Laminin Peptides

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CAT# Product Name M.W Molecular Formula Inquiry
L01001 Laminin A Chain (2091-2108) 2016.3 C82H148N31O26S1 Inquiry
L01002 Laminin Penta Peptide, amide 593.7 C26H43N9O7 Inquiry
L01003 Laminin (929-933) 594.7 C26H42N8O8 Inquiry
L01005 H-Arg-Asn-Ile-Ala-Glu-Ile-Ile-Lys-Asp-Ile-OH 1184.4 Inquiry
L01008 H-Cys-Ser-Arg-Ala-Arg-Lys-Gln-Ala-Ala-Ser-Ile-Lys-Val-Ala-Val-Ser-Ala-Asp-Arg-OH 2017.34 Inquiry

Introduction

Laminin mainly exists in basal lamina structure, which is a specific non-collagen glycoprotein. Relative molecular weight of laminin is 820 kDa, containing 13-15% sugar, and it composed of heterotrimers of α, β and γ chains. Its structure presents an asymmetric cross shape by a long arm and three similar short arms (each of the arms has rod-shaped segments and spherical terminal domains). The short arm of chain β1 and β2 have two spherical structure domains, while the chain-α has three spherical domains structure, one of which binds to collagen type IV, a second binds to heparin, and a third binds to receptors on the cell surface. Therefore, the main function of laminin is the assembly of basal membrane as the main structural component of basal membrane, forming a network structure on the cell surface and fixing the cells on the basal membrane.

Mechanism of action

In skin wound healing, for example, laminin has been shown in reepithelialization and angiogenesis. Indeed, LAMA possesses five laminin-type G domain (LG) modules at the C-terminus, arranged in a tandem array, that are differentially processed under homeostatic conditions or during tissue repair. In fact, LAMA3, LAMA4, and LAMA5 chains are physiologically cleaved by proteases, such as plasmin and elastase, in the linker sequence between the LG3 and LG4 domains, and processing in this region has been shown to correlate with the speed of wound closure.

Application of Laminin peptides

At least 16 different isoforms of laminin exist, made by various combinations of the five α (LAMA1-5), three β (LAMB1-3), and three γ (LAMC1-3) chains that have been identified. Isoforms are accordingly named by their αβγ chains: for instance, laminin-332 contains LAMA3, LAMB3, and LAMC2 chains. The differential expression of laminin isoforms depends on tissue type and state. Laminins are involved in a variety of biological processes ranging from tissue survival, angiogenesis, and neural development, to skin reepithelialization and wound healing, and even cancer metastasis. Laminins have been shown to regulate core cellular activities, such as adhesion, apoptosis, proliferation, migration, and differentiation.

References

  1. Dekkers, B. G., Bos, I. S. T., Halayko, A. J., Zaagsma, J., & Meurs, H. (2010). The laminin β1-competing peptide YIGSR induces a hypercontractile, hypoproliferative airway smooth muscle phenotype in an animal model of allergic asthma. Respiratory research, 11(1), 170.
  2. Ishihara, J., Ishihara, A., Fukunaga, K., Sasaki, K., White, M. J., Briquez, P. S., & Hubbell, J. A. (2018). Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing. Nature communications, 9(1), 2163.
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