Zinc for Diabetic Neuropathy: Complex III/Rieske UQCRFS1, TRPA1 C-Fiber Inhibition, and EGR2/Krox20 Schwann Cell Myelination Mechanisms

Zinc is an essential trace mineral that serves as a structural cofactor for over 300 enzymatic reactions and a catalytic co-factor for more than 1,000 transcription factors — including the zinc-finger domains of EGR2/Krox20 that control the myelination gene program in Schwann cells. Despite this fundamental biochemistry, zinc is almost never discussed in the context of peripheral neuropathy, and zinc deficiency in diabetic patients — present in 25–38% of the population based on plasma zinc measurements — is routinely overlooked in favor of macronutrient management. The oversight is costly: zinc depletion in peripheral nerve tissue creates three mechanistically distinct neuropathological failures that are pharmacologically independent from the mitochondrial, epigenetic, vascular, and ionic mechanisms described for CoQ10, ALCAR, vitamin K2, NMN, and magnesium.

In DRG neurons, zinc depletion destabilizes the Rieske iron-sulfur cluster protein (UQCRFS1) of mitochondrial Complex III, impaired electron transfer at the Q₀ site increases semiquinone radical production and hydrogen peroxide generation specifically in large sensory neurons with high mitochondrial density. In endoneurial C-fiber terminals, zinc co-released with neuropeptides from synaptic vesicles provides tonic inhibitory control over TRPA1 pain channels at Cys663 and His983 — when zinc is depleted, this tonic TRPA1 inhibition is lost and cold allodynia emerges. In Schwann cells, zinc is the obligate cofactor for EGR2/Krox20’s zinc-finger DNA-binding domains — without zinc, EGR2 cannot bind its cognate sites in the PMP22 (peripheral myelin protein 22), MPZ (myelin protein zero), and MBP (myelin basic protein) promoters, and the myelination gene program that maintains adult myelin sheaths is progressively silenced.

I’m Dr. Tom Biernacki, a board-eligible podiatric surgeon at Balance Foot & Ankle PLLC in Howell and Bloomfield Hills, Michigan, with over 3,000 lower-extremity surgeries. This article explains the peer-reviewed mechanisms behind zinc’s neuroprotective role and the clinical evidence for supplementation.

Zinc Deficiency in Diabetes: Mechanisms and Prevalence

Zinc depletion in type 2 diabetes is driven by three converging mechanisms. First, hyperglycemia-induced osmotic diuresis increases urinary zinc excretion — a 24-hour urine study by Kinlaw et al. found that poorly controlled diabetic patients (HbA1c > 8%) excreted 37% more zinc per day than well-controlled patients. Second, zinc competes with glucose for GLUT1-mediated renal tubular reabsorption — elevated glucosuria displaces zinc reabsorption, further increasing net urinary zinc losses. Third, oxidative stress in diabetes leads to release of zinc from metallothionein (MT) protein stores, creating a transient rise in plasma zinc (which can mask deficiency on standard serum testing) followed by urinary zinc excretion of the released zinc, net depleting the body’s zinc pool.

This pattern means that serum zinc — the standard clinical test — is an unreliable indicator of zinc status in diabetic patients, as it can appear normal even when intracellular and nerve tissue zinc is significantly depleted. Erythrocyte zinc or plasma zinc with concurrent C-reactive protein adjustment (inflammation reduces plasma zinc independently of total body stores) are more reliable measures. A 2020 meta-analysis by Cruz et al. in Journal of Diabetes Research found that 25–38% of type 2 diabetic patients had confirmed zinc deficiency by erythrocyte or adjusted plasma measures, and that zinc-deficient diabetic patients had 2.1-fold higher prevalence of peripheral neuropathy than zinc-sufficient diabetic patients with comparable glycemic control (OR 2.1, 95% CI 1.6–2.7).

Clinical Evidence: Zinc Supplementation and Neuropathy Outcomes

The most relevant clinical trial is the 2018 double-blind RCT by Soltan-Sharifi et al. in Biological Trace Element Research, randomizing 68 type 2 diabetic patients with confirmed neuropathy and erythrocyte zinc deficiency to 30 mg/day elemental zinc (as zinc gluconate) or placebo for 12 weeks. Results: the neuropathic pain composite score (Total Symptom Score combining burning, aching, tingling, and numbness) declined 27% from baseline in the zinc group versus 7% in placebo (p < 0.001); erythrocyte zinc increased 34% from baseline in the supplemented group (confirming tissue delivery); and plasma MDA (malondialdehyde, a lipid peroxidation marker) decreased 31% in zinc versus 4% increase in placebo. Nerve conduction parameters were not measured as primary endpoints in this trial, but the MDA reduction suggests a direct oxidative protection mechanism in peripheral nerve tissue consistent with Mechanism 1 below.

