Publications
Here is a selection of publications where different laminin isoforms were used to create more authentic cell culture systems.
Laminin-211 in skeletal muscle function
Holmberg J., Durbeej M. Cell Adh Migr, 2013
This review focus on the importance of laminin-211 for normal skeletal muscle function.
Skeletal muscle laminin and MDC1A: pathogenesis and treatment strategies
Gawlik K. and Durbeej M. Skelet Muscle, 2011
In this review, the authors introduce laminin-211 and describe its structure, expression pattern in developing and adult muscle and its receptor interactions. They also discuss the molecular pathogenesis of MDC1A and advances toward the development of treatment.
Laminin therapy for the promotion of muscle regeneration
Riederer I., Bonomo A.C., Mouly V., Savino W.FEBS Lett., 2015
Accumulating data show that the local microenvironment plays a major role during muscle regeneration. In the satellite cell niche, a major extracellular matrix protein is laminin. Human myoblasts transplanted into immunodeficient mice are preferentially located in laminin-enriched areas. Additionally, laminin-111 enhances myoblast proliferation in vitro and increases the expression of the α7β1 integrin-type laminin receptor. Intramuscular injection of laminin-111 ameliorates muscular pathology in mdx mice, protecting muscle fibers from damage. Moreover, transplantation of human myoblasts with laminin-111 into Rag/mdx immunodeficient recipients improved the efficacy of myoblast transplantation, increasing the number of human dystrophin-positive myofibres. Taken together, these data strongly indicate that exogenous laminin can ameliorate the regeneration process in different models of muscular dystrophies and can be instrumental for improving cell therapy aiming at repairing the degeneration/regeneration process in skeletal muscle.
Tissue distribution of the laminin β1 and β2 chain during embryonic and fetal human development
Roediger M., Miosge N., Gersdorff N. J Mol Hist., 2010
Here, the authors investigated the tissue distribution of the laminin b1 and b2 chains on the protein level in various developing embryonic and fetal human organs between gestational weeks 8 and 12. The laminin b1 chain was ubiquitously expressed in the basement membrane zones of the brain, ganglia, blood vessels, liver, kidney, skin, pancreas, intestine, heart and skeletal system. Furthermore, the laminin b2 chain was present in the basement membrane zones of the brain, ganglia, skin, heart, and skeletal system. The findings of this study support and expand upon the theory that these two laminin chains are important during human development. In cartilage, the laminin b1 chain was expressed from gw 10 onwards but not during gw 8 and 9, whereas the detection of the laminin b2 chain was limited to gw 8 and 9. This indicates a developmental switch in the laminin b chain and suggests that the laminin b1 chain does not play a role in human cartilage development until the fetal stage. In human fetal cartilage (gw 17 and 24), a strong pericellular immunohistochemical reaction for laminin 111 was shown. In embryo chick sternum and mouse limb bud, laminin b1 and b2 chains are present in the cytoplasm of chondrocytes.
Immunohistochemical Distribution of Laminin-5 γ 2 Chain and its Developmental Change in Human Embryonic and Foetal Tissues
Lu W., Miyazaki K., Mizushima H., Nemoto N.
Here, immunohistochemical distribution of laminin γ2 chain, a subunit of the basement membrane protein laminin 332, was examined in 19 cases of human embryos and foetuses ranging from 4 to 25 weeks of gestation. Laminin γ2 was first detected in the basement membranes underlying ectodermal epithelial tissues, such as the skin and tooth, as early as 5–6 weeks of gestation. Between 6–7 and 12–13 weeks, laminin γ2 was detected in the basement membranes of various endodermal epithelial tissues, such as the bronchus, oesophagus, stomach, intestines, urinary bladder, gallbladder, and hepatopancreatic duct. The deposition of laminin γ2 in the basement membrane was associated with the process of morphogenesis. In the small intestine, laminin γ2 first appeared in the basement membrane of the primitive short villi, and its level gradually increased in the villus region but decreased in the cryptic region during the maturation of the organ. In addition, non-basement membrane immunoreactivity for laminin γ2 was detected in some mesoderm-derived tissues, such as the cartilage and skeletal and smooth muscle fibers. These results suggest a common role of laminin 332 and some specific roles of its γ2 chain in the morphogenesis of human tissues.
