The laminin family

Aumailley, Monique

doi:10.4161/cam.22826

Cited by 361 publications

(348 citation statements)

References 82 publications

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“…Mouse laminin-111 [laminin isotype (31) containing the α1, β1, and γ1 paralogs, hereafter laminin] was treated with isotopic mixtures, differing by 12.076 Da, of the cross-linkers bis(sulfosuccinimidyl)suberate (BS3) and suberic acid dihydrazide (SDH) to target primary amine and carboxylic acid Significance Large, fibrous, and flexible extracellular matrix proteins are integral to development and maintenance of tissues in the body. Laminin is an extracellular matrix component that provides a physical substrate for cell adhesion and induces signaling pathways that maintain cell health and functionality.…”

Section: Resultsmentioning

confidence: 99%

Cross-linking reveals laminin coiled-coil architecture

Armony

Jacob

Moran

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Laminin, an ∼800-kDa heterotrimeric protein, is a major functional component of the extracellular matrix, contributing to tissue development and maintenance. The unique architecture of laminin is not currently amenable to determination at high resolution, as its flexible and narrow segments complicate both crystallization and single-particle reconstruction by electron microscopy. Therefore, we used cross-linking and MS, evaluated using computational methods, to address key questions regarding laminin quaternary structure. This approach was particularly well suited to the ∼750-Å coiled coil that mediates trimer assembly, and our results support revision of the subunit order typically presented in laminin schematics. Furthermore, information on the subunit register in the coiled coil and cross-links to downstream domains provide insights into the self-assembly required for interaction with other extracellular matrix and cell surface proteins.L aminins are network-forming constituents of the extracellular matrix (ECM) (1, 2). They interact with the cell surface and other ECM components to generate a physical and functional framework affecting cell viability, identity, and activity. The laminin family appears to have arisen during the evolution of multicellularity in animals (3), and laminins contribute to a diversity of basement membrane and connective tissue structures in mammals (2). Laminins are studied in the context of development (4), stem cell biology (5), tissue engineering (6), cancer (7), and aging (8). The remarkable structural organization of laminins underlies their important physiological functions.Laminins are composed of three subunits, α, β, and γ, that assemble into a roughly humanoid form as visualized using rotary shadowing electron microscopy (9). The individual subunits separately form the "head" and two "arms," which are composed of epidermal growth factor (EGF)-like cysteine-rich repeats with globular domains embedded (10) (Fig. 1). Following the head and arms, the three subunits come together to form a long coiled coil, constituting the "body." Additional globular domains unique to the α subunit are the "feet." The laminin head and arms may splay to form a tripod (2), a feature not captured in rotary shadowing images or in diagrams of domain composition. Due to the centrality of laminin in cell-ECM interactions, efforts have been made to analyze the functional regions of the trimer, to determine which α, β, and γ paralogs associate into physiological heterotrimers and to understand how trimers self-assemble into higher-order networks. Laminin fragments have been generated to assess their binding properties (11, 12) and as targets for structure determination by X-ray crystallography (13)(14)(15)(16)(17)(18)(19)(20).Despite this progress, few insights into the overall 3D architecture of laminin have been made in the past few decades, and certain regions of the complex have been neglected as targets of structural techniques. In particular, no structure has been determined for any segment of th...

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Section: Resultsmentioning

confidence: 99%

Cross-linking reveals laminin coiled-coil architecture

Armony

Jacob

Moran

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Examples of ECM proteins with significant impact on cellular dynamics are the laminins (Aumailley 2013). In normal tissues, the laminins form a major component of the basal lamina which functions to anchor the epithelium to the underlying stroma (Rousselle and Beck 2013).…”

Section: Extracellular Matrix Can Profoundly Influence Tumour Progresmentioning

confidence: 99%

Tumour–stroma crosstalk in the development of squamous cell carcinoma

Lim

South

2014

The International Journal of Biochemistry & Cell Biology

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“…1A) (Aumailley, 2013;Schéele et al, 2007). Laminins were reported to direct various cellular functions, including adhesion, migration, growth, differentiation and apoptosis, through intercommunication with specific cell surface receptors, such as dystroglycan, sulfated glycolipids or particular integrins (Fig.…”

Section: Introductionmentioning

confidence: 99%

The role of laminins in cartilaginous tissues: from development to regeneration

Sun¹,

Wang²,

Toh³

et al. 2017

eCM

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As a key molecule of extracellular matrix, laminin provides a delicate microenvironment for cell functions. Recent findings suggest that laminins expressed by cartilage-forming cells (chondrocytes, progenitor cells and stem cells) could promote chondrogenesis. However, few papers outline the effect of laminins on providing a favorable matrix microenvironment for cartilage regeneration. In this review, we delineated the expression of laminins in hyaline cartilage, fibrocartilage and cartilage-like tissue (nucleus pulposus) throughout several developmental stages. We also examined the effect of laminins on the biological activities of chondrocytes, including adhesion, migration and survival. Furthermore, we scrutinized the potential influence of various laminin isoforms on cartilage-forming cells' proliferation and chondrogenic differentiation. With this information, we hope to facilitate an understanding of the spatial and temporal interactions between cartilage-forming cells and laminin microenvironment to eventually advance cell-based cartilage engineering and regeneration.

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The laminin family

Cited by 361 publications

References 82 publications

Cross-linking reveals laminin coiled-coil architecture

Cross-linking reveals laminin coiled-coil architecture

Tumour–stroma crosstalk in the development of squamous cell carcinoma

The role of laminins in cartilaginous tissues: from development to regeneration

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