Drug Database
HY

hyaluronidase (Amphadase)

✓ Approved

Amphastar Pharmaceuticals, Inc. · HYAL1

What is hyaluronidase?

hyaluronidase is a therapeutic agent developed by Amphastar Pharmaceuticals, Inc.. It is approved for therapeutic indications via injectable (others) or subcutaneous injection.

Drug Profile

Brand NamesAmphadase
CompanyAmphastar Pharmaceuticals, Inc.
Molecular TargetHYAL1
RouteInjectable (Others), Subcutaneous Injection
StatusApproved
Sources: ClinicalTrials.gov, Amphastar Pharmaceuticals, Inc.

Mechanism of Action

Molecular Targets

hyaluronidase acts on 1 molecular target:

HYAL1hyaluronidase 1 (LUCA1, MPS9)
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Therapeutic Indications

hyaluronidase is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Surgical and medical proceduresAdjuvant therapy✓ Approved

Related Research Articles

PubMedFrontiers in drug delivery2026-09-18

Hyaluronidase-enhanced delivery in gene therapy and regenerative medicine for improved vector, cell, and cargo access.

Sewell Patrick E PE, Jensen Christopher C

Efficient delivery of gene therapy vectors and regenerative cargo to the central nervous system (CNS) is limited by the hyaluronic acid (HA)-rich extracellular matrix (ECM). Adeno-associated virus (AAV) particles, mesenchymal stem cells (MSCs), multilineage-differentiating stress-enduring (MUSE) cells, and small extracellular vesicles (sEVs) must traverse the HA-rich ECM of the nasal submucosa, the perineural and perivascular compartments, and brain parenchyma to reach CNS targets. Dense ECM imposes viscosity, steric, and hydrodynamic barriers that limit tissue penetration, and perineuronal nets impose an additional HA-based barrier around subsets of neurons. Hyaluronidase enzymes transiently depolymerize HA, reducing tissue viscosity and increasing interstitial permeability through a well-defined, reversible mechanism. Recombinant human hyaluronidase PH20 (rHuPH20) is FDA-approved as a subcutaneous delivery adjunct, demonstrating that controlled ECM modulation is clinically feasible and safe. Preclinical studies demonstrate that hyaluronidase pretreatment enhances intranasal CNS delivery of AAV vectors and sEVs, with quantified improvements in olfactory bulb and cortical distribution. Intranasal MSC and MUSE cell delivery is similarly enhanced: 100 USP units of hyaluronidase applied 30 min before cell administration significantly increased MSC delivery to the olfactory bulb and total brain area in rodent models (p = 0.02). MUSE cells, which express sphingosine-1-phosphate receptor 2 (S1PR2) and home actively to sites of neuroinflammation via the S1P-S1PR2 axis, achieve selective CNS distribution after intranasal administration in Parkinson's disease models, outperforming non-MUSE MSCs and restoring dopaminergic neuron markers and motor function. This narrative review synthesizes the mechanistic basis, evidence tiers, practical intranasal dosing and technique protocols, safety considerations, and translational knowledge gaps for hyaluronidase as a CNS delivery adjunct across viral gene therapy, non-viral platforms, gene-modified cell products, and sEV-based therapeutics. We distinguish established, off-label, and investigational applications, and provide practical guidance for clinicians developing hyaluronidase-augmented CNS programs.

PMID 42756066
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PubMedFacial plastic surgery : FPS2026-09-17

Efficacy of hyaluronidase in treating calcium hydroxylapatite-induced arterial occlusion: an experimental study using the leporine auricular artery as a model.

Rowland Payne Christopher C, Larkina Svetlana S, Seletska O O, Oliynik Nina N et al.

Hyaluronidase "melts" hyaluronic acid (HA); no such antidote exists for calcium hydroxylapatite (CaHA). Experimental evidence demonstrating efficacy of hyaluronidase in treating arterial compromise due to CaHA is lacking. Nevertheless, its use is mentioned in papers describing the management of vascular occlusion due to CaHA. Objectives & hypotheses. To investigate the efficacy of hyaluronidase as a treatment for CaHA-induced arterial occlusion using the leporine auricular artery as a model. A prospective case control series. Six Oryctolagi cuniculi were divided into two groups of three, Groups 1 and 2. Right auricular blood flow was examined by Doppler in all six. In all six, the right auricular artery was then occluded by injection of CaHA. Occlusion was confirmed by Doppler. On Day 0, Group 1 received injection of hyaluronidase, Group 2 did not. In each group, one occluded ear was biopsied on Day 1 and another on Day 4. On Day 7, the third occluded ear in each group was examined by Doppler and then biopsied. Doppler demonstrated that, without hyaluronidase blood flow rate at Day 7 was only 10% of the pre-occlusion flow rate, whereas with hyaluronidase blood flow rate at Day 7 was considerably recovered at 58% of the pre-occlusion rate. Histology revealed a similar story: without hyaluronidase at Day 7 the arterial wall anatomy was largely destroyed, whereas with hyaluronidase the arterial wall anatomy was largely conserved. Hyaluronidase improves tissue viability after arterial occlusion by CaHA. This finding has important implications for patient care.

