The receptor protein tyrosine phosphatase (RPTP)β/ζ is expressed in different subtypes of human breast cancer

Pérez-Piñera, Pablo; García‐Suárez, Olivia; Menéndez-Rodríguez, Primitiva; Mortimer, Joanne; Chang, Yunchao; Astudillo, Aurora; Deuel, Thomas F.

doi:10.1016/j.bbrc.2007.06.050

Cited by 32 publications

(25 citation statements)

References 31 publications

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“…Thus, adipose RAR induces PTHR expression and this leads to increased expression of PTN which in turn regulates mammary epithelial migration. Although, several receptors for PTN have been described, cell migration has been shown to be induced through PTN binding to a protein tyrosine phosphatase receptor ζ1 (also referred to as PTPRβ/ζ) (Ulbricht et al, 2003) with a second receptor ALK, being now considered a downstream substrates for PTPRζ1 (Perez-Pinera et al, 2007). Binding of PTN to PTPRζ1 receptor inactivates the receptor phosphatase activity, causing increased phosphorylation of target proteins.…”

Section: Discussionmentioning

confidence: 99%

Adipocyte derived paracrine mediators of mammary ductal morphogenesis controlled by retinoic acid receptors

Marzan

Kupumbati

Bertran

et al. 2011

Developmental Biology

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We generated a transgenic (Tg)-mouse model expressing a dominant negative-(DN)-RARα, (RARαG303E) under adipocytes-specific promoter to explore the paracrine role of adipocyte retinoic acid receptors (RARs) in mammary morphogenesis. Transgenic adipocytes had reduced level of RARα, β and γ, which coincided with a severely underdeveloped pubertal and mature ductal tree with profoundly decreased epithelial cell proliferation. Transplantation experiments of mammary epithelium and of whole mammary glands implicated a fat-pad dependent paracrine mechanism in the stunted phenotype of the epithelial-ductal tree. Co-cultures of primary adipocytes, or in vitro differentiated adipocyte cell line, with mammary epithelium showed that when activated, adipocyte RARs contribute to generation of secreted proliferative and pro-migratory factors. Gene expression microarrays revealed a large number of genes regulated by adipocyte-RARs. Among them, pleiotrophin (PTN) was identified as the paracrine effectors of epithelial cell migration. Its expression was found to be strongly inhibited by DN-RARα, an inhibition relieved by pharmacological doses of all-trans retinoic acid (atRA) in culture and in vivo. Moreover, adipocyte-PTHR, another atRA responsive gene, was found to be an up-stream regulator of PTN. Overall, these results support the existence of a novel paracrine loop controlled by adipocyte-RAR that regulates the mammary ductal tree morphogenesis.

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Section: Discussionmentioning

confidence: 99%

Adipocyte derived paracrine mediators of mammary ductal morphogenesis controlled by retinoic acid receptors

Marzan

Kupumbati

Bertran

et al. 2011

Developmental Biology

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“…Aberrant expression of the embryonic long receptor form of RPTP␤ in invasive glioblastoma likely contributes to the highly invasive phenotype of this tumor (56). Moreover, this form of RPTP␤ has also been consistently found expressed in different subtypes of human breast cancer, suggesting that its expression, and perhaps glycosylation, may affect the adhesion of non-neural carcinomas (57).…”

Section: Discussionmentioning

confidence: 99%

Receptor Tyrosine Phosphatase β (RPTPβ) Activity and Signaling Are Attenuated by Glycosylation and Subsequent Cell Surface Galectin-1 Binding