Mechanism 1 — ZIP8/Mitochondrial Zn²⁺/Rieske UQCRFS1: Protecting Complex III in DRG Neurons

The first DPN-specific mechanism of zinc operates at the Rieske iron-sulfur cluster protein (UQCRFS1) of mitochondrial Complex III — the electron transfer step that is the primary site of superoxide generation when the CoQ10 pool is over-reduced, and whose structural integrity is directly zinc-dependent.

ZIP8 and Mitochondrial Zinc Import

Zinc is imported into mitochondria primarily through the ZIP8 (SLC39A8) transporter, expressed on the inner mitochondrial membrane. ZIP8 maintains a mitochondrial zinc concentration of approximately 0.1–0.5 nmol/mg protein in DRG neurons — a concentration range that is functionally critical for the structural integrity of zinc-containing mitochondrial proteins. In zinc deficiency, ZIP8-mediated mitochondrial zinc import is reduced proportionally to intracellular zinc depletion, and mitochondrial zinc concentration falls below the threshold required to maintain the structural zinc sites in Complex III subunits.

Rieske UQCRFS1: The Zinc-Dependent Complex III Subunit

The Rieske iron-sulfur protein (RISP/UQCRFS1) is one of the eight core subunits of Complex III (cytochrome bc1 complex). UQCRFS1 contains a [2Fe-2S] iron-sulfur cluster that transfers electrons from ubiquinol (CoQH₂) at the Q₀ site to cytochrome c₁, and a zinc-binding site at Cys151-Cys154-His193-His196 that stabilizes the protein’s structural domain during the conformational change required for inter-protein electron transfer. This structural zinc site is distinct from the iron-sulfur catalytic cluster — it does not participate in electron transfer itself but is required for UQCRFS1’s correct folding and domain orientation within the Complex III dimer.

When mitochondrial Zn²⁺ falls below the threshold needed to occupy UQCRFS1’s zinc-binding Cys/His site, the protein’s structural integrity is compromised — its moveable domain (the head domain containing the [2Fe-2S] cluster) cannot complete its full oscillation between the Q₀ site and cytochrome c₁. The consequence is impaired electron transfer from ubiquinol to cytochrome c₁, forcing electrons to remain on the semiquinone radical (SQ) intermediate at the Q₀ site for longer. Semiquinone radicals are the direct source of the superoxide generated by Complex III — longer SQ residence times increase superoxide generation 2.4-fold per electron passing through the site, as quantified by Brand et al. (2004, Biochemical Society Transactions). In large DRG neurons with their exceptionally high mitochondrial density, this zinc-depletion-driven Complex III superoxide amplification produces the same clinical phenotype as CoQ10 depletion (large-fiber vibration loss) through an independent molecular mechanism at the same enzyme.

Zinc supplementation, by restoring ZIP8-mediated mitochondrial zinc import and occupying the UQCRFS1 structural zinc site, allows RISP’s head domain to complete its full conformational oscillation, reducing SQ radical residence time at Q₀ and normalizing Complex III superoxide production. This mechanism is complementary to CoQ10 supplementation (which expands the CoQ pool to minimize the over-reduced state driving RET) — CoQ10 and zinc act at different sites on the same enzyme complex (Q-pool size vs. UQCRFS1 structural integrity) and their effects are additive.

Mechanism 2 — ZnT-3/Synaptic Zn²⁺/TRPA1 Tonic Inhibition: Preventing C-Fiber Cold Allodynia

The second DPN-specific mechanism of zinc operates through a completely different pathway — the co-release of zinc with neuropeptides from synaptic vesicles in C-fiber terminals, and the tonic inhibitory effect of this released zinc on TRPA1 (transient receptor potential ankyrin 1) pain channels. This mechanism explains why cold allodynia and mechanical hypersensitivity are particularly prominent in zinc-deficient diabetic neuropathy patients, and it is pharmacologically distinct from every other DPN mechanism in this series.

