Fine tuning the transcriptional regulation of the CXCL1 chemokine.
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Prog Nucleic Acid Res Mol Biol 74: 1-36
PMID: 14510072

Fine Tuning the Transcriptional Regulation of the CXCL1 Chemokine

Department of Cancer Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232
Department of Microbiology, Meharry Medical College, Nashville, Tennessee, 37203
Department of Veterans Affairs, Nashville, Tennessee 37232
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Abstract

Constitutive activation of the transcription factor nuclear factor-κB (NF-κB) plays a major role in inflammatory diseases as well as cancer by inducing the endogenous expression of many proinflammatory proteins such as chemokines, and facilitating escape from apoptosis. The constitutive expression of chemokines such as CXCL1 has been correlated with growth, angiogenesis, and metastasis of cancers such as melanoma. The transcription of CXCL1 is regulated through interactions of NF-κB with other transcriptional regulatory molecules such as poly(ADP-ribose) polymerase-1 (PARP-1) and cAMP response element binding protein (CREB)-binding protein (CBP). It has been proposed that these two proteins interact with NF-κB and other enhancers to form an enhanceosome at the promoter region of CXCL1 and modulate CXCL1 transcription. In addition to these positive cofactors, a negative regulator, CAAT displacement protein (CDP), may also be involved in the transcriptional regulation of CXCL1. It has been postulated that the elevated expression of CXCL1 in melanomas is due to altered interaction between these molecules. CDP interaction with the promoter down-regulates transcription, whereas PARP and/or CBP interactions enhance transcription. Thus, elucidation of the interplay between components of the enhanceosome of this gene is important in finding more efficient and new therapies for conditions such as cancer as well as acute and chronic inflammatory diseases.

Abstract

Footnotes

Abbreviations: IL, interleukin; TNF-α, tumor necrosis factor-α; NF-κB, nuclear factor-κB; IFN-γ, interferon-γ; JAK, Janus kinases; STAT, signal tranducer and activator of transcription proteins; TGF-β, transforming growth factor-β; GTP, guanosine triphosphate; GDP, guanosine diphosphate; PLC, phospholipase Cβ2; IP3, inositol 1,4,5-triphosphate; PIP2, phosphatidylinositol 4,5-bisphosphate; PKC, protein kinase C; PI3K, phosphatidylinositol 3-kinase; MAPK, mitogen-activated protein kinases; HIP, Hsp70 interacting protein; ICAM-1, intercellular adhesion molecule-1; VCAM-1, vascular cell adhesion molecule-1; CTAPIII, connective tissue-activating peptide; MS, multiple sclerosis; AP-1, activator protein-1; NF-IL6, nuclear factor activated by interleukin 6; IRF, IFN-regulatory factor; Sp1, stimulating protein-1; HMGI/Y, high mobility group-I/Y; C/EBP, CAAT enhancer binding protein; IUR, immediate upstream region; NRF, NF-κB repressing factor; CBP, cAMP response element binding protein (CREB)-binding protein; HAT, histone acetyltransferase; HDAC, histone deacetylase; CDP, CAAT displacement protein; PARP, poly(ADP-ribose) polymerase; IκB, inhibitor of κB; NLS, nuclear localization signal; IKK, IκB kinase; PKA, protein kinase A; CKII, casein kinase II; PIP3, phosphatidylinositol 3,4,5-trisphosphate; PDK, 3-phosphoinositide-dependent protein kinase; PTEN, phosphatase and tensin homologue deleted on chromosome 10; NIK, NF-κB-inducing kinase; TRAF2, TNF receptor-associated factor 2; ERK1/2, extracellular signal-regulated kinase 1 and 2; Cdk, cyclin-dependent kinases; NAD, β-nicotinamide adenine dinucleotide; BER, base excision repair; HD, Cut homeodomain; CYP7A1, human cholesterol-7 hydroxylase; HNF-1, hepatocyte nuclear factor-1.

Footnotes

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