Prognostic Significance of the 67-Kilodalton Laminin Receptor Expression in Human Breast Carcinomas

Martignone, Stefania; Ménard, Sylvie; Bufalino, Rosaria; Cascinelli, Natale; Pellegrini, Rita; Tagliabue, Elda; Andreola, Salvatore; Rilke, F; Colnaghi, Maria I.

doi:10.1093/jnci/85.5.398

Cited by 129 publications

(84 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In fact, like ST3, LR is particularly abundant in cancers [22,42,43] and there is a strong correlation between LR overexpression and the metastatic property of tumor cells [44,45]. Furthermore, our result here shows that human LR is also a substrate for ST3.…”

Section: Discussionsupporting

confidence: 58%

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Amano

Kwak

et al. 2005

Cell Res

View full text Add to dashboard Cite

The matrix metalloproteinase (MMP) stromelysin-3 (ST3) has long been implicated to play an important role in extracellular matrix (ECM) remodeling and cell fate determination during normal and pathological processes. However, like other MMPs, the molecular basis of ST3 function in vivo remains unclear due to the lack of information on its physiological substrates. Furthermore, ST3 has only weak activities toward all tested ECM proteins. Using thyroid hormone-dependent Xenopus laevis metamorphosis as a model, we demonstrated previously that ST3 is important for apoptosis and tissue morphogenesis during intestinal remodeling. Here, we used yeast two-hybrid screen with mRNAs from metamorphosing tadpoles to identify potential substrate of ST3 during development. We thus isolated the 37 kd laminin receptor precursor (LR). We showed that LR binds to ST3 in vitro and can be cleaved by ST3 at two sites, distinct from where other MMPs cleave. Through peptide sequencing, we determined that the two cleavage sites are in the extracellular domain between the transmembrane domain and laminin binding sequence. Furthermore, we demonstrated that these cleavage sites are conserved in human LR. These results together with high levels of human LR and ST3 expression in carcinomas suggest that LR is a likely in vivo substrate of ST3 and that its cleavage by ST3 may alter cell-extracellular matrix interaction, thus, playing a role in mediating the effects of ST3 on cell fate and behavior observed during development and pathogenesis.

show abstract

Section: Discussionsupporting

confidence: 58%

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Amano

Kwak

et al. 2005

Cell Res

View full text Add to dashboard Cite

show abstract

“…34,35 Alterations in uS2 (37LRP) expression are associated with tumor invasion and metastasis. [36][37][38] In addition, this protein was shown to function as a receptor for the pathogenic prion protein PrP Sc 35 and to control the entry of different viruses (such as Sindbis virus) into mammalian cells. 35,39 Involvement of eukaryote-specific extensions of conserved ribosomal proteins in eIF3-40S interactions One of the largest, key and unique factors involved in eukaryotic translation initiation is eIF3.…”

Section: E999576-4mentioning

confidence: 99%

Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function

Ghosh

Komar

2015

Translation

View full text Add to dashboard Cite

Keywords: conserved ribosomal proteins, eukaryotic/yeast ribosome, eukaryote-specific extensions, eukaryotic translation initiation factors, protein synthesis, small ribosomal subunitHigh-resolution structures of yeast ribosomes have improved our understanding of the architecture and organization of eukaryotic rRNA and proteins, as well as eukaryote-specific extensions present in some conserved ribosomal proteins. Despite this progress, assignment of specific functions to individual proteins and/or eukaryotespecific protein extensions remains challenging. It has been suggested that eukaryote-specific extensions of conserved proteins from the small ribosomal subunit may facilitate eukaryote-specific reactions in the initiation phase of protein synthesis. This review summarizes emerging data describing the structural and functional significance of eukaryotespecific extensions of conserved small ribosomal subunit proteins, particularly their possible roles in recruitment and spatial organization of eukaryote-specific initiation factors.

show abstract

“…However, tumor cells can unmask adhesion molecule sites that are usually embedded within the matrix through overexpressed molecules in addition to ECM degradation. We demonstrated that the 67-kDa monomeric laminin receptor (67LR), which is overexpressed (Martignone et al, 1993;Ménard et al, 1998) and released by various tumor cell types (Karpatová et al, 1996;Starkey et al, 1999), changes the conformation of the laminin adhesion molecule upon binding to it . Because the integrin recognition domains of laminin appear to be conformation-dependent (Mercurio, 1995), 67LR-modified laminin interacts more readily with integrins and with other molecules that normally do not participate significantly in laminin binding to the cell surface (Ramos et al, 1990;Feldman et al, 1991;Kleinman et al, 1991;Magnifico et al, 1996).…”

Section: Unmasking Of Cryptic Sitesmentioning

confidence: 99%

New insights into the role of extracellular matrix during tumor onset and progression

Pupa

Ménard

Forti

et al. 2002

Journal Cellular Physiology

297

206

View full text Add to dashboard Cite

Recently, a view of the tumor as a functional tissue interconnected with the microenvironment has recently been described. For many years, the stroma has been studied in the context of the malignant lesion, and only rarely has its role been considered before carcinogenic lesions appear. Recent studies have provided evidence that stromal cells and their products can cause the transformation of adjacent cells through transient signaling that leads to the disruption of homeostatic regulation, including control of tissue architecture, adhesion, cell death, and proliferation. It is now well established that tumor progression requires a continually evolving network of interactions between neoplastic cells and extracellular matrix. A relevant step of this process is the remodeling of microenvironment which surrounds tumors leading to the release of ECM-associated growth factors which can then stimulate tumor and/or endothelial cells. Finally, tumor cells reorganizing the extracellular matrix to facilitate communications and escape the homeostatic control exerted by the microenvironment modify response to cytotoxic treatments.

show abstract

Prognostic Significance of the 67-Kilodalton Laminin Receptor Expression in Human Breast Carcinomas

Cited by 129 publications

References 0 publications

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain

Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function

New insights into the role of extracellular matrix during tumor onset and progression

Contact Info

Product

Resources

About