Sulfhemoglobinemia Presenting as Pulse Oximetry Desaturation

Aravindhan, N.; Chisholm, David

doi:10.1097/00000542-200009000-00040

Cited by 40 publications

(26 citation statements)

References 1 publication

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“…The inability of both sulfmyoglobin and sulfhemoglobin to bind O 2 effectively can lead to sulfhemoglobinemia, a rare cause of cyanosis induced by drugs such as phenacetin, dapsone, sulphonamides, and metoclopramide, and by exposure to other sulfur-containing compounds (57,68,76). However, moderate concentrations of sulfhemoglobin are well tolerated despite the low O 2 binding (1,25). This has been explained by the observed right shift in the Hb-O 2 dissociation curve, which indicates that although it is more difficult for sulfhemoglobin to bind O 2 , it facilitates O 2 delivery to tissues.…”

mentioning

confidence: 99%

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Pietri

Román-Morales

López‐Garriga

2011

Antioxidants & Redox Signaling

196

136

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Historically, hydrogen sulfide (H(2)S) has been regarded as a poisonous gas, with a wide spectrum of toxic effects. However, like ·NO and CO, H(2)S is now referred to as a signaling gas involved in numerous physiological processes. The list of reports highlighting the physiological effects of H(2)S is rapidly expanding and several drug candidates are now being developed. As with ·NO and CO, not a single H(2)S target responsible for all the biological effects has been found till now. Nevertheless, it has been suggested that H(2)S can bind to hemeproteins, inducing different responses that can mediate its effects. For instance, the interaction of H(2)S with cytochrome c oxidase has been associated with the activation of the ATP-sensitive potassium channels, regulating muscle relaxation. Inhibition of cytochrome c oxidase by H(2)S has also been related to inducing a hibernation-like state. Although H(2)S might induce these effects by interacting with hemeproteins, the mechanisms underlying these interactions are obscure. Therefore, in this review we discuss the current state of knowledge about the interaction of H(2)S with vertebrate and invertebrate hemeproteins and postulate a generalized mechanism. Our goal is to stimulate further research aimed at evaluating plausible mechanisms that explain H(2)S reactivity with hemeproteins.

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mentioning

confidence: 99%

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Pietri

Román-Morales

López‐Garriga

2011

Antioxidants & Redox Signaling

196

136

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“…Some drugs that cause sulfhaemoglobinaemia can also cause methaemoglobinaemia 3. The presence of methaemoglobin (2.0%) in this was almost certainly a false positive due to similarity in wavelength detection (a ‘cross reaction’) by the blood gas analyser with sulfhaemoglobin.…”

Section: Discussionmentioning

confidence: 90%

Sulfhaemoglobinaemia caused by ferrous sulfate

Derbas

Warsame

Omar³

et al. 2017

BMJ Case Reports

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A 78-year-old man was referred from his primary care clinic to the emergency department due to bluish discolouration of his lips and decreased oxygen saturation on pulse oximetry. The patient was asymptomatic. Physical exam was normal except for lip cyanosis. A CT pulmonary angiogram was negative for pulmonary embolism. Arterial blood gas (ABG) analysis with co-oximetry showed low oxyhaemoglobin, normal partial pressure of oxygen and methaemoglobinaemia, but an unexplained 'gap' in total haemoglobin saturation. This gap was felt to be due to sulfhaemoglobinaemia. After a thorough review of his medications, ferrous sulfate was stopped which resulted in resolution in patient's cyanosis and normalisation of his ABG after 7 weeks.

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“…Alternatively, this could result from conditions such as methemoglobinemia and sulfhemoglobinemia that are associated with reduced SpO 2 in the context of a normal arterial blood oxygen tension (PaO 2 ). 2,3 Venous pulsations secondary to venous congestion may result in artefactual low SpO 2 . 4 Improper application of the oximeter probe and certain nail paints can also result in decreased SpO 2 readings.…”

Section: Discussionmentioning

confidence: 99%

Unusually Low Oxyhemoglobin Saturation on Polysomnography

Mansukhani

Kolla

Altchuler

2017

Journal of Clinical Sleep Medicine

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A 22-year-old male college student with prior diagnoses of mild obstructive sleep apnea, delayed sleep-wake phase disorder, and inadequate sleep hygiene presented to the sleep clinic for an evaluation of ongoing daytime hypersomnolence despite the use of mixed dextroamphetamine/amphetamine salts extended-release preparation (Adderall XR) 20 mg two times a day prescribed by his primary care provider for sleepiness.He reported going to bed at 10:00 pm, falling asleep quickly, sleeping throughout the night until 8:00 am, and not napping during the daytime but feeling extremely sleepy with an Epworth Sleepiness Scale score of 20/24. He described waking with a dry mouth but did not endorse snoring, snort arousals, or headaches upon awakening. There was no history suggestive of leg movements at night, cataplexy, hypnagogic/hypnopompic hallucinations or sleep paralysis. On examination, The red arrow indicates oxyhemoglobin saturation. Mean saturation was 73% with a range of 66% to 78%. Hypopneas were scored when there was a further drop in oxyhemoglobin saturation from the baseline by ≥ 4% accompanied by a reduction in the nasal pressure signal by ≥ 30% for ≥ 90% of the event, each lasting ≥ 10 seconds. No apneas were noted during this study. The arousal index was 14.9 events/h and sleep efficiency was 93.6%. Sleep onset latency was 4.5 minutes and initial rapid eye movement latency was 89.5 minutes with 21% of the total time spent in rapid eye movement sleep. N1 = stage N1 sleep, N2 = stage N2 sleep, N3 = stage N3 sleep, PLM = periodic limb movement, R = rapid eye movement sleep, RERA = respiratory-effort related arousal, W = wake. SLEEP MEDICINE PEARLS Unusually Low Oxyhemoglobin Saturation on Polysomnography

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Sulfhemoglobinemia Presenting as Pulse Oximetry Desaturation

Cited by 40 publications

References 1 publication

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Hydrogen Sulfide and Hemeproteins: Knowledge and Mysteries

Sulfhaemoglobinaemia caused by ferrous sulfate

Unusually Low Oxyhemoglobin Saturation on Polysomnography

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