PMID 42753925
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PubMedPolymers2026-09-15

Enzymatic Versus Energy-Based Degradation of the Cross-Linked Hyaluronic Acid Macromolecule: A Comparative Physicochemical Study of Hyaluronidase, Focused Ultrasound and Laser Irradiation.

Deda Anna A, Wilczyński Sławomir S, Sagbas Suner Selin S, Ostróżka-Cieślik Aneta A et al.

Hyaluronic acid (HA) is a high-molecular-weight glycosaminoglycan whose cross-linked hydrogels are widely used as injectable fillers; their controlled degradation is clinically important but, in practice, achievable only enzymatically with hyaluronidase. Here we compared the enzymatic, ultrasonic and photothermal degradation of a single cross-linked HA macromolecular network and characterised the resulting structural, thermal and chromatographic changes. A cross-linked HA hydrogel (Regenyal Idea, 25 mg/mL) was embedded in an ex vivo porcine skin matrix and treated in six groups: untreated control; hyaluronidase; microfocused ultrasound (7 MHz, 3 mm focal depth); and irradiation with 1064 nm Nd:YAG, diode or alexandrite lasers. Degradation was characterised by FT-IR spectroscopy, thermogravimetric analysis (TGA) and high-performance liquid chromatography (HPLC). FT-IR showed retention of the HA backbone with partial loss of the cross-linked network, while TGA revealed treatment-dependent decreases in thermal stability. By HPLC, hyaluronidase released the most soluble HA (58.2 ± 2.9% at day 1; ~88% plateau by day 2). Among the energy-based methods, only the 1064 nm Nd:YAG laser produced comparable degradation (57.3 ± 5.2%), whereas microfocused ultrasound, the diode and the alexandrite lasers released little soluble HA (3.2-5.3%). The wavelength dependence is consistent with a water-mediated photothermal scission of the HA chains. These findings identify long-pulsed 1064 nm irradiation as an effective non-enzymatic route to degrade the cross-linked hyaluronic acid macromolecule, with hyaluronidase remaining the reference standard.

PMID 42737085
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PubMedJournal of extracellular biology2026-09-15

Proteomic Atlas of Notochordal Cell-Derived Extracellular Vesicles Highlights EV-Specific NF-κB Modulation and Functional Implications of the Protein Corona.

van Maanen Josette C JC, Voskamp Chantal C, Riemers Frank M FM, Vos Harmjan R HR et al.

The notochord is a central signalling hub during embryonic development. After regression of the notochord, notochordal cells (NCs) reside within the developing intervertebral disc. The NC-secretome, including matrix, proteins and extracellular vesicles (NC-EVs), promotes regeneration of degenerate intervertebral discs and cartilage. This study aims to unravel the NC-EV-associated proteome and modulatory role in regenerative processes. NC-EVs were isolated from conditioned medium from porcine NC-rich tissue using differential centrifugation, size exclusion chromatography and density gradient centrifugation. Proteomic analysis of NC-EVs was performed using LC-MS/MS and identified 4042 unique proteins, including EV-associated markers, matrisome proteins and proteins associated with critical nodes in canonical signalling pathways. To test NC-EV bioactivity, functional analysis was performed using SBE, TCF/LEF and NF-κB luciferase reporters. NC-EVs activated SMAD3 and inhibited IL-1β-mediated NF-κB signalling. NC-EV depleted controls showed similar effects, indicating that co-isolated proteins played a major role in modulating signalling. Therefore, NC-EVs were further purified and the GAG-rich biomolecular corona was modified with hyaluronidase. Post-hyaluronidase treatment, SMAD3 activation was enhanced only in methodological controls, while inhibition of IL-1β-mediated NF-κB signalling was NC-EV specific. This study is the first to reveal the NC-EV proteome and illustrates that proteins absorbed on the NC-EVs attribute to EV-mediated functional effects.