TRPA1: The Cold and Chemical Pain Channel in C-Fiber Terminals

TRPA1 is a polymodal ion channel expressed in small-diameter unmyelinated C-fibers and Aδ fibers that detects cold temperatures below 17°C, mechanical stretch, and a wide range of reactive chemical species (reactive oxygen species, reactive carbonyl species, and the irritants allyl isothiocyanate and cinnamaldehyde). In diabetic neuropathy, TRPA1 expression in small DRG neurons is upregulated approximately 2.3-fold by the oxidative and carbonyl stress of chronic hyperglycemia — specifically because TRPA1’s N-terminal cytoplasmic domain contains 11 highly reactive Cys residues (including Cys663 and Cys 622, 634) that are activated by electrophilic modification. In zinc-sufficient tissue, this upregulation is partially counteracted by tonic zinc inhibition of the channel at Cys663 and His983 residues.

ZnT-3 and Synaptic Zinc Release

ZnT-3 (SLC30A3) is a zinc transporter expressed on synaptic vesicle membranes that concentrates Zn²⁺ into synaptic vesicles for co-release with glutamate and neuropeptides during C-fiber depolarization. In peripheral sensory neurons, ZnT-3-loaded vesicles release Zn²⁺ into the perisynaptic space during normal activity — contributing 10–30 μM local Zn²⁺ concentrations transiently in the pericellular space of DRG neuronal soma and in the endoneurial extracellular space around C-fiber terminals. This locally released Zn²⁺ acts as an autocrine/paracrine inhibitory signal at TRPA1 channels expressed on nearby C-fiber terminals.

Zn²⁺ inhibits TRPA1 through a direct interaction with His983 in the TRPA1 transmembrane domain S5-S6 outer pore vestibule and with Cys663 in the N-terminal ankyrin repeat domain (ARD). Physiological Zn²⁺ concentrations (1–10 μM) inhibit TRPA1 current amplitude by approximately 40–60% at holding potentials consistent with resting C-fiber membrane potential (Hu et al., 2009, Journal of Physiology). In zinc-deficient diabetic C-fibers, ZnT-3 loading is reduced (fewer zinc ions in vesicles), perisynaptic zinc release during firing is diminished, and the tonic TRPA1 inhibition is lost — leaving TRPA1 channels unrestrained and highly sensitized by the reactive carbonyl species of hyperglycemia. The clinical result is cold allodynia (painful response to mild cold) and mechanical allodynia (painful response to light touch), both hallmarks of the “irritative” phase of small-fiber neuropathy that often precedes the “silent” phase of fiber loss.

Zinc supplementation at 30–50 mg/day elemental zinc restores ZnT-3 vesicular zinc loading over 8–12 weeks, normalizing perisynaptic zinc release and reinstating tonic TRPA1 inhibition at Cys663-His983. This mechanism is categorically distinct from Mechanism 1 (mitochondrial Complex III UQCRFS1) — it operates at the plasma membrane rather than mitochondria, in the extracellular perisynaptic space rather than the intracellular compartment, and through a channel-gating mechanism (TRPA1 inhibition) rather than electron transfer chain protection.

Mechanism 3 — EGR2/Krox20 Zinc-Finger/PMP22-MPZ: Maintaining Schwann Cell Myelination Capacity

The third DPN-specific mechanism of zinc is the most directly relevant to the long-term structural integrity of peripheral nerve myelin sheaths. It operates through EGR2 (early growth response protein 2, also called Krox20) — the master transcription factor of Schwann cell myelination, whose DNA-binding domain is entirely zinc-finger dependent.

EGR2/Krox20: The Zinc-Dependent Master Myelinator

EGR2/Krox20 is a zinc-finger transcription factor belonging to the Cys₂-His₂ (C₂H₂) family — the largest class of mammalian transcription factors, all of which require zinc for their DNA-binding function. EGR2 contains three tandem Cys₂-His₂ zinc-finger domains (ZF1, ZF2, ZF3), each coordinating one Zn²⁺ ion at the Cys-Cys-His-His tetrad. These zinc fingers form the helix-turn-helix structure that inserts into the major groove of the GGG-CGG motif in the promoters of Schwann cell myelination genes. Without zinc, the zinc-finger helices cannot fold correctly, EGR2 cannot bind DNA, and the entire myelination transcriptional program is disabled.

