Two genes, COL4A3 and COL4A4 coding for the human α3(IV) and α4(IV) collagen chains are arranged head‐to‐head on chromosome 2q361

Momota, Ryusuke; Sugimoto, Mineharu; Oohashi, Toshitaka; Kigasawa, Kazuteru; Yoshioka, Hidekatsu; Ninomiya, Yoshifumi

doi:10.1016/s0014-5793(98)00128-8

Cited by 47 publications

(35 citation statements)

References 24 publications

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“…Type IV collagen is one of the most abundant constituents of basement membrane (BM) architecture that forms a network like structure in ECM (18,19). Type IV collagen consists of six distinct gene products (α1 to α6 chains) and their genomic localization shows a pair-wise head-to-head arrangement with a bi-directional promoter, that were mapped onto three different chromosomes (20)(21)(22). Each α-chain in type IV collagen is composed of three distinct domains, a cysteine-rich N-terminal 7S domain, a central long triple helical domain and a globular C-terminal NC1 domain (Fig.…”

Section: Physiological Functions Of Type IV Collagenmentioning

confidence: 99%

RETRACTED ARTICLE: Inhibition of Tumor Angiogenesis by Tumstatin: Insights into Signaling Mechanisms and Implications in Cancer Regression

Sudhakar

Boosani

2008

Pharm Res

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Growing tumors develop additional new blood vessels to meet the demand for adequate nutrients and oxygen, a process called angiogenesis. Cancer is a highly complex disease promoted by excess angiogenesis; interfering with this process poses for an attractive approach for controlling tumor growth. This hypothesis led to the identification of endogenous angiogenesis inhibitors generated from type IV collagen, a major component of vascular basement membrane (VBM). Type IV collagen and the angiogenesis inhibitors derived from it are involved in complex roles, than just the molecular construction of basement membranes. Protease degradation of collagens in VBM occurs in various physiological and pathological conditions and produces several peptides. Some of these peptides are occupied in the regulation of functions conflicting from those of their original integral molecules. Tumstatin (α3(IV)NC1), a proteolytic C-terminal non-collagenous (NC1) domain from type IV collagen α3 chain has been highlighted recently because of its potential role in anti-angiogenesis, however its biological actions are not limited to these processes. α3(IV)NC1 inhibits proliferation by promoting endothelial cell apoptosis and suppresses diverse tumor angiogenesis, thus making it a potential candidate for future cancer therapy. The present review surveys the physiological functions of type IV collagen and discovery of α3(IV)NC1 as an antiangiogenic protein with a comprehensive overview of the knowledge gained by us towards understanding its signaling mechanisms.

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Section: Physiological Functions Of Type IV Collagenmentioning

confidence: 99%

RETRACTED ARTICLE: Inhibition of Tumor Angiogenesis by Tumstatin: Insights into Signaling Mechanisms and Implications in Cancer Regression

Sudhakar

Boosani

2008

Pharm Res

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“…For example, some bidirectional promoters serve to maintain a stoichiometric relationship, such as the histone genes (Albig et al 1997;Ahn and Gruen 1999;Maxson et al 1983), whereas others regulate the coexpression of genes that function in the same biological pathway (Schmidt et al 1993;Sugimoto et al 1994;Momota et al 1998), or to control expression through different timepoints such as genes involved in the cell cycle (Guarguaglini et al 1997). Other bidirectional promoters provide coordinated responses to induction signals such as heat shock (Hansen et al 2003).…”

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confidence: 99%

An Abundance of Bidirectional Promoters in the Human Genome

Trinklein¹,

Aldred²,

Hartman³

et al. 2004

Genome Res.

551

706

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The alignment of full-length human cDNA sequences to the finished sequence of the human genome provides a unique opportunity to study the distribution of genes throughout the genome. By analyzing the distances between 23,752 genes, we identified a class of divergently transcribed gene pairs, representing more than 10% of the genes in the genome, whose transcription start sites are separated by less than 1000 base pairs. Although this bidirectional arrangement has been previously described in humans and other species, the prevalence of bidirectional gene pairs in the human genome is striking, and the mechanisms of regulation of all but a few bidirectional genes are unknown. Our work shows that the transcripts of many bidirectional pairs are coexpressed, but some are antiregulated. Further, we show that many of the promoter segments between two bidirectional genes initiate transcription in both directions and contain shared elements that regulate both genes. We also show that the bidirectional arrangement is often conserved among mouse orthologs. These findings demonstrate that a bidirectional arrangement provides a unique mechanism of regulation for a significant number of mammalian genes

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“…genes form collagen IV heterotrimers † (Filie et al, 1995;Momota et al, 1998;Soininen et al, 1988;Sugimoto et al, 1994).…”

mentioning

confidence: 99%

New functional roles for non-collagenous domains of basement membrane collagens

Ortéga

Werb

2002

Journal of Cell Science

198

145

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Collagens IV, XV and XVIII are major components of various basement membranes. In addition to the collagen-specific triple helix, these collagens are characterized by the presence of several non-collagenous domains. It is clear now that these ubiquitous collagen molecules are involved in more subtle and sophisticated functions than just the molecular architecture of basement membranes, particularly in the context of extracellular matrix degradation. Degradation of the basement membrane collagens occurs during numerous physiological and pathological processes such as embryonic development or tumorigenesis and generates collagen fragments. These fragments are involved in the regulation of functions differing from those of their original intact molecules. The non-collagenous C-terminal fragment NC1 of collagen IV, XV and XVIII have been recently highlighted in the literature because of their potential in reducing angiogenesis and tumorigenesis, but it is clear that their biological functions are not limited to these processes. Proteolytic release of soluble NC1 fragments stimulates migration, proliferation, apoptosis or survival of different cell types and suppresses various morphogenetic events.

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Two genes, COL4A3 and COL4A4 coding for the human α3(IV) and α4(IV) collagen chains are arranged head‐to‐head on chromosome 2q36¹

Cited by 47 publications

References 24 publications

RETRACTED ARTICLE: Inhibition of Tumor Angiogenesis by Tumstatin: Insights into Signaling Mechanisms and Implications in Cancer Regression

RETRACTED ARTICLE: Inhibition of Tumor Angiogenesis by Tumstatin: Insights into Signaling Mechanisms and Implications in Cancer Regression

An Abundance of Bidirectional Promoters in the Human Genome

New functional roles for non-collagenous domains of basement membrane collagens

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