Chromosomal, in silico and in vitro Expression Analysis of Cardiovascular-based Genes Encoding Zinc Finger Proteins

Dai, Ken-Shwo; Liew, Choong‐Chin

doi:10.1006/jmcc.1999.1011

Cited by 19 publications

(10 citation statements)

References 145 publications

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“…Stimulation of GECs with P. gingivalis also resulted in hypo-methylation of ZNF287, a member of Zinc finger protein family. The up-regulation of Zinc finger proteins has been associated with cardiovascular disease (Dai and Liew 1999), thus this observation is in line with recent studies linking periodontal disease with increased risk of systemic disease (Persson and Persson 2008). GECs exposed to P. gingivalis also showed a decrease in the methylation of STAT5A, which mediates cellular responses to cytokines IL-2, IL-3, IL-7, GM-CSF and plays a role in progression of tumors.…”

Section: Epigenetic Regulation and Its Implication On Periodontal Dissupporting

confidence: 84%

Periodontal Disease and Gingival Innate Immunity – Who Has the Upper Hand?

Chung¹,

An²

2012

Periodontal Diseases - A Clinician's Guide

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Section: Epigenetic Regulation and Its Implication On Periodontal Dissupporting

confidence: 84%

Periodontal Disease and Gingival Innate Immunity – Who Has the Upper Hand?

Chung¹,

An²

2012

Periodontal Diseases - A Clinician's Guide

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“…The ZFPs are a group of proteins involved in a wide spectrum of cellular regulatory functions (13). Since protein-protein interaction plays an important role in cell regulatory networks, identification of novel ZFP genes and characterization of their protein-protein interactions will facilitate our understanding of ZFP cellular regulatory mechanisms.…”

Section: Discussionmentioning

confidence: 99%

“…Combinational diversities among the conserved cysteines and histidines of the domain classifies ZFPs into several types: C 2 H 2 , C 2 C 2, C 2 HC, C 2 HC 4 C(HD), C 3 H, and C 3 HC 4 (3,(5)(6)(7)(8)(9)(10)(11)(12). These ZFP types have been described in a human heart EST data base survey as well as in an in silico Northern analysis of a total of 15 different tissues (13).…”

mentioning

confidence: 99%

A Novel Human Striated Muscle RING Zinc Finger Protein, SMRZ, Interacts with SMT3b via Its RING Domain

Dai¹,

Liew

2001

Journal of Biological Chemistry

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The RING domain is a conserved zinc finger motif, which serves as a protein-protein interaction interface. Searches of a human heart expressed sequence tag data base for genes encoding the RING domain identified a novel cDNA, named striated muscle RING zinc finger protein (SMRZ). The SMRZ cDNA is 1.9 kilobase pairs in length and encodes a polypeptide of 288 amino acid residues; analysis of the peptide sequence demonstrated an N-terminal RING domain. Fluorescence in situ hybridization localized SMRZ to chromosome 1p33-34. Northern blots demonstrated that SMRZ is expressed exclusively in striated muscle. In the cardiovascular system, SMRZ is more highly expressed in the fetal heart than in the adult heart (slightly higher expression in the ventricle than in the atrium), suggesting that SMRZ is developmentally regulated. SMRZ was found to interact with SMT3b, a ubiquitin-like protein, through the SMRZ-RING domain. This interaction was abolished by mutagenesis of conserved RING domain residues. Transient transfection of SMRZ into C2C12 myoblasts showed localization of SMRZ to the nucleus. These data suggest that SMRZ may play an important role in striated muscle cell embryonic development and perhaps in cell cycle regulation.The zinc finger proteins (ZFPs) 1 are a group of proteins containing zinc finger domains. The finger-like structures are formed by the coordination of conserved cysteines (C) and histidines (H) with zinc ions (1-3). The discovery of the zinc finger domain in the Xenopus transcription factor IIIA (4), together with ongoing cDNA sequencing projects, has led to a significant acceleration in the discovery of ZFP genes. Combinational diversities among the conserved cysteines and histidines of the domain classifies ZFPs into several types: C 2 H 2 , C 2 C 2, C 2 HC, C 2 HC 4 C(HD), C 3 H, and C 3 HC 4 (3, 5-12). These ZFP types have been described in a human heart EST data base survey as well as in an in silico Northern analysis of a total of 15 different tissues (13).The C 3 HC 4 -type zinc finger domain, also termed RING domain, was first described in the sequence of the human ring 1 gene (14). This domain was subsequently found in a number of virus, yeast, plant, and animal proteins, which have various functions such as oncogenesis, signal transduction, peroxisome biogenesis, viral infection, development, transcriptional repression, and ubiquitination (15, 16). The widespread presence of the RING domain in functionally distinct proteins and in many different species indicates that the domain is essential to basic cellular function and is conserved during evolution. With the aid of sequence alignment, the consensus sequence of this domain was defined as CX 2 CX (9 -39) CX (1-3) HX (2-3) CX 2 CX (4 -48) CX 2 C, where X can be any amino acid. Unlike other zinc finger domains, this domain shows a unique cross-brace arrangement on the conserved residues that coordinate the two zinc ions (15,16).Accumulated evidence suggests that the RING domain is mainly involved in protein-protein interactions (15,16...

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“…It is characterized by C 2 H 2 zinc finger motifs and has a highly conserved H/C linker (TGE(K/R)P(Y/F)X) [2,3]. The study of zinc finger proteins has revealed their crucial roles in normal and pathological biological processes [4,5]. The ZNF300 gene encodes a typical KRAB-type zinc finger protein with twelve C 2 H 2 zinc finger motifs in the C-terminus [6].…”

Section: Introductionmentioning

confidence: 99%

ZNF300, a recently identified human transcription factor, activates the human IL-2Rβ promoter through the overlapping ZNF300/EGR1 binding site

Lü

Qiu

et al. 2010

Cellular and Molecular Biology Letters

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ZNF300 was recently identified as a member of the human KRAB/C2H2 zinc finger protein family. Little is known about the role of ZNF300 in human gene regulation networks. In this study, the DNA-binding property of ZNF300 was further analyzed. We found that the recombinant ZNF300 could bind to the binding site 5′-GCGGGGGCG-3′ of Egr1, another member of the KRAB/C2H2 zinc finger protein family. Similarly, recombinant Egr1 also showed a similar binding affinity to the ZNF300 binding site 5′-CTGGGGGCG-3′. Bioinformatics analysis revealed that there is an overlapping ZNF300/Egr1 binding site in the human IL-2Rβ promoter region, which was previously known to be recognized by endogenous Egr1. Electrophoretic mobility shift assays showed that endogenous ZNF300 could also bind to this site. A transient transfection assay revealed that both ZNF300 and Egr1 could transactivate the IL-2Rβ promoter, and that the activation was abrogated by a mutation of residues in the overlapping ZNF300/Egr1 binding site. Co-expression of ZNF300 and Egr1 led to enhanced IL-2Rβ promoter activity. Thus, ZNF300 is likely to be another regulator of the human IL-2Rβ promoter.

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Chromosomal, in silico and in vitro Expression Analysis of Cardiovascular-based Genes Encoding Zinc Finger Proteins

Cited by 19 publications

References 145 publications

Periodontal Disease and Gingival Innate Immunity – Who Has the Upper Hand?

Periodontal Disease and Gingival Innate Immunity – Who Has the Upper Hand?

A Novel Human Striated Muscle RING Zinc Finger Protein, SMRZ, Interacts with SMT3b via Its RING Domain

ZNF300, a recently identified human transcription factor, activates the human IL-2Rβ promoter through the overlapping ZNF300/EGR1 binding site

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