Abbott

Matthews

Pierce

2008

Journal of Biological Chemistry

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O-Mannosyl-linked glycosylation is abundant within the central nervous system, yet very few glycoproteins with this glycan modification have been identified. Congenital diseases with significant neurological defects arise from inactivating mutations found within the glycosyltransferases that act early in the O-mannosyl glycosylation pathway. The N-acetylglucosaminyltransferase known as GnT-Vb or -IX is highly expressed in brain and branches O-mannosyl-linked glycans. Our results using SH-SY5Y neuroblastoma cells indicate that GnT-Vb activity promotes the addition of the O-mannosyl-linked HNK-1 modification found on the developmentally regulated and neuronspecific receptor protein-tyrosine phosphatase ␤ (RPTP␤). These changes in glycosylation accompany decreased cell-cell adhesion and increased rates of migration on laminin. In addition, we show that expression of GnT-Vb promotes its dimerization and inhibits RPTP␤ intrinsic phosphatase activity, resulting in higher levels of phosphorylated ␤-catenin, suggesting a mechanism by which GnT-Vb glycosylation couples to changes in cell adhesion. GnT-Vb-mediated glycosylation of RPTP␤ promotes galectin-1 binding and RPTP␤ levels of retention on the cell surface. N-Acetyllactosamine, but not sucrose, treatment of cells results in decreased RPTP retention, showing that galectin-1 binding contributes to the increased retention after GnT-Vb expression. These results place GnT-Vb as a regulator of RPTP␤ signaling that influences cell-cell and cell-matrix interactions in the developing nervous system. Glycosylation is regulated spatially and temporally during the development of the nervous system (1). In particular, sulfated glycoconjugates, such as the human natural killer-1 epitope, are important for proper migration and adhesion during neural development (2, 3). The human natural killer-1 (HNK-1) 3 epitope was originally discovered using a monoclonal antibody raised against a specific T-lymphoblastoid cell type (4). Since its discovery in lymphocytes, the HNK-1 (also known as CD57) antibody has been shown to react with many neural cell types, including glial, neuroectoderm, and neuroendocrine cells (5-8). The HNK-1 epitope consists of a glucuronic acid, transferred by glucuronyltransferases (GlcATs), that is 3-sulfated by HNK-1 sulfotransferase (HNK1st), linked to a precursor N-acetyllactosamine structure (Fig. 1). Numerous glycoproteins bearing the HNK-1 epitope have been identified in the nervous system, such as neural cell adhesion molecule (9), L1 (10), neural-glia cell adhesion molecule (11), myelinassociated glycoprotein (12), tenascin R (13), and RPTP (receptor protein-tyrosine phosphatase) (14, 15). In certain cell types, such as neural crest cells, the expression of the HNK-1 antigen is highly regulated during development (2) and is often found on migratory cells (3). The HNK-1 antigen is linked to critical functions during the formation of the nervous system, such as cell-matrix interactions (16), cell-cell adhesion (17), memory, and synaptic plasticity (15,18,19...

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“…Furthermore, the full-length ALK cDNA was originally cloned from an Rh30 rhabdomyosarcoma cell line cDNA library [5,17,19], and expression of the full-length protein has subsequently been reported to occur in a subset of rhabdomyosarcoma tumors [88-91]. In addition, anti-ALK immunoreactivity has been observed in tissue immunostaining studies of other malignancies, such as breast carcinoma, malignant peripheral nerve-sheath tumors, and lipogenic tumors [70,89,91-93]; in these tumors, however, whether the full-length or rather fusion forms of ALK might be expressed in immuno positive cases has not yet been unequivocally determined (indeed, it has been noted that at least some breast carcinomas appear to exhibit an ALK immunostaining pattern more characteristic of certain ALK fusion proteins than the full-length receptor) [92]. With the exception of neuroblastoma (in which a pathogenic role for full-length ALK expression seems clear, vide infra ), the pathogenic significance – if any – of ALK receptor expression in each of the aforementioned tumor types remains uncertain at this time.…”

Section: Role Of Alk In Cancer Pathogenesismentioning

confidence: 99%

Anaplastic lymphoma kinase: role in cancer pathogenesis and small-molecule inhibitor development for therapy

Webb

Slavish

George

et al. 2009

Expert Review of Anticancer Therapy

211

177

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Anaplastic lymphoma kinase (ALK), a receptor tyrosine kinase in the insulin receptor superfamily, was initially identified in constitutively activated oncogenic fusion forms – the most common being nucleophosmin-ALK – in anaplastic large-cell lymphomas, and subsequent studies have identified ALK fusions in diffuse large B-cell lymphomas, systemic histiocytosis, inflammatory myofibroblastic tumors, esophageal squamous cell carcinomas and non-small-cell lung carcinomas. More recently, genomic DNA amplification and protein overexpression, as well as activating point mutations, of ALK have been described in neuroblastomas. In addition to those cancers for which a causative role for aberrant ALK activity is well validated, more circumstantial links implicate the full-length, normal ALK receptor in the genesis of other malignancies – including glioblastoma and breast cancer – via a mechanism of receptor activation involving autocrine and/or paracrine growth loops with the reported ALK ligands, pleiotrophin and midkine. This review summarizes normal ALK biology, the confirmed and putative roles of ALK in the development of human cancers and efforts to target ALK using small-molecule kinase inhibitors.

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The receptor protein tyrosine phosphatase (RPTP)β/ζ is expressed in different subtypes of human breast cancer

Cited by 32 publications

References 31 publications

Adipocyte derived paracrine mediators of mammary ductal morphogenesis controlled by retinoic acid receptors

Adipocyte derived paracrine mediators of mammary ductal morphogenesis controlled by retinoic acid receptors

Receptor Tyrosine Phosphatase β (RPTPβ) Activity and Signaling Are Attenuated by Glycosylation and Subsequent Cell Surface Galectin-1 Binding

Anaplastic lymphoma kinase: role in cancer pathogenesis and small-molecule inhibitor development for therapy

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