Expression of the membrane protein tyrosine phosphatase CD148 in human tissues

Autschbach, Frank; Palou, Eduard; Mechtersheimer, Gunhild; Rohr, Claudia; Pirotto, F; Gaßler, Nikolaus; Otto, Henning; Schraven, Burkhart; Gayà, Antoni

doi:10.1034/j.1399-0039.1999.540506.x

Cited by 44 publications

(44 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It is composed of an extracellular domain containing eight type III fibronectin repeats, a transmembrane segment, and a single intracellular catalytic domain. DEP-1 is expressed in various cell types including all hematopoietic lineages, endothelial cells, fibroblasts, different epithelial, and smooth muscle cells (Ö stman et al, 1994;Borges et al, 1996;de la Fuente-Garcia et al, 1998;Autschbach et al, 1999;Schraven, 2000). DEP-1 activity is enhanced by an as yet unidentified component of extracellular matrix (So¨rby et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell–matrix adhesion

et al. 2003

View full text Add to dashboard Cite

Density-enhanced protein-tyrosine phosphatase-1 (DEP-1 also CD148) is a transmembrane molecule with a single intracellular PTP domain. It has recently been proposed to function as a tumor suppressor. We have previously shown that DEP-1 dephosphorylates the activated plateletderived growth factor (PDGF) b-receptor in a siteselective manner (Kovalenko et al. (2000). J. Biol. Chem. 275, 16219-16226). We analysed cell lines with inducible DEP-1 expression for cellular functions of DEP-1. Several aspects of PDGFb-receptor signaling were negatively affected by DEP-1 expression. These include PDGFstimulated activation of inositol trisphosphate formation, Erk1/2, p21Ras, and Src. Activation of receptor-associated phosphoinositide-3 kinase activity and of Akt/PKB were weakly attenuated at early time points of stimulation. Inhibition of PDGF-stimulated signaling depended on DEP-1 catalytic activity. Importantly, DEP-1 inhibited PDGF-stimulated cell migration. The catalytically inactive DEP-1 C1239S variant enhanced cell migration and PDGF-stimulated Erk1/2 activation, suggesting a dominant negative interference with endogenous DEP-1. In contrast to cell migration, cell-substrate adhesion was promoted by active DEP-1 and delayed or suppressed by DEP-1 C1239S, correlating with positive effects of DEP-1 on adhesion-stimulated Src kinase. We propose that negative regulation of growth-factor stimulated cell migration and promotion of cell-matrix adhesion may be related to the function of DEP-1 as tumor suppressor.

show abstract

Section: Introductionmentioning

confidence: 99%

The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell–matrix adhesion

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Immunohistochemical stainings have revealed a broad tissue distribution of DEP-1; prominent expression was found in thymus, and also on many epithelial cell types with glandular or endocrine di erentiation (Autschbach et al, 1999). DEP-1 expression is enhanced in high cell density cultures of ®broblasts and in contactinhibited endothelial cells (Borges et al, 1996;O È stman et al, 1994), and heterologous expression of DEP-1 in bovine aortic endothelial cells leads to inhibition of cfos and Cyclin A promotor activity (Suzuki et al, 2000).…”

mentioning

confidence: 99%

“…The expression of DEP-1 in many epithelial cells with glandular di erentiation (Autschbach et al, 1999), which are juxtaposed to extracellular-rich basement membranes suggests that regulated expression of a DEP-1 agonist in extracellular matrix constitutes a biological control mechanism.…”

