Enoyl-coenzyme A hydratase in cancer

Zhang, Jun; Ibrahim, Mohammed Mohammed; Sun, Ming‐Zhong; Tang, Jianwu

doi:10.1016/j.cca.2015.01.020

Cited by 17 publications

(16 citation statements)

References 45 publications

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“…ECHDC3 shares 30 % identity with ECHDC2 [24], and these proteins may possibly have similar functions in the pathophysiology of cardiovascular diseases. In addition, both proteins are named after enoyl-CoA hydratase, an essential enzyme for the β-oxidation of FAs, because they share a conserved domain [7, 23]. The potential involvement of ECHDC3 in β-oxidation of FA pathway led us to investigate the possible correlation between changes of FA profile and this gene expression.…”

Section: Discussionmentioning

confidence: 99%

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The relationship of the oleic acid level and ECHDC3 mRNA expression with the extent of coronary lesion

et al. 2016

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Section: Discussionmentioning

confidence: 99%

“…ECHDC3 encodes enoyl-CoA hydratase domain containing 3, a mitochondrial enzyme that has a crotonase-like domain similar to enoyl-CoA hydratase [4]. Furthermore, ECHDC3 is presumed to be involved in β-oxidation, the most important and well-known pathway for fatty acid (FA) oxidation [5–7]. …”

Section: Introductionmentioning

confidence: 99%

The relationship of the oleic acid level and ECHDC3 mRNA expression with the extent of coronary lesion

et al. 2016

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“…This superfamily represents a diverse range of enzymes including enoyl-CoA hydratase and dienoyl-CoA isomerase, which catalize the β-oxidation of fatty acids (123, 124). The 7-lung-transmembrane domain has homology with GPCRs found in desmosponges, invertebrates, and amoebozoa species (125, 126).…”

Section: Early Coevolution Of Complement and Metabolismmentioning

confidence: 99%

Keeping It All Going—Complement Meets Metabolism

Kolev

Kemper²

2017

Front. Immunol.

377

553

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The complement system is an evolutionary old and crucial component of innate immunity, which is key to the detection and removal of invading pathogens. It was initially discovered as a liver-derived sentinel system circulating in serum, the lymph, and interstitial fluids that mediate the opsonization and lytic killing of bacteria, fungi, and viruses and the initiation of the general inflammatory responses. Although work performed specifically in the last five decades identified complement also as a critical instructor of adaptive immunity—indicating that complement’s function is likely broader than initially anticipated—the dominant opinion among researchers and clinicians was that the key complement functions were in principle defined. However, there is now a growing realization that complement activity goes well beyond “classic” immune functions and that this system is also required for normal (neuronal) development and activity and general cell and tissue integrity and homeostasis. Furthermore, the recent discovery that complement activation is not confined to the extracellular space but occurs within cells led to the surprising understanding that complement is involved in the regulation of basic processes of the cell, particularly those of metabolic nature—mostly via novel crosstalks between complement and intracellular sensor, and effector, pathways that had been overlooked because of their spatial separation. These paradigm shifts in the field led to a renaissance in complement research and provide new platforms to now better understand the molecular pathways underlying the wide-reaching effects of complement functions in immunity and beyond. In this review, we will cover the current knowledge about complement’s emerging relationship with the cellular metabolism machinery with a focus on the functional differences between serum-circulating versus intracellularly active complement during normal cell survival and induction of effector functions. We will also discuss how taking a closer look into the evolution of key complement components not only made the functional connection between complement and metabolism rather “predictable” but how it may also give clues for the discovery of additional roles for complement in basic cellular processes.

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“…in Tunicates harbored a crotonase domain which is commonly present in crotonase/enoyl-coenzyme A (CoA) hydratases, enzymes that are key to fatty acid oxidation. 128 Similarly, avian C3 has a ferredoxin NADP(H) reductase domain, 129 indicating functional involvement in the regulation of the electron transport chain in mitochondria as well as regulation of cholesterol and steroid metabolism. 130 Importantly, there are still remnants of such metabolic domains in modern C3.…”

Section: Lo C Ati On Mat Ter S: S Patial B Ia S In Prr Ac Tivitie Smentioning

confidence: 99%

Complement and human T cell metabolism: Location, location, location

West

Kunz

Kemper

2020

Immunological Reviews

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Immunological Reviews. 2020;295:68-81. wileyonlinelibrary.com/journal/imr 1 | INTRODUC TI ON Our contemporary immune system has evolved under the constant pressure from a broad range of pathogens that manipulate the host to enhance their own propagation. As diverse as the pathogenic threats are, ranging from intra-and extracellular bacteria, viruses, fungi, and complex parasites, as elegant and effective are the defense mechanisms developed and employed by the host to combat this constant onslaught. Particularly, the detection systems that are functioning as the first lines of defense against such invaders are formidable. If a microbe has managed to penetrate the protective physical barriers, such as the skin, or lung, a range of innate immune sensors either circulating in the blood, lymph, and interstitial fluids or expressed in and on scavenger and sentinel cells, such as neutrophils and microphages, detect the conserved pathogen-associated molecular patterns (PAMPs). These sensor systems comprise several pattern recognition receptors (PRRs) and include the Toll-like receptors (TLRs), the NOD-like receptors (NLRs), the retinoic acid-inducible gene-I (RIG)-like system, several distinct inflammasomes, and the complement system-derived receptors. 1,2 Activation of PRRs by a pathogen is most often triggered in several sensor systems in parallel and then initiates the general inflammatory reaction as well as tailored immune cell activation specifically effective toward the identified pathogen. The ability of PRR systems to decisively discriminate between a real threat, that is non-self and dangerous self via recognizing so-called danger-associated molecular patterns (DAMPs), and self and harmless alterations of self is critical for our health. Thus, there are several checks and balances build into the PRR systems that prevent unwanted reactions against sensed AbstractThe complement system represents one of the evolutionary oldest arms of our immune system and is commonly recognized as a liver-derived and serum-active system critical for providing protection against invading pathogens. Recent unexpected findings, however, have defined novel and rather "uncommon" locations and activities of complement. Specifically, the discovery of an intracellularly active complement system-the complosome-and its key role in the regulation of cell metabolic pathways that underly normal human T cell responses have taught us that there is still much to be discovered about this system. Here, we summarize the current knowledge about the emerging functions of the complosome in T cell metabolism. We further place complosome activities among the non-canonical roles of other intracellular innate danger sensing systems and argue that a "location-centric" view of complement evolution could logically justify its close connection with the regulation of basic cell physiology. K E Y W O R D S CD46, complement, complosome, metabolism, T cells | 69 WEST ET al.innocuous antigens. However, PRRs not only take care to contain tissue injury during their...

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Enoyl-coenzyme A hydratase in cancer

Cited by 17 publications

References 45 publications

The relationship of the oleic acid level and ECHDC3 mRNA expression with the extent of coronary lesion

The relationship of the oleic acid level and ECHDC3 mRNA expression with the extent of coronary lesion

Keeping It All Going—Complement Meets Metabolism

Complement and human T cell metabolism: Location, location, location

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