Alternative spliced variants in the pantetheinase family of genes expressed in human neutrophils

Nitto, Takeaki; Inoue, Teruo; Node, Koichi

doi:10.1016/j.gene.2008.08.019

Cited by 24 publications

(20 citation statements)

References 35 publications

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“…Vanin-3 expression is induced by oxidative stress, which is involved in the antioxidant response as well as mouse vanin-1 gene (12). While the mouse vanin-3 has pantetheinase activity (10), the putative human vanin-3 homologue (VNN3) seems to encode a truncated protein (14). This suggests that human VNN3 is either encoding a protein other than pantetheinase or a pseudogene.…”

Section: Vanin-3/vnn3mentioning

confidence: 99%

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The Linkage Between Coenzyme A Metabolism and Inflammation: Roles of Pantetheinase

Nitto

Onodera

2013

J Pharmacol Sci

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Abstract.Pantetheinase is an enzyme hydrolyzing pantetheine, an intermediate of the coenzyme A degradation pathway. Pantetheinase has long been considered as the enzyme that recycles pantothenic acid (vitamin B 5 ) generated during coenzyme A breakdown. Genetic analyses showed that mammals have multiple genes known as vanin family genes. Recent studies using mice lacking the vanin-1 gene (pantetheinase gene) suggest that pantetheinase is actively involved in the progression of inflammatory reactions by generating cysteamine. Additional studies using human leukocytes demonstrate that human neutrophils have abundant pantetheinase proteins on the surface and inside the cells. The second pantetheinase protein, GPI-80/VNN2, is suggested to work as a modulator of the function of Mac-1 (CD11b/CD18), an adhesion molecule important to neutrophil functions. This review delineates the characteristics of the pantetheinase/vanin gene family and how they affect inflammation.

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Section: Vanin-3/vnn3mentioning

confidence: 99%

“…It has been shown that several alternative splice variants are generated from the human GPI-80/VNN2 and VNN3 genes (14). Although their specific functional differences remain to be elucidated, products derived from these alternative splice variants may have some biological activities other than pantetheinase enzyme.…”

Section: Vanin-3/vnn3mentioning

confidence: 99%

The Linkage Between Coenzyme A Metabolism and Inflammation: Roles of Pantetheinase

Nitto

Onodera

2013

J Pharmacol Sci

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“…Human Vanin 3 was recently classified a pseudogene as the open reading frame is disrupted by a frameshift. Nine splice variants for Vanin 3 have been reported in human neutrophils, however none of these extend the full span of exon 7, suggesting they don't encode the predicted Vanin protein[6]. …”

Section: Gene and Proteinmentioning

confidence: 99%

Diverse biological activities of the vascular non-inflammatory molecules – The Vanin pantetheinases

Kaskow

Proffit

Blangero

et al. 2012

Biochemical and Biophysical Research Communications

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The Vanin genes are a family that encode pantetheinases involved in recycling Coenzyme A, caytalysing the breakdown of intermediate panetheine to vitamin B5 for reuse in CoA biosynthesis. The role of pantetheinase in this most fundamental of cellular processes, was substantially characterised by the 1970s. The next 20 years saw little further interest in pantetheinase until various genetic studies implicated the vanin locus in a range of normal and disease phenotypes, and a consequent interest in the other product of pantetheinase activity, cysteamine. This report seeks to bring together the early biochemical studies with recent biological data implicating cysteamine as a regulator of the oxidative state of a cell. Numerous studies now report a role for Vanin in inflammation, oxidative stress, cell migration and numerous diseases including cardiovascular disease.

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“…Vanin-1 and vanin-2 genes have a region containing a glycosyl-phosphatidylinositol (GPI)-anchored cleavage site in exon 7 responsible for the attachment to the cell membrane through GPI anchoring [13,14]. These proteins may be released from cell surfaces as soluble forms through a cleavage by phospholipase C. In neutrophils, vanin-3 has nine splice variants lacking the full span of exon 7 [15]. …”

Section: Introductionmentioning

confidence: 99%

“…Vanin-3 , by lacking the GPI-anchoring consensus, seems to encode a truncated protein and to be a secreted protein, and its expression is induced by oxidative stress [15,21]. …”

Section: Introductionmentioning

confidence: 99%

Role of the Vanins–Myeloperoxidase Axis in Colorectal Carcinogenesis

Mariani

Roncucci

2017

IJMS

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The presence of chronic inflammation in the colonic mucosa leads to an increased risk of cancer. Among proteins involved in the regulation of mucosal inflammation and that may contribute both to structural damage of the intestinal mucosa and to intestinal carcinogenesis, there are myeloperoxidase (MPO) and vanins. The infiltration of colonic mucosa by neutrophils may promote carcinogenesis through MPO, a key enzyme contained in the lysosomes of neutrophils that regulates local inflammation and the generation of reactive oxygen species (ROS) and mutagenic species. The human vanin gene family consists of three genes: vanin-1, vanin-2 and vanin-3. All vanin molecules are pantetheinases, that hydrolyze pantetheine into pantothenic acid (vitamin B5), and cysteamine, a sulfhydryl compound. Vanin-1 loss confers an increased resistance to stress and acute intestinal inflammation, while vanin-2 regulates adhesion and transmigration of activated neutrophils. The metabolic product of these enzymes has a prominent role in the inflammation processes by affecting glutathione levels, inducing ulcers through a reduction in mucosal blood flow and oxygenation, decreasing local defense mechanisms, and in carcinogenesis by damaging DNA and regulating pathways involved in cell apoptosis, metabolism and growth, as Nrf2 and HIF-1α.

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Alternative spliced variants in the pantetheinase family of genes expressed in human neutrophils

Cited by 24 publications

References 35 publications

The Linkage Between Coenzyme A Metabolism and Inflammation: Roles of Pantetheinase

The Linkage Between Coenzyme A Metabolism and Inflammation: Roles of Pantetheinase

Diverse biological activities of the vascular non-inflammatory molecules – The Vanin pantetheinases

Role of the Vanins–Myeloperoxidase Axis in Colorectal Carcinogenesis

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