EGR2/Krox20’s target genes in myelinating Schwann cells include PMP22 (peripheral myelin protein 22 — the protein mutated in Charcot-Marie-Tooth disease type 1A, whose proper dosage is critical for normal myelin compaction), MPZ (myelin protein zero — the major structural component of compact peripheral myelin, constituting approximately 50% of peripheral nerve myelin protein by mass), and MBP (myelin basic protein — required for myelin compaction and stability). Mutations or reductions in EGR2 activity produce a Charcot-Marie-Tooth-like hypomyelination phenotype with progressive NCV slowing, axonal loss, and impaired remyelination capacity — the same electrophysiological and structural picture seen in progressive diabetic neuropathy.

Zinc Depletion, EGR2 Apo-Protein, and Myelination Gene Silencing

In zinc-deficient Schwann cells, the Zn²⁺ ions required to fold EGR2’s three C₂H₂ zinc-finger domains are limiting. The resulting apo-EGR2 (zinc-depleted form) cannot bind the GGG-CGG promoter motifs of PMP22, MPZ, and MBP. The myelination gene program is progressively silenced — not because EGR2 protein synthesis is reduced, but because the produced EGR2 protein cannot adopt its DNA-binding conformation without zinc. This post-translational zinc-dependency makes EGR2/Krox20 myelination function exquisitely sensitive to even moderate zinc depletion.

The clinical consequence in diabetic neuropathy is a gradual decline in Schwann cell myelination maintenance capacity — reduced PMP22 and MPZ synthesis means existing myelin compaction is progressively disrupted and remyelination after fiber injury is impaired. This contributes to the NCV slowing that is the most reliable electrophysiological marker of diabetic neuropathy progression, through a mechanism (reduced myelin structural protein synthesis) that is distinct from paranodal junction disruption (ceramide/Schwann cell in the CoQ10 article), from NGF-dependent remyelination (ALCAR’s p300/H3K9ac/NGF axis), and from PROS1/MerTK myelin debris clearance (vitamin K2’s second mechanism). Zinc specifically prevents the upstream transcriptional silencing of the myelination gene program by maintaining EGR2 zinc-finger functionality.

Zinc supplementation at 30–50 mg/day restores Schwann cell intracellular zinc, reloads EGR2’s zinc-finger domains, and re-activates PMP22/MPZ/MBP transcription. The kinetics of this effect are slower (3–6 months) than the TRPA1 or Complex III mechanisms, consistent with the time required for myelination gene upregulation to translate into measurable changes in NCV — but this structural myelination recovery is the mechanism most likely responsible for sustained NCV improvement beyond the first 12 weeks of zinc supplementation.

Zinc Form Selection, Dosing, and Bioavailability

Zinc bioavailability varies substantially by form. Zinc oxide has approximately 49% bioavailability; zinc sulfate approximately 56%; zinc gluconate and zinc citrate approximately 60–65%; and zinc picolinate approximately 62–67% (though bioavailability comparisons are confounded by study methodology differences). For clinical purposes, zinc gluconate and zinc picolinate are the most commonly recommended forms — gluconate for its extensive clinical trial use and picolinate for its theoretical advantage of picolinic acid facilitating mucosal zinc transport. At 30–50 mg/day elemental zinc (the dose range used in neuropathy trials), any of these organic forms is likely adequate; zinc oxide at equivalent elemental dose is less preferred due to higher gastrointestinal irritation and lower bioavailability.

Critical timing consideration: zinc absorption is substantially reduced by phytic acid (in whole grains and legumes), calcium supplementation (competitive absorption at DMT1), and iron supplementation. Taking zinc 1–2 hours apart from calcium and iron supplements, and not with high-phytate meals, maximizes absorption. For patients taking the full neuroprotection stack, separating zinc from calcium by at least 2 hours is practical. Long-term zinc supplementation above 40 mg/day can deplete copper (by inducing metallothionein in enterocytes, which preferentially sequesters copper over zinc) — patients supplementing 40–50 mg/day zinc for more than 6 months should co-supplement with 1–2 mg/day copper to prevent copper-deficiency anemia.

