Genomic Organization, Physical Mapping, and Expression Analysis of the Human Protein Arginine Methyltransferase 1 Gene

Scorilas, Andreas; Black, Margot H.; Talieri, Maroulio; Diamandis, Eleftherios P.

doi:10.1006/bbrc.2000.3807

Cited by 67 publications

(68 citation statements)

References 35 publications

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“…cDNAs were amplified using the PF/PR primers (24) specific for PRMT1v1 to -3 or using either a forward PRMT1v4-specific primer (5Ј-aaatcttccagcggggtcgcg-3Ј), PRMT1v5-specific primer (5Ј-actggagagatggtgtcctgtgg-3Ј), PRMT1v6-specific primer (5Ј-aagctgaccagacaaagagagg-3Ј), or a PRMT1v7-specific primer (5Ј-tgcatcatggaggagatgctgaagg-3Ј) with the reverse PR primer. Primers specific for actin (24) were used to show that an equal amount of total cDNA was used for each reaction. An initial incubation at 98°C for 2 min was followed by 35 cycles consisting of a 95°C denaturation step (30 s), a 65°C annealing step (30 s), and a 72°C extension step (30 s).…”

Section: Mouse Wild Type and Prmt1mentioning

confidence: 99%

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Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization

Goulet

Gauvin

Boisvenue

et al. 2007

Journal of Biological Chemistry

166

200

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PRMT1 is the predominant member of a family of protein arginine methyltransferases (PRMTs) that have been implicated in various cellular processes, including transcription, RNA processing, and signal transduction. It was previously reported that the human PRMT1 pre-mRNA was alternatively spliced to yield three isoforms with distinct N-terminal sequences. Close inspection of the genomic organization in the 5-end of the PRMT1 gene revealed that it can produce up to seven protein isoforms, all varying in their N-terminal domain. A detailed biochemical characterization of these variants revealed that unique N-terminal sequences can influence catalytic activity as well as substrate specificity. In addition, our results uncovered the presence of a functional nuclear export sequence in PRMT1v2. Finally, we find that the relative balance of PRMT1 isoforms is altered in breast cancer.

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Section: Mouse Wild Type and Prmt1mentioning

confidence: 99%

“…It was previously reported that alternative splicing of the human PRMT1 primary transcript could generate at least three protein isoforms, themselves differing at their N terminus (23,24). We describe here the complex genomic organization in the 5Ј-end of the PRMT1 gene that can produce up to seven protein isoforms expressed in a tissue-specific manner.…”

mentioning

confidence: 92%

Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization

Goulet

Gauvin

Boisvenue

et al. 2007

Journal of Biological Chemistry

166

200

View full text Add to dashboard Cite

show abstract

“…The PRMT1 gene was known to give rise to three distinct isoforms of the same enzyme (Scott et al, 1998;Scorilas et al, 2000), due to alternative splicing. The sequence of the splice variants that produce each isoform have been reported by Scorilas et al (2000), and the variants have been characterised as v1, v2 and v3, v1 being the shortest one.…”

Section: Identification Of a New Prmt1 Splice Variantmentioning

confidence: 99%

“…The sequence of the splice variants that produce each isoform have been reported by Scorilas et al (2000), and the variants have been characterised as v1, v2 and v3, v1 being the shortest one. During the course of this study, the emergence of an additional gene product came to our attention.…”

Section: Identification Of a New Prmt1 Splice Variantmentioning

confidence: 99%

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The PRMT1 gene expression pattern in colon cancer

et al. 2008

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The methylation of arginine has been implicated in many cellular processes, such as regulation of transcription, mRNA splicing, RNA metabolism and transport. The enzymes responsible for this modification are the protein arginine methyltransferases. The most abundant methyltransferase in human cells is protein arginine methyltransferase 1. Methylation processes appear to interfere in the emergence of several diseases, including cancer. During our study, we examined the expression pattern of protein arginine methyltransferase 1 gene in colon cancer patients. The emerging results showed that the expression of one of the gene variants is associated with statistical significant probability to clinical and histological parameters, such as nodal status and stage. This is a first attempt to acquire an insight on the possible relation of the expression pattern of protein arginine methyltransferase 1 and colon cancer progression.

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Immune responses to DNA mismatch repair enzymes hMSH2 and hPMS1 in patients with pancreatic cancer, dermatomyositis and polymyositis

Okada

Noji

Goto

et al. 2005

Intl Journal of Cancer

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To identify tumor antigens useful for diagnosis and immunotherapy of patients with pancreatic ductal adenocarcinoma, we applied a SEREX approach with a cDNA library made from 5 pancreatic cancer cell lines and sera obtained from 8 patients with pancreatic cancer, and isolated total 32 genes, including 14 previously characterized genes and 18 genes with unknown functions. Among these isolated antigens, serum IgG antibodies for 2 isolated DNA mismatch repair enzymes, Homo sapiens mutS homolog 2 (hMSH2) and Homo sapiens postmeiotic segregation increased 1 (hPMS1), were detected in patients with pancreatic ductal adenocarcinoma and dermatomyositis (DM), and polymyositis (PM), but not in sera from healthy individuals. Immunohistochemical study demonstrated that hMSH2 and hPMS1 were over-expressed in pancreatic ductal adenocarcinoma compared to normal pancreatic ducts. These results suggested that hMSH2 and hPMS1 may be useful as CD41 helper T cell antigens for immunotherapy of pancreatic cancer patients and that serum IgG antibodies may be useful for diagnosis of patients with pancreatic ductal adenocarcinoma and DM/PM. ' 2005 Wiley-Liss, Inc.Key words: SEREX; tumor antigens; pancreatic cancer; DNA mismatch repair enzyme Early diagnosis and curative treatment are still difficult for pancreatic ductal adenocarcinoma despite of increased incidence rate.

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Genomic Organization, Physical Mapping, and Expression Analysis of the Human Protein Arginine Methyltransferase 1 Gene

Cited by 67 publications

References 35 publications

Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization

Alternative Splicing Yields Protein Arginine Methyltransferase 1 Isoforms with Distinct Activity, Substrate Specificity, and Subcellular Localization

The PRMT1 gene expression pattern in colon cancer

Immune responses to DNA mismatch repair enzymes hMSH2 and hPMS1 in patients with pancreatic cancer, dermatomyositis and polymyositis

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