Immunohistochemical Distribution of Laminin-5 γ 2 Chain and its Developmental Change in Human Embryonic and Foetal Tissues
Lu W., Miyazaki K., Mizushima H., Nemoto N.The Histochemical Journal, 2001
Here, immunohistochemical distribution of laminin γ2 chain, a subunit of the basement membrane protein laminin 332, was examined in 19 cases of human embryos and fetuses ranging from 4 to 25 weeks of gestation. Laminin γ2 was first detected in the basement membranes underlying ectodermal epithelial tissues, such as the skin and tooth, as early as 5–6 weeks of gestation. Between 6–7 and 12–13 weeks, laminin γ2 was detected in the basement membranes of various endodermal epithelial tissues, such as the bronchus, oesophagus, stomach, intestines, urinary bladder, gallbladder, and hepatopancreatic duct. The deposition of laminin γ2 in the basement membrane was associated with the process of morphogenesis. In the small intestine, laminin γ2 first appeared in the basement membrane of the primitive short villi, and its level gradually increased in the villus region but decreased in the cryptic region during the maturation of the organ. In addition, non-basement membrane immunoreactivity for laminin γ2 was detected in some mesoderm-derived tissues, such as the cartilage and skeletal and smooth muscle fibers. These results suggest a common role of laminin 332 and some specific roles of its γ2 chain in the morphogenesis of human tissues.
Laminin/β1 integrin signal triggers axon formation by promoting microtubule assembly and stabilization
Lei W.L., Xing S.G., Deng C.Y., Ju X.C., Jiang X.Y., Luo Z.G.Cell Research 2012
In this study, the authors present several lines of evidence implicating the indispensable role of laminin in promoting neural polarization through integrin b1 (Itgb1) mediated microtubule assembly and stabilization. Laminin coated substrates (either in stripes or gradient) could initiate directional axon growth in undifferentiated neurites of both cultured hippocampal neurons and cortical slices in an Itgb1 dependent manner. Impairing endogenous laminin function either by treatment with exogenous laminins or by abolishing Itgb1 signaling using siRNA, resulted in defective axonal formation. Conditional knock out mice with abrogated Itgb1 expression in dorsal telencephalic progenitors displayed defective expression/activity of neuronal polarity related proteins, SAD and LKB1 kinases in addition to abnormal axonal development of cortical pyramidal neurons. These results not only identify laminin/ integrin b1 signaling as a crucial step in axon initiation and development but also link extracellular matrix adhesion to cytoskeleton remodeling that occurs during neuronal polarization.
Laminin 521 maintains differentiation potential of mouse and human satellite cell-derived myoblasts during long-term culture expansion
Penton C.M., Badarinarayana V., Prisco J., Powers E., Pincus M., Allen R.E., August P.R. Skeletal Muscle, 2016
Here, the authors comprehensively examine the effect of physiologically relevant laminins, laminin-211 and laminin-521, compared to traditionally utilized ECMs (e.g., laminin-111, gelatin, and Matrigel) to assess their capacity to propagate and preserve myogenic differentiation potential. The results demonstrate laminin-521 is a superior substrate for both short-term and long-term myogenic cell culture applications compared to other commonly utilized substrates. Laminin-521 also provides more consistent and reliable differentiation over long-term culture. Laminin-521 supported increased proliferation in early phases of expansion and was the only substrate facilitating high-level fusion following eight passages in mouse myoblast cell cultures. In human myoblast cell cultures, laminin 521 supported increased proliferation during expansion and superior differentiation with myotube hypertrophy. Counterintuitively, however, laminin-211, the native laminin isoform in resting skeletal muscle, resulted in the low proliferation and poor differentiation in mouse and human cultures. Matrigel performed well in short-term mouse studies but showed high amounts of variability following long-term expansion.