Laminin-Induced Signaling in Tumor Cells

Givant-Horwitz, Vered; Davidson, Ben; Reich, Reuven

doi:10.1158/0008-5472.can-03-3424

Cited by 172 publications

(139 citation statements)

References 55 publications

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“…The 67LR protein is a cellular receptor for cell adhesive protein laminin and a 37 kDa protein is the precursor of the receptor, although the exact manner by which it configures its mature form is not clear (4). Previous studies have shown that the cell sur- HL-60 cells similar to that of normal monocytic cells (1).…”

Section: Expression Of 67lrmentioning

confidence: 99%

Differentiation-associated alteration in sensitivity to apoptosis induced by (-)-epigallocatechin-3-O-gallate in HL-60 cells

et al. 2009

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Section: Expression Of 67lrmentioning

confidence: 99%

Differentiation-associated alteration in sensitivity to apoptosis induced by (-)-epigallocatechin-3-O-gallate in HL-60 cells

et al. 2009

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“…During tumor invasion and metastasis, cancer cells are known to interact with laminin. For instance, a nonintegrin receptor known as M r 67-kDa laminin receptor, which can interact with ␣6-integrin, has been shown to induce laminin signaling in tumor cells through mitogen-activated protein kinases cascades (52,53). This 67-kDa laminin receptor has high affinity toward laminin through the binding site of peptide G (54).…”

Section: Laminin-333⅐␣6␤1-integrin Is a Putative Adhesion Protein Commentioning

confidence: 99%

Laminin α 3 Forms a Complex with β3 and γ3 Chains That Serves as the Ligand for α 6β1-Integrin at the Apical Ectoplasmic Specialization in Adult Rat Testes

Yan¹,

Cheng

2006

Journal of Biological Chemistry

129

139

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Apical ectoplasmic specialization (ES) is a testis-specific hybrid cell/cell actin-based adherens junction and cell/matrix focal contact anchoring junction type restricted to the interface between Sertoli cells and developing spermatids. Recent studies have shown that laminin ␥3, restricted to elongating spermatids, is a putative binding partner of ␣6␤1-integrin localized in Sertoli cells at the apical ES. However, the identity of the ␣ and ␤ chains, which constitute a functional laminin ligand with the ␥3 chain at the apical ES, is not known. Using reverse transcription-PCR and immunoblotting to survey all laminin chains in cells of the seminiferous epithelium, it was noted that ␣2, ␣3, ␤1, ␤2, ␤3, and ␥3 chains were found in germ cells, whereas ␣1, ␣2, ␣4, ␣5, ␤1, ␤2, ␥1, ␥2, and ␥3 chains were found in Sertoli cells, implying that ␣3 and ␤3 are the plausible laminin chains restricted to germ cells that may be the bona fide partners of ␥3. To verify this postulate, recombinant proteins based on domain G of ␣3 and domain I of ␤3 and ␥3 chains were produced and used to obtain the corresponding specific polyclonal antibodies. Additional studies have demonstrated that the laminin ␣3, ␤3, and ␥3 chains indeed are restricted to germ cells at the apical ES, co-localizing with each other and with ␤1-integrin. Furthermore, co-immunoprecipitation studies have confirmed the interactions among laminin ␣3, ␤3, and ␥3, as well as ␤1-integrin. When the functional laminin ligand at the apical ES was disrupted via blocking antibodies, such as using anti-laminin ␣3 or ␥3 IgG, this treatment perturbed adhesion between Sertoli and germ cells (mostly spermatids), leading to germ cell loss from the epithelium. More important, a transient disruption of the bloodtestis barrier was also detected.During spermatogenesis, preleptotene spermatocytes residing at the basal compartment of the seminiferous tubules must traverse the BTB 3 to the apical compartment at late stage VII through early stage VIII of the epithelial cycle in adult rat testes (1). Once in the adluminal compartment, spermatocytes differentiate into round spermatids, and the elongating/elongate spermatids orientate themselves with heads and tails pointing toward the basal lamina and the tubule lumen, respectively. The primary anchoring device that facilitates this process of orientation, while maintaining adhesion at the Sertoli cell/spermatid interface, is the apical ectoplasmic specialization (ES), a cell/cell actin-based adherens junction (AJ) type (2-4). In recent years, numerous reports have been published identifying the adhesion molecules at the apical ES. These include the cadherin⅐catenin, nectin⅐afadin, and integrin⅐laminin protein complexes (5-10), which are the primary adhesion protein complexes at the Sertoli cell/developing spermatid interface. Interestingly, in virtually all other epithelia, the integrin⅐laminin complex is usually restricted to the basement membrane at the cell/matrix interface (11,12). Yet studies have shown that integrin is a crucial adhe...

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“…In particular, human TSP1 shows the highest identity (22%) with the corresponding region of hNELL1. The laminin G domain serves in the interaction with integrins and a 67-kDa laminin receptor [26]. Mutational analyses of TSP1 and TSP2 have demonstrated that a Glu residue (Glu-90) between b-strands D and E is important for the interaction with integrin a6b1, which is conserved in the similar positions of hNELL1 [22] (Fig.…”

Section: Putative Nell1 Receptormentioning

confidence: 99%

Involvement of MAPK signaling molecules and Runx2 in the NELL1‐induced osteoblastic differentiation

Bokui

Otani²,

Igarashi³

et al. 2007

FEBS Letters

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NELL1 is an extracellular protein inducing osteogenic differentiation and bone formation of osteoblastic cells. To elucidate the intracellular signaling cascade evoked by NELL1, we have shown that NELL1 protein transiently activates the MAPK signaling cascade, induces the phosphorylation of Runx2, and promotes the rapid intracellular accumulation of Tyr-phosphorylated proteins. Unlike BMP2, NELL1 protein does not activate the Smad signaling cascade. These findings suggest that upon binding to a specific receptor NELL1 transduces an osteogenic signal through activation of certain Tyrkinases associated with the Ras-MAPK cascade, and finally leads to the osteogenic differentiation.

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Laminin-Induced Signaling in Tumor Cells

Cited by 172 publications

References 55 publications

Differentiation-associated alteration in sensitivity to apoptosis induced by (-)-epigallocatechin-3-O-gallate in HL-60 cells

Differentiation-associated alteration in sensitivity to apoptosis induced by (-)-epigallocatechin-3-O-gallate in HL-60 cells

Laminin α 3 Forms a Complex with β3 and γ3 Chains That Serves as the Ligand for α 6β1-Integrin at the Apical Ectoplasmic Specialization in Adult Rat Testes

Involvement of MAPK signaling molecules and Runx2 in the NELL1‐induced osteoblastic differentiation

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