Identification of a set of genes expressed during the G0/G1 transition of cultured mouse cells.

Lau, Lester F.; Nathans, Daniel

doi:10.1002/j.1460-2075.1985.tb04057.x

Cited by 581 publications

(363 citation statements)

References 47 publications

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“…We therefore postulated that ATRA stimulation of pgrn mRNA expression would not be mediated through direct actions on the GRN promoter but would be a secondary action of ATRA requiring intermediate gene induction and de novo protein synthesis. This was investigated using CHX, a protein synthesis inhibitor (32). In ATRA-stimulated HL-60 cells, CHX suppressed the upregulation of the pgrn transcript, whereas CHX on its own had no effects (Fig.…”

Section: Resultsmentioning

confidence: 99%

Regulation of progranulin expression in myeloid cells

Ong

He²,

Kriazhev³

et al. 2006

American Journal of Physiology-Regulatory, Integrative and Comp

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Progranulin (pgrn; granulin-epithelin precursor, PC-cell-derived growth factor, or acrogranin) is a multifunctional secreted glycoprotein implicated in tumorigenesis, development, inflammation, and repair. It is highly expressed in macrophage and monocyte-derived dendritic cells. Here we investigate its regulation in myeloid cells. All-trans retinoic acid (ATRA) increased pgrn mRNA levels in myelomonocytic cells (CD34 ϩ progenitors; monoblastic U-937; monocytic THP-1; progranulocytic HL-60; macrophage RAW 264.7) but not in nonmyeloid cells tested. Interleukin-4 impaired basal expression of pgrn in U-937. Differentiation agents DMSO, and, in U-937 only, phorbol ester [phorbol 12-myristate,13-acetate (PMA)] elevated pgrn mRNA expression late in differentiation, suggestive of roles for pgrn in more mature terminally differentiated granulocyte/monocytes rather than during growth or differentiation. The response of pgrn mRNA to ATRA differs in U-937 and HL-60 lineages. In U-937, ATRA and chemical differentiation agents greatly increased pgrn mRNA stability, whereas, in HL-60, ATRA accelerated pgrn mRNA turnover. The initial upregulation of pgrn mRNA after stimulation with ATRA was independent of de novo protein synthesis in U-937 but not HL-60. Chemical blockade of nuclear factor-B (NF-B) activation impaired ATRAstimulated pgrn expression in HL-60 but not U-937, whereas in U-937 it blocked PMA-induced pgrn mRNA expression, suggestive of cellspecific roles for NF-B in determining pgrn mRNA levels. We propose that: 1) ATRA regulates pgrn mRNA levels in myelomonocytic cells; 2) ATRA acts in a cell-specific manner involving the differential control of mRNA stability and differential requirement for NF-B signaling; and 3) elevated pgrn mRNA expression is characteristic of more mature cells and does not stimulate differentiation.granulin; stem cell factor; colony-stimulating factor THE GRANULIN-EPITHELIN precursor progranulin (pgrn; see Ref. 4), which is also called proepithelin (47), PC-cell-derived growth factor (66), or acrogranin (1), is a multifunctional regulatory protein that promotes mitosis, survival, and migration in many cell types (43). It stimulates growth factor-related signaling pathways such as the phosphorylation of shc, p44/42 mitogen-activated protein kinase, phosphatidylinositol 3-kinase, protein kinase B/AKT, and the p70 S6 kinase (24,35,65) and contributes to carcinogenesis in breast (51), ovarian (16,26), renal (18), hepatocellular (10), and prostate (44) cancers, gliomas (33), and multiple myelomas (63). Physiologically, pgrn is involved in wound repair (25,67) and is expressed during development (8) where it regulates cavitation in preimplantation embryos (17), blastocyst hatching (48), and malespecific differentiation of the neonatal hypothalamus (56,58).The granulin (GRN) gene is highly expressed in monocytederived cells, being the 17th and 30th most abundant transcript in human macrophage (9) and monocyte-derived dendritic cells (21), respectively. Peptides derived from pgrn, the granulin/ epit...

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Section: Resultsmentioning

confidence: 99%

Regulation of progranulin expression in myeloid cells

Ong

He²,

Kriazhev³

et al. 2006

American Journal of Physiology-Regulatory, Integrative and Comp

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“…Consistent with this notion, several recent investigations have shown that MAP kinase specific phosphatase-1 (MKP-1) deficiency results in enhanced and prolonged p38 and JNK activation (Nimah et al, 2005;Wu and Bennett, 2005;Zhao et al, 2005). MKPs were initially identified as early response genes (Lau and Nathans, 1985;Sun et al, 1993) and are expressed ubiquitously in response to growth factors, stress, or heat shock (Farooq and Zhou, 2004;Chi et al, 2006;Hammer et al, 2006). They are known to play a regulatory role in the production of pro-or anti-inflammatory cytokines following stimulation with LPS, peptidoglycan, or dexamethasone (Hammer et al, 2005;Chi et al, 2006).…”

Section: Introductionmentioning

confidence: 81%

Astragali Radix elicits anti-inflammation via activation of MKP-1, concomitant with attenuation of p38 and Erk

Ryu

Kim

Chun

et al. 2008

Journal of Ethnopharmacology

149

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“…The matching expression and binding pattern suggest that WISP-1 interacts with the surface of its expressing cells. Other members of the CCN family including WISP-2, CTGF, and Cyr61 are also expressed by fibroblasts (4,26,27). Moreover, CTGF and Cyr61 remain associated with the extracellular matrix and the cell surface upon secretion (26,28,29).…”

Section: Wisp-1 Binds To Decorin At the Surface Of Human Skinmentioning

confidence: 99%

WISP-1 Binds to Decorin and Biglycan

Desnoyers¹,

Arnott²,

Pennica³

2001

Journal of Biological Chemistry

109

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Wnt-1-induced secreted protein 1 (WISP-1) is a member of the CCN (connective tissue growth factor, Cyr61, NOV) family of growth factors. Structural and experimental evidence suggests that CCN family member activities are modulated by their interaction with sulfated glycoconjugates. To elucidate the mechanism of action for WISP-1, we characterized the specificity of its tissue and cellular interaction and identified binding factors. WISP-1 binding was restricted to the stroma of colon tumors and to cells with a fibroblastic phenotype. By using a solid phase assay, we showed that human skin fibroblast conditioned media contained WISP-1 binding factors. Competitive inhibition with different glycosaminoglycans and treatment with glycosaminoglycan lyases and proteases demonstrated that binding to the conditioned media was mediated by dermatan sulfate proteoglycans. Mass spectrometric analysis identified the isolated binding factors as decorin and biglycan. Decorin and biglycan interacted directly with WISP-1 and inhibited its binding to components in the conditioned media. Similarly, WISP-1 interaction with human skin fibroblasts was inhibited by dermatan sulfate, decorin, and biglycan or by treatment of the cell surface with dermatan sulfate-specific lyases. Together these results demonstrate that decorin and biglycan are WISP-1 binding factors that can mediate and modulate its interaction with the surface of fibroblasts. We propose that this specific interaction plays a role in the regulation of WISP-1 function.

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Identification of a set of genes expressed during the G0/G1 transition of cultured mouse cells.

Cited by 581 publications

References 47 publications

Regulation of progranulin expression in myeloid cells

Regulation of progranulin expression in myeloid cells

Astragali Radix elicits anti-inflammation via activation of MKP-1, concomitant with attenuation of p38 and Erk

WISP-1 Binds to Decorin and Biglycan

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