The direct chemical estimation of carbamino compounds of CO<sub>2</sub> with hæmoglobin

Ferguson, John; Roughton, F. J. W.

doi:10.1113/jphysiol.1934.sp003212

Cited by 70 publications

(7 citation statements)

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“…This covalent bond causes a + 44 Da mass shift and can take place on lysine side chain amino groups [130] or at the protein's N-terminus [131] to result in the formation of a labile carbamate compound. Carbamate formation, or carbamylation, is an intrinsically rapid chemical reaction that has been shown to take place on proteins such as haemoglobin [132,133], ribulose bisphosphate carboxylase-oxygenase (RuBisCO) [134], peroxisome proteins [135] and select connexin hemichannels [136,137]. Carbamylation of these proteins has been shown to play important functional roles in regulating their activity.…”

Section: Co 2 -Dependent Post-translational Modificationsmentioning

confidence: 99%

Carbon dioxide-dependent signal transduction in mammalian systems

et al. 2021

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Carbon dioxide (CO 2 ) is a fundamental physiological gas known to profoundly influence the behaviour and health of millions of species within the plant and animal kingdoms in particular. A recent Royal Society meeting on the topic of ‘Carbon dioxide detection in biological systems' was extremely revealing in terms of the multitude of roles that different levels of CO 2 play in influencing plants and animals alike. While outstanding research has been performed by leading researchers in the area of plant biology, neuronal sensing, cell signalling, gas transport, inflammation, lung function and clinical medicine, there is still much to be learned about CO 2 -dependent sensing and signalling. Notably, while several key signal transduction pathways and nodes of activity have been identified in plants and animals respectively, the precise wiring and sensitivity of these pathways to CO 2 remains to be fully elucidated. In this article, we will give an overview of the literature relating to CO 2 -dependent signal transduction in mammalian systems. We will highlight the main signal transduction hubs through which CO 2 -dependent signalling is elicited with a view to better understanding the complex physiological response to CO 2 in mammalian systems. The main topics of discussion in this article relate to how changes in CO 2 influence cellular function through modulation of signal transduction networks influenced by pH, mitochondrial function, adenylate cyclase, calcium, transcriptional regulators, the adenosine monophosphate-activated protein kinase pathway and direct CO 2 -dependent protein modifications. While each of these topics will be discussed independently, there is evidence of significant cross-talk between these signal transduction pathways as they respond to changes in CO 2 . In considering these core hubs of CO 2 -dependent signal transduction, we hope to delineate common elements and identify areas in which future research could be best directed.

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Section: Co 2 -Dependent Post-translational Modificationsmentioning

confidence: 99%

Carbon dioxide-dependent signal transduction in mammalian systems

et al. 2021

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The Transport of Carbon Dioxide by Erythrocytes and Plasma in Dogfish Blood

Ferguson¹,

Horváth²,

Pappenheimer³

1938

The Biological Bulletin

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During the summer of 1936, unsuccessful attempts were made by J. K. W. F. and J. R. P. to measure (using the chemical method of Ferguson and Roughton, 1934) the carbamino compounds of CO 2 with hemoglobin of mackerel blood and dogfish blood. The difficulty of preparing stable solutions of hemoglobin from these bloods proved to be the most serious obstacle. An attempt was then made to apply the kinetic method of Meldrum and Roughton (1933) to dogfish blood. This too was unsuccessful because carbonic anhydrase could not be completely inactivated by cyanide as required in this method. Some evidence as to the state of CO 2 in dogfish blood was then sought by determining the distribution of CO 2 between the erythrocytes

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“…Bohr and co-workers demonstrated that the haemoglobin oxygen saturation curve was responsive to the partial pressure of CO 2 while Christiansen and co-workers showed that CO 2 uptake by the blood at constant p CO 2 was increased by the presence of O 2 2 , 3 . Henriques then used kinetic evidence to postulate the direct combination of CO 2 with the free amino groups on haemoglobin 4 and Ferguson and Roughton confirmed this through direct chemical analyses 5 . The site of CO 2 binding was demonstrated 6 , 7 to occur at the Val-1β site 8 linked to the O 2 binding state of the β-chain 9 .…”

Section: Introductionmentioning

confidence: 98%

The identification of carbon dioxide mediated protein post-translational modifications

et al. 2018

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Carbon dioxide is vital to the chemistry of life processes including metabolism, cellular homoeostasis, and pathogenesis. CO2 is generally unreactive but can combine with neutral amines to form carbamates on proteins under physiological conditions. The most widely known examples of this are CO2 regulation of ribulose 1,5-bisphosphate carboxylase/oxygenase and haemoglobin. However, the systematic identification of CO2-binding sites on proteins formed through carbamylation has not been possible due to the ready reversibility of carbamate formation. Here we demonstrate a methodology to identify protein carbamates using triethyloxonium tetrafluoroborate to covalently trap CO2, allowing for downstream proteomic analysis. This report describes the systematic identification of carbamates in a physiologically relevant environment. We demonstrate the identification of carbamylated proteins and the general principle that CO2 can impact protein biochemistry through carbamate formation. The ability to identify protein carbamates will significantly advance our understanding of cellular CO2 interactions.

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The direct chemical estimation of carbamino compounds of CO₂ with hæmoglobin

Cited by 70 publications

References 3 publications

Carbon dioxide-dependent signal transduction in mammalian systems

Carbon dioxide-dependent signal transduction in mammalian systems

The Transport of Carbon Dioxide by Erythrocytes and Plasma in Dogfish Blood

The identification of carbon dioxide mediated protein post-translational modifications

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The direct chemical estimation of carbamino compounds of CO2 with hæmoglobin

Cited by 70 publications

References 3 publications

Carbon dioxide-dependent signal transduction in mammalian systems

Carbon dioxide-dependent signal transduction in mammalian systems

The Transport of Carbon Dioxide by Erythrocytes and Plasma in Dogfish Blood

The identification of carbon dioxide mediated protein post-translational modifications

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The direct chemical estimation of carbamino compounds of CO₂ with hæmoglobin