mentioning

confidence: 99%

An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1

2001

View full text Add to dashboard Cite

Cellular growth, di erentiation and migration is regulated by protein tyrosine phosphorylation. Receptor-like protein tyrosine phosphatases are thus likely to be key regulators of vital cellular processes. The regulation of these enzymes is in general poorly understood. Ligands have been identi®ed only for a small subset of the receptor-like protein tyrosine phosphatases and in no case has upregulation of the speci®c activity by extracellular ligands been demonstrated. Prompted by earlier ®ndings of ligands for receptor-like protein tyrosine phosphatases in extracellular matrix we investigated if Matrigel TM , a preparation of extracellular matrix proteins, contained modulators of the speci®c activity of the receptor-like protein tyrosine phosphatase DEP-1. Matrigel TM stimulation of cells increased the speci®c activity of immunoprecipitated DEP-1. Also, incubation of immunoprecipitated DEP-1 with Matrigel TM led to an increase in DEP-1 activity, which was blocked by soluble DEP-1 extracellular domain. Finally, immunoprecipitated DECD-DEP-1, a mutant form of DEP-1 lacking most of the extracellular domain, failed to respond to Matrigel TM stimulation. These experiments identify Matrigel TM as a source of DEP-1 agonist(s) and provide the ®rst evidence for upregulation of the speci®c activity of receptor-like protein tyrosine phosphatases by extracellular ligands. Oncogene (2001) 20, 5219 ± 5224.

show abstract

“…CD148 (DEP-1, PTPRJ) is an R3 family receptor-like PTP with a large highly N-glycosylated extracellular segment containing multiple fibronectin III-like repeats, a transmembrane domain, and a single intracellular protein-tyrosine phosphatase domain followed by a short C-terminal tail containing three conserved tyrosine residues (1)(2)(3)(4)(5).…”

mentioning

confidence: 99%

“…In peripheral blood, CD148 is expressed on all white blood cell populations, including T cells, and platelets in humans (5)(6)(7)(8). CD148 is further up-regulated on T cells after activation with mitogens (5,6,8). Less is known about CD148 expression on thymocytes.…”

mentioning

confidence: 99%

Regulation of Src Family Kinases Involved in T Cell Receptor Signaling by Protein-tyrosine Phosphatase CD148

Štěpánek

Kalina

Dráber

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

CD148 is a receptor-like protein-tyrosine phosphatase known to inhibit transduction of mitogenic signals in non-hematopoietic cells. Similarly, in the hematopoietic lineage, CD148 inhibited signal transduction downstream of T cell receptor. However, it also augmented immunoreceptor signaling in B cells and macrophages via dephosphorylating C-terminal tyrosine of Src family kinases (SFK). Accordingly, endogenous CD148 compensated for the loss of the main SFK activator CD45 in murine B cells and macrophages but not in T cells. Hypothetical explanations for the difference between T cells and other leukocyte lineages include the inability of CD148 to dephosphorylate a specific set of SFKs involved in T cell activation or the lack of CD148 expression during critical stages of T cell development. Here we describe striking differences in CD148 expression between human and murine thymocyte subsets, the only unifying feature being the absence of CD148 during the positive selection when the major developmental block occurs under CD45 deficiency. Moreover, we demonstrate that similar to CD45, CD148 has both activating and inhibitory effects on the SFKs involved in TCR signaling. However, in the absence of CD45, activating effects prevail, resulting in functional complementation of CD45 deficiency in human T cell lines. Importantly, this is independent of the tyrosines in the CD148 C-terminal tail, contradicting the recently proposed phosphotyrosine displacement model as a mechanism of SFK activation by CD148. Collectively, our data suggest that differential effects of CD148 in T cells and other leukocyte subsets cannot be explained by the CD148 inability to activate T cell SFKs but rather by its dual inhibitory/ activatory function and specific expression pattern.

show abstract

Expression of the membrane protein tyrosine phosphatase CD148 in human tissues

Cited by 44 publications

References 17 publications

The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell–matrix adhesion

The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell–matrix adhesion

An extracellular ligand increases the specific activity of the receptor-like protein tyrosine phosphatase DEP-1

Regulation of Src Family Kinases Involved in T Cell Receptor Signaling by Protein-tyrosine Phosphatase CD148

Contact Info

Product

Resources

About