Laminin receptor ?6?4 integrin is highly expressed in ENU-induced glioma in rat

Previtali, Stefano C.; Quattrini, Angelo; Pardini, Celia; Nemni, Raffaello; Feltri, M. Laura; Boncinelli, Edoardo; Canal, N.; Wrabetz, Lawrence

doi:10.1002/(sici)1098-1136(199903)26:1<55::aid-glia6>3.0.co;2-1

Cited by 7 publications

(3 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…cDNAs were amplified by PCR, ligated into pBluescript SKII (Stratagene, La Jolla, CA), and sequenced. Generation of RNA probes and in situ hybridization was performed as described (Previtali et al, 1999).…”

Section: Mice and Genotypingmentioning

confidence: 99%

Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Previtali¹,

Nodari²,

Taveggia³

et al. 2003

J. Neurosci.

Self Cite

119

View full text Add to dashboard Cite

Schwann cells require laminin-2 throughout nerve development, because mutations in the alpha2 chain in dystrophic mice interfere with sorting of axons before birth and formation of myelin internodes after birth. Mature Schwann cells express several laminin receptors, but their expression and roles in development are poorly understood. Therefore, we correlated the onset of myelination in nerve and synchronized myelinating cultures to the appearance of integrins and dystroglycan in Schwann cells. Only alpha6beta1 integrin is expressed before birth, whereas dystroglycan and alpha6beta4 integrin appear perinatally, just before myelination. Although dystroglycan is immediately polarized to the outer surface of Schwann cells, alpha6beta4 appears polarized only after myelination. We showed previously that Schwann cells lacking beta1 integrin do not relate properly to axons before birth. Here we show that the absence of beta1 before birth is not compensated by other laminin receptors, whereas coexpression of both dystroglycan and beta4 integrin is likely required for beta1-null Schwann cells to myelinate after birth. Finally, both beta1-null and dystrophic nerves contain bundles of unsorted axons, but they are predominant in different regions: in spinal roots in dystrophic mice and in nerves in beta1-null mice. We show that differential compensation by laminin-1, but not laminin receptors may partially explain this. These data suggest that the action of laminin is mediated by beta1 integrins during axonal sorting and by dystroglycan, alpha6beta1, and alpha6beta4 integrins during myelination.

show abstract

Section: Mice and Genotypingmentioning

confidence: 99%

Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Previtali¹,

Nodari²,

Taveggia³

et al. 2003

J. Neurosci.

Self Cite

119

View full text Add to dashboard Cite

show abstract

“…Like the oligodendrocytes, the astroglial cells in the brain express primarily ␣6␤1. However, tumors and cell lines derived from transformed astroglial cells express high levels of ␣6␤4 suggesting that ␣6␤4 plays a role in cell proliferation and metastasis in gliomas (Paulus et al, 1994;Previtali et al, 1996Previtali et al, , 1999. In support of a role for ␣6 integrins in the development and organization of the central nervous system, the genetic disruption of ␣6 integrins in mice causes defects in cortical and retinal lamination, suggesting general defects in the proliferation of neural precursors as well as in the organization of the central nervous system (Georges-Labouesse et al, 1998).…”

Section: Laminin-binding Integrins In Thementioning

confidence: 99%

Integrins as receptors for laminins

Belkin

Stepp

2000

Microsc. Res. Tech.

329

212

View full text Add to dashboard Cite

Laminins are a family of trimeric glycoproteins present in the extracellular matrix and the major constituents of basement membranes. Integrins are αβ transmembrane receptors that play critical roles in both cell‐matrix and cell‐cell adhesion. Several members of the integrin family, including α1β1, α2β1, α3β1, α6β1 , α7β1 and α6β4 heterodimers serve as laminin receptors on a variety of cell types. This review summarizes recent advances in understanding the involvement of individual integrins in cell interactions with laminins and the roles of laminin‐binding integrins in adhesion‐mediated events in vertebrates, including embryonic development, cell migration and tumor cell invasiveness, cell proliferation and differentiation, as well as basement membrane assembly. We discuss the regulation of integrin function via alternative splicing of cytoplasmic domains of α and β subunits of the integrin receptors for laminins and present examples of functional collaboration between laminin‐binding integrins and non‐integrin laminin receptors. Advances in our understanding of the laminin‐binding integrins continue to demonstrate the essential roles these receptors play in maintaining cell polarity and tissue architecture. Microsc. Res. Tech. 51:280–301, 2000. © 2000 Wiley‐Liss, Inc.

show abstract

“…These transmembrane receptors not only play a role in the adhesion of cells with the extracellular matrix but are also involved in processes such as the regulation of induced cell death, intracellular transport mechanisms, or migration in conjunction with growth factors [ 73 ]. For over 20 years, it is known that α6β4 integrin has significantly increased in human astrocytomas [ 74 ]. Recently, it was reported that in the presence of 1p/19q deletion and IDH1-mut, the expression of integrin beta-1 (ITGB1) was reduced compared to IDH1-mut, but a knockdown of α6β4 integrin in 1p/19q intact glioma cells (in vitro) and patient-derived glioma cells led to a decreased glioma development [ 75 ] (Fig.…”

Section: Molecular Signatures and Interactions With Tmementioning

confidence: 99%

Glioma: molecular signature and crossroads with tumor microenvironment

Barthel¹,

Hadamitzky²,

Dammann³

et al. 2021

Cancer Metastasis Rev

View full text Add to dashboard Cite

In patients with glioblastoma, the average survival time with current treatments is short, mainly due to recurrences and resistance to therapy. This insufficient treatment success is, in large parts, due to the tremendous molecular heterogeneity of gliomas, which affects the overall prognosis and response to therapies and plays a vital role in gliomas’ grading. In addition, the tumor microenvironment is a major player for glioma development and resistance to therapy. Active communication between glioma cells and local or neighboring healthy cells and the immune environment promotes the cancerogenic processes and contributes to establishing glioma stem cells, which drives therapy resistance. Besides genetic alterations in the primary tumor, tumor-released factors, cytokines, proteins, extracellular vesicles, and environmental influences like hypoxia provide tumor cells the ability to evade host tumor surveillance machinery and promote disease progression. Moreover, there is increasing evidence that these players affect the molecular biological properties of gliomas and enable inter-cell communication that supports pro-cancerogenic cell properties. Identifying and characterizing these complex mechanisms are inevitably necessary to adapt therapeutic strategies and to develop novel measures. Here we provide an update about these junctions where constant traffic of biomolecules adds complexity in the management of glioblastoma. Graphical abstract

show abstract

Laminin receptor ?6?4 integrin is highly expressed in ENU-induced glioma in rat

Cited by 7 publications

References 54 publications

Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Integrins as receptors for laminins

Glioma: molecular signature and crossroads with tumor microenvironment

Contact Info

Product

Resources

About