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Laminin Expression
Published by Anonymous on 2007/9/24 (1594 reads)
1: Matrix Biol. 2003 Mar;22(1):35-47.


Expression and biological role of laminin-1.

Ekblom P, Lonai P, Talts JF.

Department of Cell and Molecular Biology, BMC B12, Lund University, Sweden. Peter.Ekblom@medkem.lu.se

Of the approximately 15 laminin trimers described in mammals, laminin-1 expression seems to be largely limited to epithelial basement membranes. It appears early during epithelial morphogenesis in most tissues of the embryo, and remains present as a major epithelial laminin in some adult tissues. Previous organ culture studies with embryonic tissues have suggested that laminin-1 is important for epithelial development. Recent data using genetically manipulated embryonic stem (ES) cells grown as embryoid bodies provide strong support for the view of a specific role of laminin-1 in epithelial morphogenesis. One common consequence of genetic ablation of FGF signaling, beta1-integrin or laminin gamma1 chain expression in ES cells is the absence of laminin-1, which correlates with failure of BM assembly and epiblast differentiation. Partial but distinct rescue of epiblast differentiation has been achieved in all three mutants by exogenously added laminin-1. Laminin-1 contains several biologically active modules, but several are found in beta1 or gamma1 chains shared by at least 11 laminins. However, the carboxytermini of the alpha chains contain five laminin globular (LG) modules, distinct for each alpha chain. There is increasing evidence for a particular role of alpha1LG4 binding to its receptors for epithelial tubulogenesis. The biological roles of this and other domains of laminin-1 are currently being explored by genetic means. The pathways controlling laminin-1 synthesis have remained largely unknown, but recent advances raise the possibility that laminin-1 and collagen IV synthesis can be regulated by pro-survival kinases of the protein kinase B/Akt family.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 12714040 [PubMed - indexed for MEDLINE]

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2: Microsc Res Tech. 2000 Nov 1;51(3):228-37.


Transcriptional regulation of laminin gene expression.

Aberdam D, Virolle T, Simon-Assmann P.

INSERM U385, 06107 Nice, France. aberdam@unice.fr

Laminins are the most abundant structural non-collagenous glycoproteins ubiquitously present in basement membranes. They are multidomain molecules consisting of of alpha, beta, and gamma chains. Although the precise functional differences between the laminin variants are not well understood, the diversity of laminin isoforms may reflect the formation of distinct basement membranes. The laminins display a remarkable restricted expression profile, suggesting a fine regulation of their genes. In this review, we focus on the most recent developments of laminin biology, centering on transcriptional and posttranscriptional controls. We discuss only those laminin chains whose gene organization and promoter elements have been characterized and proved to be functional. When possible, we correlate the effects of growth factors, cytokines, retinoids, and transcription factors on laminin gene expression with the identity of cis-acting elements in their genomic control regions. Copyright 2000 Wiley-Liss, Inc.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 11054873 [PubMed - indexed for MEDLINE]

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3: Semin Cancer Biol. 1993 Oct;4(5):311-7.


Differential expression of the 67 kDa laminin receptor in cancer.

Sobel ME.

Molecular Pathology Section, National Cancer Institute, Bethesda, MD 20892.

During tumor invasion and metastasis, cancer cells interact with host tissues. Penetration of the extracellular matrix by cancer cells is mediated in part by interaction of cell surface receptors with laminin, the major glycoprotein component of the basement membrane. A variety of cell surface laminin binding proteins have been identified, including members of both the integrin and non-integrin families. The 67 kDa laminin receptor is a non-integrin protein with a high affinity for laminin. Immunohistochemical, immunoblot, RNA blot and in situ hybridization studies have demonstrated that levels of 67 kDa laminin receptor protein and/or mRNA are increased in a variety of human adenocarcinomas. In contrast, cancers of squamous cell origin may not demonstrate the same pattern of laminin receptor expression.

Publication Types:
Review

PMID: 8257781 [PubMed - indexed for MEDLINE]

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4: J Cell Sci Suppl. 1991;15:9-12.


The expression and distribution of laminin in the developing nervous system.

Edgar D.

Department of Human Anatomy and Cell Biology, University of Liverpool, England.

The extracellular matrix glycoprotein laminin exerts profound effects on the survival and differentiation of neurons in vitro. Although principally confined to the basement membranes of the adult extracellular matrix, during development laminin immunoreactivity may be found both within the interstitial extracellular matrix and on the membranes of neural cells, in which location it may be expected to affect their development in vivo. To investigate the reasons for the occurrence of laminin outside basement membranes, the expression of genes coding for laminin subunits has been analysed in mouse sciatic nerves at different postnatal ages. The results show that the expression of genes coding for laminin subunits decreases from high levels at birth, very low steady state levels of the individual mRNAs being found in the adult. Thus, the predicted high rate of laminin synthesis during development might exceed the rate at which it may be incorporated into basement membranes. The effective change in distribution of laminin into the basement membrane is therefore likely to be simply a consequence of the down-regulation of gene expression, rather than being caused, for example, by the differential expression of laminin variants.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1824111 [PubMed - indexed for MEDLINE]

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5: Cell Differ Dev. 1990 Dec 2;32(3):377-81.


The expression and interactions of laminin in the developing nervous system.

Edgar D.

Department of Human Anatomy and Cell Biology, University of Liverpool, U.K.

Publication Types:
Research Support, Non-U.S. Gov't
Review

PMID: 1983074 [PubMed - indexed for MEDLINE]

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6: Tanpakushitsu Kakusan Koso. 1987 May;32(5):397-410.


[Laminin B1 chain; its structure and gene expression]

[Article in Japanese]

Kohno K, Sasaki M, Kato S, Yamada Y.

Publication Types:
Review

PMID: 3303142 [PubMed - indexed for MEDLINE]
 

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