Phorbol ester stimulates the activity of a protein tyrosine phosphatase containing SH2 domains (PTP1C) in HL-60 leukemia cells by increasing gene expression

Uchida, Tsuyoshi; Matozaki, Takashi; Matsuda, Kohei; Suzuki, Toshiya; Matozaki, Sachiko; Nakano, Osamu; Wada, Keinoshin; Konda, Yoshitaka; Sakamoto, Choitsu; Kasuga, Masato

doi:10.1016/s0021-9258(19)50277-0

Cited by 49 publications

(8 citation statements)

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“…We have not determined if the effects of elevating SHP-1 in the Burkitt lymphoma reflects decreased catabolism of mIgM or its increased biosynthesis, although the 24-h delay in mIgM expression, relative to induced SHP-1, would be consistent with enhanced synthesis. That SHP-1 levels may vary with stages of cellular differentiation has also been shown in studies finding that PMA induction of HL-60 cells to a more macrophage-like phenotype was accompanied by a two-to threefold increase in the concentration of the PTPase (51,52). However, our study is the first to demonstrate a reversible downregulation of SHP-1 expression coincident with a specific phase of cellular differentiation.…”

Section: Discussionsupporting

confidence: 86%

Downregulated Expression of SHP-1 in Burkitt Lymphomas and Germinal Center B Lymphocytes

Delibrias

Floettmann

Rowe

et al. 1997

The Journal of Experimental Medicine

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We wish to identify developmental changes in germinal center B cells that may contribute to their rapid growth. SHP-1 is an SH2 domain–containing phosphotyrosine phosphatase that negatively regulates activation of B cells and other cells of hematopoietic lineages. We have found that in all 13 EBV-negative and 11 EBV-positive Burkitt lymphomas with a nonlymphoblastoid phenotype, the mean concentration of SHP-1 was reduced to 5% of that of normal B and T cells. The possibility that this diminished expression of SHP-1 was related to the germinal center phenotype of Burkitt lymphomas was supported by the low to absent immunofluorescent staining for SHP-1 in germinal centers, and by the inverse relationship between the concentration of SHP-1 and the expression of the germinal center marker CD38 on purified tonsillar B cells. In CD38-high B cells, SHP-1 concentration was 20% of that of mantle zone B cells from the same donor. This reduction in SHP-1 is comparable to that of cells from motheaten viable mev/mev mice in which there is dysregulated, spontaneous signaling by cytokine and antigen receptors. Therefore, germinal center B cells may have a developmentally regulated, low threshold for cellular activation.

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Section: Discussionsupporting

confidence: 86%

Downregulated Expression of SHP-1 in Burkitt Lymphomas and Germinal Center B Lymphocytes

Delibrias

Floettmann

Rowe

et al. 1997

The Journal of Experimental Medicine

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“…3 B) and in the C57BL/6J bone marrow macrophages studied by Shultz et al . (19), as well as recent data on PTP1C expression in human tumor cell lines (27), raise the possibility that PTPIC isoforms may be differentially expressed in various cell types and possibly among different inbred strains.…”

Section: Resultsmentioning

confidence: 96%

Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice.

Kozlowski

Mlinarič-Raščan

Feng

et al. 1993

The Journal of Experimental Medicine

232

142

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SummaryMutations in the gene encoding the phosphotyrosine phosphatase PTP1C, a cytoplasmic protein containing a C0014-terminal catalytic and two NH2-terminal Src homology 2 (SH2) domains, have been identified in motheaten (me) and viable motheaten (me) mice and are associated with severe hemopoietic dysregulation. The me mutation is predicted to result in termination of the PTP1C polypeptide within the first SH2 domain, whereas the me°mutation creates an insertion or deletion in the phosphatase domain. No PTPIC RNA or protein could be detected in the hemopoietic tissues ofme mice, nor could PTP1C phosphotyrosine phosphatase activity be isolated from cells homozygous for the me mutation. In contrast, mice homozygous for the less severe me mutation expressed levels of full-length PTP1C protein comparable to those detected in wild type mice and the SH2 domains of me°PTPIC bound normally to phosphotyrosine-containing ligands in vitro . Nevertheless, the me mutation induced a marked reduction in PTPIC activity. These observations provide strong evidence that the motheaten phenotypic results from loss-offunction mutations in the PTP1C gene and imply a critical role for PTP1C in the regulation of hemopoietic differentiation and immune function.

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“…The glucocorticoid dexamethasone inhibits proliferation of rat pancreatic tumor acinar cells and selectively increases SHP-1 expression and activity by severalfold (Cambillau et al, 1995). Phorbol esters inhibit the proliferation in human leukemia cells and stimulate expression and activity of SHP-1 (Uchida et al, 1993;Zhao et al, 1994).…”

Section: Shp-1 and Cell Divisionmentioning

confidence: 99%

Tyrosine phosphatase SHP-1 immunoreactivity increases in a subset of astrocytes following deafferentation of the chicken auditory brainstem

et al. 2000

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Proliferation of astrocytes is a dramatic response of the central nervous system (CNS) to injury and disease. Such proliferation results in the formation of the neural/glial scar and the reconstitution of the glial limitans. However, not all astrocytes enter the proliferative cycle following injury, and for those that do, the period of cell division is limited. Little attention has focused on the events that regulate the duration and extent of astrocyte proliferation following damage, but clearly control mechanisms are in place as CNS injury does not result in the continuous astrocyte proliferation seen in glial tumorigenesis. Protein tyrosine phosphorylation has been implicated in both astrocyte proliferation and differentiation and plays an important role in the regulation of the cell cycle in a number of different systems. We have found a small subset of astrocytes in the chick auditory brainstem that are immunopositive for the protein tyrosine phosphatase SHP‐1. SHP‐1 appears to negatively regulate cellular division in the hematopoietic system and is involved in the mitogenic response to various growth factors. Following cochlea removal, there is a marked increase within the auditory brainstem nucleus, nucleus magnocellularis (NM), in both in the number of SHP‐1‐positive astrocytes and the length of their immunopositive fibers. Significantly, those animals showing the greatest increases in SHP‐1 immunoreactivity do not exhibit large amounts of astrocyte proliferation. We hypothesize that the expression of SHP‐1 plays a role in negatively regulating the mitotic behavior of astrocytes following deafferentation. J. Comp. Neurol. 421:199–214, 2000. © 2000 Wiley‐Liss, Inc.

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Phorbol ester stimulates the activity of a protein tyrosine phosphatase containing SH2 domains (PTP1C) in HL-60 leukemia cells by increasing gene expression

Cited by 49 publications

References 0 publications

Downregulated Expression of SHP-1 in Burkitt Lymphomas and Germinal Center B Lymphocytes

Downregulated Expression of SHP-1 in Burkitt Lymphomas and Germinal Center B Lymphocytes

Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice.

Tyrosine phosphatase SHP-1 immunoreactivity increases in a subset of astrocytes following deafferentation of the chicken auditory brainstem

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