Laminin α1 is essential for mouse cerebellar development

Ichikawa‐Tomikawa, Naoki; Ogawa, Jun; Douet, Vanessa; Xu, Zhuo; Kamikubo, Yuji; Sakurai, Takashi; Kohsaka, Shinichi; Chiba, Hideki; Yamada, Yoshihiko; Arikawa‐Hirasawa, Eri

doi:10.1016/j.matbio.2011.09.002

Cited by 58 publications

(52 citation statements)

References 59 publications

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“…Thus, as in mammals, zebrafish lama1 is temporally regulated to be expressed broadly in early embryogenesis and down-regulated in late embryogenesis. This expression pattern overlaps with the distribution of Laminin-111, the main Laminin -containing isoform in embryos, and is consistent with defects in the development of the notochord, cerebellum and the eye in zebrafish bal mutant and conditional Lama1 knockout mice [23,[45][46][47][48][49][50]. Furthermore, the emergence of LAMA1 mutations associated with developmental defects in the cerebellum and retina in humans suggests a conversed expression pattern and function for Laminin 1 during evolution [51].…”

Section: Conservation Of Lama1 Expression Pattern In Vertebratessupporting

confidence: 63%

Hedgehog signalling acts upstream of Laminin alpha1 transcription in the zebrafish paraxial mesoderm

et al. 2017

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Section: Conservation Of Lama1 Expression Pattern In Vertebratessupporting

confidence: 63%

Hedgehog signalling acts upstream of Laminin alpha1 transcription in the zebrafish paraxial mesoderm

et al. 2017

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“…These four proteins can bind to each other as shown by the solid lines in Fig. 4 [34, 35]. Their stability is enhanced by a direct interaction with TIMP1 [36] and via an indirect positive action by IL-8 [37].…”

Section: Resultsmentioning

confidence: 99%

“…However, it is a fact that laminins interact with several integrin isoforms and are involved in migration and development [35, 68]. Moreover, since the gene expression of LAMA1 was down-regulated in MCS cells, an impact of this gene or protein seems to be very likely.…”

Section: Discussionmentioning

confidence: 99%

Cytokine Release and Focal Adhesion Proteins in Normal Thyroid Cells Cultured on the Random Positioning Machine

Warnke

Pietsch

Kopp

et al. 2017

Cell Physiol Biochem

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Background/Aims: Spaceflight impacts on the function of the thyroid gland in vivo. In vitro normal and malignant thyrocytes assemble in part to multicellular spheroids (MCS) after exposure to the random positioning machine (RPM), while a number of cells remain adherent (AD). We aim to elucidate possible differences between AD and MCS cells compared to 1g-controls of normal human thyroid cells. Methods: Cells of the human follicular epithelial thyroid cell line Nthy-ori 3-1 were incubated for up to 72 h on the RPM. Afterwards, they were investigated by phase-contrast microscopy, quantitative real-time PCR and by determination of cytokines released in their supernatants. Results: A significant up-regulation of IL6, IL8 and CCL2 gene expression was found after a 4h RPM-exposure, when the whole population was still growing adherently. MCS and AD cells were detected after 24 h on the RPM. At this time, a significantly reduced gene expression in MCS compared to 1g-controls was visible for IL6, IL8, FN1, ITGB1, LAMA1, CCL2, and TLN1. After a 72 h RPM-exposure, IL-6, IL-8, and TIMP-1 secretion rates were increased significantly. Conclusion: Normal thyrocytes form MCS within 24 h. Cytokines seem to be involved in the initiation of MCS formation via focal adhesion proteins.

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“…25,42 Due to the lack of these essential components, the basement membrane changes in lungs and kidneys lead to intrauterine or postpartum death. It is important to note that postnatal development is possible in mice with a lack of b1-integrins 11 or the a1 subunit of laminin; 17 however, cerebellar fissuration and foliation disorder are also present. The loss of Purkinje cell polarity, ectopic EGL cells along the fusion line of 2 opposing folia, and atrophied internal granular layer are identical to those observed in our study.…”

Section: Characteristics Of Lissencephaly Type IImentioning

confidence: 99%

Vitamin C Depletion in Prenatal Guinea Pigs as a Model of Lissencephaly Type II

Čapo¹,

Hinić²,

Lalošević³

et al. 2014

Vet Pathol

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Humans and guinea pigs are unable to produce vitamin C, with deficiency resulting in a well-known disorder of collagen synthesis. Pial basement membrane structure preservation is essential in the proper migration of neurons. In our study, intrauterine deprivation of vitamin C in guinea pig fetuses led to a collagen synthesis disorder, weakness, and finally a breach of pial basement membrane. We found excessive migration of the external germinal layer cells into the subarachnoid space of the cerebellum through defects in the pial basement membrane. The changes ranged from focal rupture of pial basement membranes to their complete disintegration. The loss of proper folia formation resulted in macroscopically visible flattening of the cerebellar surface. Different grades of dysplastic changes in the folia of the cerebellar cortex were observed in 2 experimental groups assigned different limits to mark the time of commencement and duration of vitamin C deprivation. The most severe form of dysplastic changes was characterized by marked irregularity of the cerebellar cortex similar to that in lissencephaly type II. Thus, prenatal vitamin C deficiency represents a novel animal model to study the effects of collagen synthesis on development of breaches in the pial basement membrane, disordered migration of neurons, dysplasia of cerebellar cortex, and the pathogenesis of lissencephaly.Keywords scurvy, cerebellum, guinea pigs, vitamin c deficiency, lissencephaly, animal model Lissencephaly type II is a disease caused by alteration to the pial basement membrane (PBM) proteins, which causes it to weaken and become porous. This causes a deficiency of the glia limitans superficialis and radial glial cell connectivity. As a result, migrating neural cells pass through the pial gaps to form cell ectopia near the brain surface. This leads to loss of gyri and sulci, forming irregularities on the brain surface and a so-called cobbled formation, which is why lissencephaly type II is also sometimes called cobblestone lissencephaly. 9,34Based on the fact that the structural integrity of the PBM is necessary for proper migration of the neurons, 2 main approaches have been established for experimental modeling of lissencephaly type II. First, animal models with targeted inactivation of genes involved in membrane protein synthesis have been studied. The lack of these proteins, such as collagen, laminin, and others, causes the PBM to weaken and finally rupture. 13,16,17,25,43 The second approach uses chemical destruction of meningeal cells over the developing cerebellum through exposure to 6-hydroxydopamine (6-OHDA). The loss of glio-pial membrane allows for overmigration of neurons through the pial breaches into the subarachnoid space. 1,29,30 Collagen is one of the key structural units of the basement membrane, and its synthesis is dependent on vitamin C. Humans, monkeys, and guinea pigs are unable to synthesize vitamin C because of a lack of L-gulono-g-lactone oxidase. 27It is well known that a deficiency of vitamin C in guinea...

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Laminin α1 is essential for mouse cerebellar development

Cited by 58 publications

References 59 publications

Hedgehog signalling acts upstream of Laminin alpha1 transcription in the zebrafish paraxial mesoderm

Hedgehog signalling acts upstream of Laminin alpha1 transcription in the zebrafish paraxial mesoderm

Cytokine Release and Focal Adhesion Proteins in Normal Thyroid Cells Cultured on the Random Positioning Machine

Vitamin C Depletion in Prenatal Guinea Pigs as a Model of Lissencephaly Type II

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