Building collagen IV smart scaffolds on the outside of cells

Brown, Kyle L.; Cummings, Christopher F.; Vanacore, Roberto M.; Hudson, Billy G.

doi:10.1002/pro.3283

Cited by 67 publications

(61 citation statements)

References 69 publications

(170 reference statements)

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“…Type IV collagen is a major constituent of BMs. This evolutionarily conserved protein forms networks and plays a crucial structural role in the maintenance of BM architecture (Brown et al, 2017;Fidler et al, 2018). In addition, it serves as a ligand for cell-surface integrins, thus influencing cell adhesion, migration and differentiation (Wang et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

Casino

Gozalbo-Rovira

Rodrı́guez-Dı́az

et al. 2018

IUCrJ

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Crystal structures of the noncollagenous domains of the collagen type IV α1–α5 chains provide structural insight into Alport’s syndrome (a genetic kidney disorder) and the first views of the components of Goodpasture’s autoimmune disease epitopes. These structures define key folding motifs for collagen IV scaffolding of basement membranes, support the operation of mechanisms for restricting the self-assembly of noncollagenous domains, and raise the possibility that homohexamers of α1 or α3 chains could occur in nature.

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Section: Introductionmentioning

confidence: 99%

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

Casino

Gozalbo-Rovira

Rodrı́guez-Dı́az

et al. 2018

IUCrJ

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“…Basement membranes are well‐known structural features of many tissues, providing a substrate for epithelial cell attachment and organization, as well as separating epithelial and mesenchymal tissues . The basement membrane provides a well‐known barrier to epithelial (carcinoma) cell invasion, and a classical feature of malignancy is tumour cell invasion across the basement membrane.…”

Section: Basement Membrane Dynamicsmentioning

confidence: 99%

Extracellular matrix dynamics in cell migration, invasion and tissue morphogenesis

Yamada

Collins

Walma

et al. 2019

Int J Experimental Path

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This review describes how direct visualization of the dynamic interactions of cells with different extracellular matrix microenvironments can provide novel insights into complex biological processes. Recent studies have moved characterization of cell migration and invasion from classical 2D culture systems into 1D and 3D model systems, revealing multiple differences in mechanisms of cell adhesion, migration and signalling-even though cells in 3D can still display prominent focal adhesions.Myosin II restrains cell migration speed in 2D culture but is often essential for effective 3D migration. 3D cell migration modes can switch between lamellipodial, lobopodial and/or amoeboid depending on the local matrix environment. For example, "nuclear piston" migration can be switched off by local proteolysis, and proteolytic invadopodia can be induced by a high density of fibrillar matrix. Particularly, complex remodelling of both extracellular matrix and tissues occurs during morphogenesis. Extracellular matrix supports self-assembly of embryonic tissues, but it must also be locally actively remodelled. For example, surprisingly focal remodelling of the basement membrane occurs during branching morphogenesis-numerous tiny perforations generated by proteolysis and actomyosin contractility produce a microscopically porous, flexible basement membrane meshwork for tissue expansion. Cells extend highly active blebs or protrusions towards the surrounding mesenchyme through these perforations. Concurrently, the entire basement membrane undergoes translocation in a direction opposite to bud expansion. Underlying this slowly moving 2D basement membrane translocation are highly dynamic individual cell movements. We conclude this review by describing a variety of exciting research opportunities for discovering novel insights into cell-matrix interactions. K E Y W O R D S3D culture, basement membrane remodelling, branching morphogenesis, cell migration, extracellular matrix, invasion

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“…One is the globular C-terminal domain, whose presence inhibits fibril formation and is proteolytically removed from fibril-forming collagens prior to assembly (11). By contrast, the C-terminal non-collagenous domain of collagen IV (NC1) is not removed, and plays a central, chloride-directed role in forming networks (12,13). The second distinguishing feature of collagen IV is the presence of natural discontinuities (interruptions) in the (Gly-X-Y)n repeating unit within its collagenous domain.…”

Section: Introductionmentioning

confidence: 99%

Sequence-dependent mechanics of collagen reflect its structural and functional organization

Al-Shaer¹,

Lyons²,

Ishikawa

et al. 2020

Preprint

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Extracellular matrix mechanics influence diverse cellular functions, yet surprisingly little is known about the mechanical properties of their constituent collagens. In particular, network-forming collagen IV, an integral component of basement membranes, has been far less studied than fibril-forming collagens. A key feature differentiating collagen IV is the presence of interruptions in the triple-helix-defining (Gly-X-Y) sequence along its collagenous domain. Here, we used atomic force microscopy (AFM) to determine the impact of these interruptions on the flexibility of collagen. Our extracted flexibility profile reveals that collagen IV possesses highly heterogeneous mechanics, ranging from semi-flexible regions as found for fibril-forming collagens to a lengthy region of high flexibility towards its N terminus. A simple model in which flexibility is dictated only by the presence of interruptions fit the extracted profile reasonably well, providing insight into the alignment of chains and supporting the role of interruptions in instilling flexibility. However, limitations of this model were illuminated by our determination of variable flexibility along continuously triple-helical collagen III, which we found to possess a high-flexibility region around its matrix-metalloprotease (MMP) binding site. Surprisingly, proline content did not correlate with local flexibility in either collagen type. We also found that physiologically relevant changes in pH and chloride concentration did not alter the flexibility of collagen IV, indicating such environmental changes are not used to control its compaction during secretion. Although extracellular chloride ions play a role in triggering collagen IV network formation, they do not appear to modulate the structure of its collagenous domain.

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Building collagen IV smart scaffolds on the outside of cells

Cited by 67 publications

References 69 publications

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

Structures of collagen IV globular domains: insight into associated pathologies, folding and network assembly

Extracellular matrix dynamics in cell migration, invasion and tissue morphogenesis

Sequence-dependent mechanics of collagen reflect its structural and functional organization

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