Biorelevant culture of intestinal cells on Biolaminin substrates

Laminin expression in the intestine

The small intestine contains mucosal epithelial invaginations called crypts of Lieberkühn that are continuous with evaginations into the lumen called villi. The intestinal epithelia are self-renewed by a population of intestinal stem cells within the intestinal crypt that gives rise to progenitor cells, which can subsequently differentiate into the mature cell types. The intestinal epithelium is in direct contact with a basement membrane. All laminin a-chains (laminin 111, 211, 332, 411 and 511) are expressed at significant amounts in the small intestine. Importantly, they are distributed in specific patterns along the crypt-villus axis of the intestine and are developmentally regulated (Teller, 2007; Lefebvre, 1999). 

Laminin 111 has a vital role in the early developing intestine

The α1 laminin expression is restricted to the intervillous areas in the early developing intestine and is gradually replaced by the α2 laminins as crypts begin to form. The α3 and α5 laminins were both expressed at the base of the intestinal epithelium at the early stages of gut development but tend to be restricted to the villus from mid-gestation onward. The α4 laminins are not expressed in the epithelial basement membrane (Teller, 2007).

Alpha-5 laminins are crucial for establishing and maintaining the intestinal architecture

The villus basement membrane is rich in laminin α5 which is crucial for both establishing and maintaining the small intestinal crypt-villus architecture (Mahoney, 2008; Ritié, 2011). In a publication by Ritié et al., the authors described a mechanistic link between laminin α5 gene deficiency and the physiological phenotype showing that laminin a5 plays a crucial role in both epithelial and mesenchymal cell behavior by regulating Wnt and PI3K signaling (Ritié, 2011). Laminin 511 was shown to stimulate the expression and activity of the survival factor Akt and stimulate cell adhesion, migration as well as epithelial differentiation (Ritié, 2011). In the absence of laminin α5, the proliferative compartment of the intestine expanded, suggesting a delay in initiating differentiation (Mahoney, 2008). Lack of the laminin α5 chain was accompanied by a decrease in epithelial α3β1 integrin and the Lutheran receptor, indicating that those are likely targets for the laminin α5 laminins (Bolcato-Bellemin, 2003). The B4 integrin is also expressed in the Enterocytes differentiated normally in the absence of laminin α5 but the terminal differentiation of goblet cells was affected, as shown by the increased numbers of intermediate cells and alteration of mucous granules towards the colon type (Mahoney, 2008). The α5 laminins have also shown a major role in intestinal smooth muscle organization and differentiation (Bolcato-Bellemin, 2003).

We recommend Biolaminin 111 for early intestinal specification and Biolaminin 511 for maturation and maintenance.


WHAT OUR CUSTOMERS SAY

“Biolaminin 521 has simplified the day-to-day expansion of our human pluripotent stem cells and significantly reduced the operator time. Our new costs are only a fraction of what they used to be when we relied on MEFs.”

Dr. Roger E. Rönn,

Univ. of Edinburgh, Scotland


Biolaminin Key Advantages

Different laminin isoforms are distributed in specific patterns along the crypt-villus axis of the intestine and are developmentally regulated. The laminin-111 expression is restricted to the intervillous areas in the early developing intestine. The villus basement membrane is rich in laminin α5, crucial for both establishing and maintaining the small intestinal crypt-villus architecture. Laminin α5 plays a crucial role in both epithelial and mesenchymal cell behavior by regulating Wnt and PI3K signaling.

Specific laminin isoforms are present in different tissue microenvironments and they are essential for cell survival, proliferation and differentiation. Biolaminin products allow you to imitate the natural cell-matrix interactions in vitro.

All our matrices are chemically defined and animal origin-free, which makes them ideal substrates for each level of the scientific process – from basic research to clinical applications.

Our products have consistent composition and quality. This enables minimized variability between experiments and uniform pluripotency gene expression profiles between different cell lines.

Numerous scientists have found our products and finally succeeded in their specific stem cell application. The power of full-length laminins incorporated into various cell systems is well documented in scientific articles and clinical trials.




  • Biolaminin 521 LN (LN521)

    Human recombinant laminin 521

    Biolaminin 521 LN is the natural laminin for pluripotent stem cells and therefore reliably facilitates self-renewal of human ES and iPS cells in a chemically defined, feeder-free and animal origin-free stem cell culture system. LN521 is animal origin-free to the primary level.
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  • Biolaminin 511 LN (LN511)

    Human recombinant laminin 511

    Biolaminin 511 is the natural laminin for mouse embryonic stem cells and allows sustained pluripotency without the need to use feeder cells or differentiation inhibitors like LIF.
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  • Biolaminin 111 LN (LN111)

    Human recombinant laminin 111

    Biolaminin 111 is commonly used as a general attachment protein for many cell types in vitro.
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  • Biosilk

    3D culture substrate

    Biosilk is a natural biomaterial made from recombinant spider silk protein, a useful tool for a wide range of 3D culture applications, such as organoid culture and other tissue engineering applications. Biosilk can be mixed with any Biolaminin matrix.
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