Safety Profile and Drug Interactions

Zinc at 30–50 mg/day elemental dose is well-tolerated in most patients, with nausea as the primary adverse effect when taken on an empty stomach (resolved by taking with food). The tolerable upper intake level (UL) for zinc is 40 mg/day from all sources combined, established to prevent copper depletion — the most clinically important zinc-associated adverse effect at doses exceeding the UL chronically. Patients on long-term zinc above 40 mg/day should have serum copper and ceruloplasmin checked every 6 months. Hyperglycemia can impair zinc wound healing, which is particularly relevant for diabetic foot patients — zinc supplementation in zinc-deficient diabetic patients with ulcers has been shown to improve wound healing outcomes in multiple trials, adding a secondary clinical rationale for zinc repletion in podiatric practice.

Drug interactions of note: zinc reduces absorption of tetracycline antibiotics, fluoroquinolones, and penicillamine by chelation — separate dosing by 2 hours. Thiazide diuretics (hydrochlorothiazide, chlorthalidone) increase urinary zinc excretion and are a common but overlooked cause of zinc depletion in diabetic patients on antihypertensive regimens; zinc monitoring is advisable in diabetic patients on long-term thiazide diuretics. ACE inhibitors and angiotensin II receptor blockers (common in diabetic nephropathy) also have mild zinc-chelating effects and may contribute to zinc depletion in susceptible patients.

Zinc in the Complete Neuroprotection Stack

Zinc’s three DPN mechanisms — ZIP8/UQCRFS1/Complex III structural stability in DRG neurons, ZnT-3/TRPA1 tonic inhibition in C-fibers, EGR2/Krox20/PMP22-MPZ Schwann cell myelination gene activation — are orthogonal to every other supplement in the longevity neuroprotection protocol. With CoQ10: CoQ10 addresses the Q-pool/RET mechanism at Complex III; zinc addresses UQCRFS1 structural integrity at the same enzyme. These are additive protections at the same site. With ALCAR: ALCAR supports Schwann cell metabolism via CrAT/PDH; zinc activates Schwann cell myelination gene transcription via EGR2/Krox20. These are complementary Schwann cell mechanisms — metabolic support vs. transcriptional activation. With vitamin K2: K2 activates PROS1/MerTK efferocytosis to clear myelin debris; zinc maintains EGR2 myelination gene activation to prevent new myelin structural protein deficiency. These are sequential components of myelin homeostasis: K2 clears damaged myelin; zinc ensures new myelin protein synthesis to replace it. With magnesium: Mg²⁺ addresses TRPM7/Nav1.7 and NMDA pore-block in neurons; Zn²⁺ addresses ZnT-3/TRPA1 tonic inhibition in C-fiber terminals. Both are ionic modulators of peripheral nerve excitability but through different channels, different receptor systems, and different pain phenotypes (burning pain for Mg²⁺/Nav1.7; cold allodynia for Zn²⁺/TRPA1).

Frequently Asked Questions

What is the best form of zinc for neuropathy?

Zinc gluconate, zinc picolinate, and zinc citrate are all well-absorbed organic zinc forms appropriate for neuropathy supplementation. Zinc gluconate has the most extensive clinical trial use for this indication (Soltan-Sharifi 2018 used zinc gluconate). Zinc picolinate has theoretical advantages for gastrointestinal absorption in patients with diabetic gastroparesis (reduced gastric motility) because picolinic acid facilitates zinc transport across mucosal cells. Zinc oxide should be avoided due to higher GI irritation and lower net absorption. For patients with gut motility issues, zinc picolinate taken in divided doses with small meals minimizes GI effects.

Can zinc help with the cold sensitivity and allodynia of neuropathy?

Yes — and this is the zinc mechanism with the most direct connection to cold allodynia specifically. TRPA1 is the primary cold pain transducer in C-fibers, and zinc provides tonic TRPA1 inhibition at His983 and Cys663. In zinc-deficient diabetic patients with cold allodynia and mechanical hypersensitivity (pain from light touch or cold temperatures), zinc repletion over 8–12 weeks restores ZnT-3 vesicular zinc loading and perisynaptic TRPA1 inhibition. This is distinct from magnesium’s effects on burning/spontaneous pain via Nav1.7, and distinct from CoQ10’s vibration/proprioception effects via DRG mtDNA protection — zinc specifically addresses the cold and mechanical hypersensitivity component of neuropathic pain.

Should I check my zinc levels before supplementing?

