Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity.

Yurchenco, Peter D.; Tsilibary, Effie-Photini C; Charonis, Aristidis S.; Furthmayr, Heinz

doi:10.1016/s0021-9258(17)39656-4

Cited by 249 publications

(54 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Much like type IV collagen, laminin can self-assemble in BM into a honeycomb-like polymer. Self-assembly of the heterotrimeric laminins into oligomers is calcium dependent and attributed to the globular domain VI of each chain, although the mechanism remains elusive (10,20,30). The three-arm interaction model for laminin polymer selfassembly hypothesizes that the a-VI domain, b-VI domain, and c-VI domain bind and form the honeycomb network depicted in Figure 3 (31,32).…”

Section: Basement Membrane Assemblymentioning

confidence: 99%

Structure and Function of Basement Membranes

LeBleu

MacDonald

Kalluri

2007

Exp Biol Med (Maywood)

485

425

View full text Add to dashboard Cite

Basement membranes (BMs) are present in every tissue of the human body. All epithelium and endothelium is in direct association with BMs. BMs are a composite of several large glycoproteins and form an organized scaffold to provide structural support to the tissue and also offer functional input to modulate cellular function. While collagen I is the most abundant protein in the human body, type IV collagen is the most abundant protein in BMs. Matrigel is commonly used as surrogate for BMs in many experiments, but this is a tumor-derived BM-like material and does not contain all of the components that natural BMs possess. The structure of BMs and their functional role in tissues are unique and unlike any other class of proteins in the human body. Increasing evidence suggests that BMs are unique signal input devices that likely fine tune cellular function. Additionally, the resulting endothelial and epithelial heterogeneity in human body is a direct contribution of cell-matrix interaction facilitated by the diverse compositions of BMs.

show abstract

Section: Basement Membrane Assemblymentioning

confidence: 99%

Structure and Function of Basement Membranes

LeBleu

MacDonald

Kalluri

2007

Exp Biol Med (Maywood)

485

425

View full text Add to dashboard Cite

show abstract

“…This report further demonstrates the importance of limiting secreted protein diffusion to enhance local pericellular protein concentrations to promote matrix assembly in a cell culture system. In earlier reports Yurchenko and co-workers demonstrated that BL assembly can be recapitulated in vitro using purified basement membrane components (Yurchenco et al 1985(Yurchenco et al ,1992. In an earlier study using the L-2 cell culture system, Delvoye et al (1988) suggested that such a mechanism might be applicable but dismissed the concept as a result of the outcome of their studies.…”

Section: Discussionmentioning

confidence: 99%

In Vitro Matrix Assembly Induced by Critical Assembly Concentration (CAC)

Lauer

McCarthy

2002

J Histochem Cytochem.

View full text Add to dashboard Cite

L-2 cells are an immortalized cell line derived from yolk sac parietal endoderm cells, which are responsible for the production of Reichert's membrane, a thick basement membrane produced during rat gestation. Although the L-2 cells secrete all the major components of the basal lamina, they do not assemble a robust matrix in cell culture. We hypothesized that the reason L-2 cells fail to assemble a matrix in cell culture is because the concentrations of matrix components necessary for this matrix assembly do not reach a critical association concentration (CAC) under standard cell culture conditions. To limit the diffusion of secreted molecules while maintaining a nutrient-rich environment for the cells to thrive, we developed a technique that uses a dialysis membrane to limit protein diffusion in a 2-well plate format. This technique permits L-2 cells to assemble a robust matrix in as little as 24 hr that continues to be formed for at least 72 hr. This technique may address some of the physical limitations imposed by cell culture and could be readily applied to other cell types and medium conditions.

show abstract

“…Laminin polymers are the bioactive forms of this glycoprotein. In vitro laminin polymerization was first demonstrated in a cell-free system, dependent on a critical protein concentration, which was optimized by the use of planar lipid bilayers containing sulfated glycolipids and has since been studied extensively in cultured cells [19,20]. More recently, it was demonstrated that laminin could self-polymerize in a cell-free and lipid-free environment forming a polymer called polylaminin that recapitulates the in vivo protein architecture [21,22].…”

Section: Polylaminin's Effects On Cardiac Stiffnessmentioning

confidence: 99%

Change the Laminin, Change the Cardiomyocyte: Improve Untreatable Heart Failure

Hochman‐Mendez¹,

Curty²,

Taylor³

2020

IJMS

View full text Add to dashboard Cite

No effective medical treatment exists for heart failure with preserved ejection fraction (HFpEF), accounting for approximately half of all heart failure cases. The elevated passive myocardial stiffness in HFpEF is attributed to a combination of alterations in the extracellular matrix (ECM) collagen content and modifications in the sarcomeric protein titin. Here, we propose polylaminin, a biomimetic polymer of laminin, as a promising approach for manipulating the titin isoform shift and phosphorylation in cardiomyocytes. Exploring the pleiotropic effects of polylaminin may be a novel strategy for alleviating symptoms in HFpEF’s multifactorial pathophysiology.

show abstract

Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity.

Cited by 249 publications

References 26 publications

Structure and Function of Basement Membranes

Structure and Function of Basement Membranes

In Vitro Matrix Assembly Induced by Critical Assembly Concentration (CAC)

Change the Laminin, Change the Cardiomyocyte: Improve Untreatable Heart Failure

Contact Info

Product

Resources

About