Incorporation of Histamine into Liver Protein in vivo

Wajda, Isabel J.; Ginsburg, M.; Waelsch, Heinrich

doi:10.1038/1911204a0

Cited by 10 publications

(6 citation statements)

References 4 publications

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“…We found radioactivity in protein fractions obtained from a mastocytoma cell line (P815) that had been treated with tritium‐labeled histamine ([ 3 H]‐HA) (Fig 1 a). This indicates that HA added extracellularly is incorporated into the proteome, confirming previous reports [18–21]. Since it has been reported that histamine is a substrate for transglutaminases (TGM, E.C.…”

Section: Resultssupporting

confidence: 89%

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Histaminylation of glutamine residues is a novel posttranslational modification implicated in G‐protein signaling

et al. 2012

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Section: Resultssupporting

confidence: 89%

“…In these cases, histamine signaling is induced by G protein coupled receptors, that are activated through binding histamine as non‐covalent ligand [16,17]. However, although still lacking a recognized function, work in the 1960s–1980s also provided evidence for histamine incorporation into proteins [18–21].…”

Section: Introductionmentioning

confidence: 99%

Histaminylation of glutamine residues is a novel posttranslational modification implicated in G‐protein signaling

et al. 2012

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“…Because mono- and polyamines, such as serotonin, histamine, dopamine, norepinephrine, putrescine, spermine, and spermidine, are abundant in vivo , protein-incorporated monoamines were detected a long time ago in various tissues and organs (Wajda et al, 1961). They were considered to be natural inhibitors of the cross-linking activity of TGs rather than functional modifiers of protein substrates.…”

Section: Enzymatic and Nonenzymatic Activities Of Tg2mentioning

confidence: 99%

Cellular Functions of Tissue Transglutaminase

Nurminskaya

Belkin

2012

International Review of Cell and Molecular Biology

216

255

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Transglutaminase 2 (TG2 or tissue transglutaminase) is a highly complex multifunctional protein that acts as transglutaminase, GTPase/ATPase, protein disulfide isomerase, and protein kinase. Moreover, TG2 has many well-documented nonenzymatic functions that are based on its noncovalent interactions with multiple cellular proteins. A vast array of biochemical activities of TG2 accounts for its involvement in a variety of cellular processes, including adhesion, migration, growth, survival, apoptosis, differentiation, and extracellular matrix organization. In turn, the impact of TG2 on these processes implicates this protein in various physiological responses and pathological states, contributing to wound healing, inflammation, autoimmunity, neurodegeneration, vascular remodeling, tumor growth and metastasis, and tissue fibrosis. TG2 is ubiquitously expressed and is particularly abundant in endothelial cells, fibroblasts, osteoblasts, monocytes/macrophages, and smooth muscle cells. The protein is localized in multiple cellular compartments, including the nucleus, cytosol, mitochondria, endolysosomes, plasma membrane, and cell surface and extracellular matrix, where Ca2+, nucleotides, nitric oxide, reactive oxygen species, membrane lipids, and distinct protein–protein interactions in the local microenvironment jointly regulate its activities. In this review, we discuss the complex biochemical activities and molecular interactions of TG2 in the context of diverse subcellular compartments and evaluate its wide ranging and cell type-specific biological functions and their regulation.

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“…4, lower scheme) [72,73]. Protein-bound c-glutamyl-HA was detected in liver and murine brain [74][75][76], but monoamines were considered as natural inhibitors for the crosslinking activity of TGs until very recently [77]. Nonetheless, Fe´su¨s et al [78] postulated a functional role for HA incorporation into proteins of activated murine mast cells as early as 1985.…”

Section: Mammalian Tgsmentioning

confidence: 99%

Novel roles for biogenic monoamines: from monoamines in transglutaminase‐mediated post‐translational protein modification to monoaminylation deregulation diseases

2011

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Functional protein serotonylation is a newly recognized post-translational modification with the primary biogenic monoamine (PBMA) serotonin (5-HT). This covalent protein modification is catalyzed by transglutaminases (TGs) and, for example, acts in the constitutive activation of small GTPases. Multiple physiological roles have been identified since its description in 2003 and, importantly, deregulated serotonylation was shown in the etiology of bleeding disorders, primary pulmonary hypertension and diabetes. The PBMAs 5-HT, histamine, dopamine, and norepinephrine all act as neurotransmitters in the nervous system and as hormones in non-neuronal tissues, which points out their physiological importance. In analogy to serotonylation we have found that also the other PBMAs act through the TG-catalyzed mechanisms of 'histaminylation', 'dopaminylation' and 'norepinephrinylation'. Therefore, PBMAs deploy a considerable portion of their effects via protein monoaminylation in addition to their canonical receptor-mediated signaling. Here, the implications of these newly identified post-translational modifications are presented and discussed. Furthermore, the potential regulatory roles of protein monoaminylation in small GTPase, heterotrimeric G-protein and lipid signaling, as well as in modulating metabolic enzymes and nuclear processes, are critically assessed.

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Incorporation of Histamine into Liver Protein in vivo

Cited by 10 publications

References 4 publications

Histaminylation of glutamine residues is a novel posttranslational modification implicated in G‐protein signaling

Histaminylation of glutamine residues is a novel posttranslational modification implicated in G‐protein signaling

Cellular Functions of Tissue Transglutaminase

Novel roles for biogenic monoamines: from monoamines in transglutaminase‐mediated post‐translational protein modification to monoaminylation deregulation diseases

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