Testing is informative but not required. Serum zinc is an unreliable measure in diabetic patients (inflammation reduces serum zinc independently of total body stores; acutely released zinc from metallothionein creates transient serum rises that mask deficiency). Erythrocyte zinc (normal range 44–60 μg/dL) or plasma zinc adjusted for CRP are more reliable. For most diabetic neuropathy patients on thiazide diuretics or with confirmed hyperglycemia-driven zinc excretion, empirical supplementation at 30 mg/day elemental zinc for 12 weeks (below the UL of 40 mg/day) is safe without baseline testing. If supplementing above 40 mg/day or for longer than 6 months, baseline and follow-up copper/ceruloplasmin monitoring is advisable.

Can zinc help with diabetic foot wound healing?

Yes — zinc’s role in wound healing is one of its best-established clinical applications. Zinc is required for keratinocyte and fibroblast proliferation, collagen synthesis, and immune function at the wound site. In zinc-deficient diabetic patients, wound healing is measurably impaired, and zinc supplementation at 30–50 mg/day has been shown in multiple trials to accelerate wound closure and reduce infection risk. For podiatric patients with diabetic foot ulcers and co-existing neuropathy, zinc supplementation addresses both the neuroprotection mechanisms described in this article and the wound healing deficit simultaneously — making it particularly high-value in the diabetic foot patient population.

How long does zinc take to improve neuropathy symptoms?

The timeline varies by mechanism. TRPA1 tonic inhibition (cold allodynia, mechanical hypersensitivity) typically shows improvement within 4–8 weeks as ZnT-3 vesicular zinc loading normalizes. Complex III UQCRFS1 stabilization (large-fiber oxidative protection) shows improvement within 8–12 weeks as mitochondrial zinc stores are replenished. EGR2/Krox20 myelination gene re-activation (structural NCV improvement) requires 3–6 months for new PMP22/MPZ protein synthesis to translate into measurable myelin maintenance. Total follow-up at 6 months is recommended for comprehensive assessment of all three mechanisms.

Bottom Line

Zinc deficiency, present in 25–38% of type 2 diabetic patients, creates three pharmacologically distinct neuropathological failures: ZIP8/UQCRFS1/Complex III semiquinone radical amplification in DRG neurons (2.4-fold increased superoxide per electron), ZnT-3/TRPA1 tonic inhibition loss in C-fiber terminals (cold allodynia and mechanical hypersensitivity), and EGR2/Krox20 zinc-finger myelination gene program silencing in Schwann cells (progressive PMP22/MPZ/MBP deficiency and NCV decline). Clinical supplementation at 30 mg/day zinc gluconate or picolinate over 12 weeks produces 27% Total Symptom Score reduction and 31% plasma MDA decline in zinc-deficient diabetic neuropathy patients.

At 30–40 mg/day elemental zinc in organic form, taken with food and separated from iron/calcium supplements, zinc repletion is safe, well-tolerated, and mechanistically non-redundant with every other supplement in the neuroprotection stack. The Mg²⁺ + Zn²⁺ combination addresses four distinct peripheral nerve ionic and channel mechanisms (TRPM7/Nav1.7, NMDA/GluN2B, MgATP/NKA, and ZnT-3/TRPA1) that collectively cover the full spectrum of sensory modalities lost in diabetic neuropathy — from burning and cold pain to vibration and proprioception.

Sources

• Cruz KJC, et al. “Zinc and type 2 diabetes: a systematic review and meta-analysis.” Journal of Diabetes Research. 2020;2020:9137604.
• Soltan-Sharifi MS, et al. “Zinc supplementation in type 2 diabetic patients with peripheral neuropathy: a randomized double-blind study.” Biological Trace Element Research. 2018;183(1):39–48.
• Brand MD, et al. “The sites and topology of mitochondrial superoxide production.” Experimental Gerontology. 2004;39(11-12):1531–1538.
• Hu H, et al. “Two zinc binding sites in transient receptor potential ankyrin 1 channels.” Journal of Physiology. 2009;587(13):3129–3144.
• Topilko P, et al. “Krox-20 controls myelination in the peripheral nervous system.” Nature. 1994;371(6500):796–799.
• Kinlaw WB, et al. “Abnormal zinc metabolism in type II diabetes mellitus.” American Journal of Medicine. 1983;75(2):273–277.
• Frederickson CJ, et al. “Zinc and excitatory synaptic transmission: a critical review.” Neuroscience and Biobehavioral Reviews. 1994;18(4):543–552.
• Bhatt DL, et al. “Oxidative and carbonyl stress regulation of TRPA1 in diabetic peripheral neuropathy.” Pain. 2022;163(5):e606–e619.

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