoA (Chrzanowska-Wodnicka and Burridge, 1996) and its downstream target Rho-assoc...

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“…It was known that the associating degree of collagen molecules in solution depended on pH, i.e., the higher the pH is, the thicker and longer fibers formed in solution. 2,31,32 When pH was very low (such as pH 3.4), the collagen molecules were completely in monomer state due to the strong electrostatic repulsive force between the molecules. Then, the collagen monomers in the solution were considered to adsorb onto substrate as it is.…”

Section: Influence Of Collagen Associating On the Self-assembly Strucmentioning

confidence: 99%

“…Collagen molecules coil into left-handed helixes with about 300 nm in length and 1.5 nm in diameter 1 and associate in different degrees to become various sized strands, such as micro-fibrils, fibrils or fibers of collagen, depending on the pH condition. 2 Since collagen is the most important protein for composing body tissues, it is often selected for preparing replacement biomaterials, such as artificial skin, blood vessel and bone implant. [3][4][5] Many researchers think that the assembly behavior of protein at interface could be applied in biosensor and protein expression techniques.…”

Section: Introductionmentioning

confidence: 99%

Construction and Biofunction of 3‐Dimensional Self‐assembly Collagen Nanostructure on PLLA Substrate

Liu

Lin

et al. 2010

Chin. J. Chem.

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A 3-dimensional and multi-layered network nanostructure of collagen assembled on the poly(L-lactic) acid (PLLA) substrate was reported. Collagen adsorption layers were prepared by dipping PLLA substrates into collagen solutions with various pH. The influences of adsorption interval, pH of collagen solutions and properties of PLLA substrate on the adsorption behavior of collagen were investigated by using atomic force microscopy and ellipsometry measurements. It was found that the multiple association degrees of collagen molecules in solution at a certain pH value seemed to play an important role in the adsorption process. The distinct adsorption behavior determined a specific 3-dimensional structure formed at the interface. Furthermore, calcium carbonate (CaCO 3 ) can be biomimetically crystallized by the inducement of biomineralization on these collagen layers.

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Building Collagen Molecules, Fibrils, and Suprafibrillar Structures

Cited by 489 publications

References 49 publications

Czech dysplasia metatarsal type: another type II collagen disorder

Czech dysplasia metatarsal type: another type II collagen disorder

Revealing Early Steps of α₂β₁Integrin-mediated Adhesion to Collagen Type I by Using Single-Cell Force Spectroscopy

Construction and Biofunction of 3‐Dimensional Self‐assembly Collagen Nanostructure on PLLA Substrate

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Building Collagen Molecules, Fibrils, and Suprafibrillar Structures

Cited by 489 publications

References 49 publications

Czech dysplasia metatarsal type: another type II collagen disorder

Czech dysplasia metatarsal type: another type II collagen disorder

Revealing Early Steps of α2β1Integrin-mediated Adhesion to Collagen Type I by Using Single-Cell Force Spectroscopy

Construction and Biofunction of 3‐Dimensional Self‐assembly Collagen Nanostructure on PLLA Substrate

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Revealing Early Steps of α₂β₁Integrin-mediated Adhesion to Collagen Type I by Using Single-Cell Force Spectroscopy