Oxidation (HSA Cys34 — HMA/HNA1/HNA2)

Definition

Oxidation of HSA refers to the chemical modification of cysteine-34 (Cys34) — the only free thiol group on the albumin molecule — by reactive oxygen species (ROS) and reactive nitrogen species (RNS). It exists along a reversibility continuum from mild (reversible) to severe (irreversible), captured by the HMA/HNA1/HNA2 nomenclature.

The HMA/HNA1/HNA2 Nomenclature

FormFull nameCys34 stateΔmassReversibilityFraction (healthy)
HMAHuman MercaptalbuminFree reduced thiol (–SH)0 Da— (reference)70–80%
HNA1Human Nonmercaptalbumin-1Disulfide bond to small thiol (Cys, homocysteine, glutathione)+119 Da (cysteinylation most common)Reversible — disulfide bond can be reduced20–30%
HNA2Human Nonmercaptalbumin-2Irreversibly oxidized to sulfenic (–SOH, +16 Da), sulfinic (–SO₂H, +32 Da), or sulfonic acid (–SO₃H, +48 Da)+16 / +32 / +48 DaIrreversible — permanent loss of antioxidant function~5%

Note: In the top-down LC-MS nomenclature used in ALBOM (el-balkhi-2025), HNA1 corresponds primarily to the HSA+CYS isoform (+119 Da); HNA2 corresponds to the sulfonylated form (HSA+SULF, +48 Da). The IEC-based HMA/HNA1/HNA2 fractionation (oettl-2013 method) captures this at lower isoform resolution.

Mechanism

ROS-driven oxidation at Cys34

HSA-Cys34-SH (HMA, antioxidant active)
  ↓ + ROS (H₂O₂, HOCl, ONOO⁻)
HSA-Cys34-S-S-Cys (HNA1 / cysteinylation) — if small thiol mixes
or
HSA-Cys34-SOH (sulfenic acid, +16 Da) — transient, unstable
  ↓ + further ROS
HSA-Cys34-SO₂H (sulfinic acid, +32 Da = HNA2 partial)
  ↓ + further ROS  
HSA-Cys34-SO₃H (sulfonic acid, +48 Da = HNA2 full, irreversible)

Homodimerization pathway (alternative fate of HMA)

HSA-Cys34-SH + HSA-Cys34-SH → (HD-HSA) disulfide homodimer

— see baldassarre-2016-dimers; both Cys34 residues consumed, both monomers lose antioxidant function

Mass spectrometry signature

ModificationΔmass (Da)ResidueDetection
Cysteinylation (HNA1)+119 DaCys34TD: HSA+CYS; BU: Cys34 +119 peptide
Sulfenic acid (intermediate)+16 DaCys34Unstable; rarely detected intact
Sulfinic acid (HNA2 partial)+32 DaCys34TD: HSA+SO₂H; noted in domenicali-2014
Sulfonic acid (HNA2 full)+48 DaCys34TD: HSA+SULF (ALBOM nomenclature); most stable irreversible form
Methionine oxidation+16 DaMet residuesBU approach; detectable by rahali-2022

Biological significance

HMA (reduced):

  • Free thiol at Cys34 = primary extracellular antioxidant — scavenges H₂O₂, peroxynitrite, hypochlorous acid
  • Metal chelation at N-terminus (Cu, Fe) — prevents Fenton reaction
  • Drug binding preserved at Sudlow sites

HNA1 (reversibly oxidized):

  • Antioxidant function lost at Cys34 — thiol consumed
  • HNA1 actively triggers cytokine production in leukocytes via p38 MAPK → alcaraz-quiles-2018
  • Reversible: in favorable redox environment, can theoretically be reduced back to HMA

HNA2 (irreversibly oxidized):

  • Permanent loss of Cys34 antioxidant function
  • Elevated HNA2 > 12% = poor 30/90-day prognosis in cirrhosis → oettl-2013
  • Correlates with MELD, bilirubin, INR, CRP

Clinical relevance

DiseaseOxidation findingClinical significance
Liver fibrosis / cirrhosisHNA1↑↑, HNA2↑, HMA↓Progressive increase with stage; HNA2 >12% predicts 90-day mortality
ACLFHNA1 and HNA2 highestWorst outcome group; multiple mechanisms of Cys34 loss
Alcoholic hepatitis (AAH)HNA1 elevatedAcute oxidative burst; see montomoli-2026-aah, das-2017-sah
DILIEarly HNA1 elevationPrecedes enzyme elevation (D3 vs D7); el-balkhi-2024-seb
Diabetes mellitusHNA1 moderately elevatedOxidative stress from metabolic disease
SepsisHNA2 elevatedSystemic oxidative stress, not liver-specific

Affected proteins in our research

  • HSA — Cys34 is the primary site; 99% of relevant oxidative changes
  • Other proteins oxidized in systemic oxidative stress (Met oxidation etc.) — detectable by BU but not our TD panel

Analytical approaches

  • IEC-HPLC (UV): separates HMA / HNA1 / HNA2 fractions; oettl-2013 method; clinical-grade; limited to 3 fractions
  • RP-LC-HR-MS top-down: full isoform landscape; +16/+32/+48 Da resolved at protein level; el-balkhi-2025 method; 10 isoforms
  • RP-LC-MS bottom-up: site-level confirmation at Cys34; oxidation states confirmed by peptide MS; rahali-2022
  • SEB test: functional assay detecting binding site disruption by oxidation at Cys34 → el-balkhi-2024-seb

Key references