PMID 42741550
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PubMedThe journal of venomous animals and toxins including tropical diseases2026-09-15

Proteomic characterization of Tityus championi venom and recombinant expression of its major neurotoxin.

Muñoz-Agames Milena Del C MDC, Salazar Marcos H MH, Clement Herlinda H, Hernández-Orihuela Lorena L et al.

Tityus championi is a species endemic to the southern Talamanca Mountain Range, along the border region between Costa Rica and Panama, and has been associated with severe clinical cases. Despite its medical relevance, the composition of its venom remains poorly studied. The present study aimed to characterize the proteomic composition of T. championi venom, identify its main toxin families, and recombinantly produce one of its most abundant and lethal toxins for potential use in antivenom development. Venom composition was analyzed by tandem mass spectrometry (MS/MS), enabling the identification of venom proteins. Subsequently, one of its primary lethal toxins (Tcham27) was identified and recombinantly expressed. Proteomic analysis revealed that the most abundant family in the venom corresponded to metalloproteases, with 43 protein groups (17% of the total identifications), which are associated with processes such as hemorrhage, edema, inflammation, hypotension, and necrosis. CIIMET family toxins comprised 27 protein groups (11%). Among ion channel-acting toxins, 18 protein groups (7%) corresponded to sodium channel toxins and 14 (6%) to potassium channel toxins, homologous to components from geographically proximate species such as Tityus discrepans, Tityus cf. asthenes, and Tityus jaimei. Other relevant families included cysteine-rich secretory proteins (CRISPs; 6 proteins, 3%), serine proteases (5 proteins, 2%), and lectins (5 proteins, 2%). In addition, low-abundance components such as insulin-like growth factors, nucleotide pyrophosphatases, hyaluronidase, α-amylase, lipolysis-activated toxins, and chitinase were detected, contributing to the functional diversity of the venom. Proteomic characterization of T. championi venom demonstrates that metalloproteases constitute a major protein family alongside neurotoxins. Recombinant production of its most abundant toxic peptide, which is identical to toxins in the venom of geographically proximate Tityus species, provides a key tool for developing specific antivenoms.

PMID 42741776
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PubMedFrontiers in pharmacology2026-09-13

Pharmacological characterization and nephroprotective potential of venoms from three egyptian scorpion species.

Megaly Alhussin M A AMA, Miyashita Masahiro M, Alqahtani Abdulaziz R AR, Ashry Mahmoud M et al.

Scorpion venoms are complex natural mixtures rich in bioactive molecules with emerging pharmacological relevance. Drug-induced kidney injury, particularly from chemotherapy agents like Taxol® (paclitaxel), remains a significant clinical challenge. This study investigates the molecular composition, enzymatic activities, and potential nephroprotective effects of venoms from three Egyptian scorpion species (Leiurus quinquestriatus, Buthacus leptochelys, and Scorpio maurus palmatus) against Taxol®-induced kidney injury. Comprehensive molecular mass profiling of the three venoms was performed using liquid chromatography-mass spectrometry (LC-MS). Enzymatic characterization included assays for hyaluronidase, phospholipase A2 (PLA2), hemolytic, and antibacterial activities. The disulfide-bonded versus non-disulfide-bonded peptide (NDBP) ratios were also determined. To evaluate nephroprotective efficacy, the venoms were administered in an in vivo model of Taxol®-induced nephrotoxicity. Renal antioxidant defenses, oxidative stress markers, inflammatory responses, and histopathological architecture were assessed. LC-MS revealed hundreds of venom components within the 500-9,000 Da range, indicating a high diversity of low-molecular-weight peptides. All venoms exhibited notable hyaluronidase activity, whereas PLA2 activity varied markedly: absent in L. quinquestriatus, low in B. leptochelys, and pronounced in S. m. palmatus. Minor hemolytic activity was observed only in B. leptochelys, and all venoms demonstrated weak antibacterial effects. The ratio of disulfide-bonded to non-disulfide-bonded peptides ranged from 7.5% NDBPs in L. quinquestriatus to 48% in S. m. palmatus. Despite these biochemical differences, all three venoms significantly attenuated Taxol-induced nephrotoxicity, as evidenced by restored renal antioxidant defenses, suppressed oxidative stress and inflammatory responses, and improved renal histopathological architecture. The inverse correlation between PLA2 and hyaluronidase activities, coupled with striking differences in peptide composition, exemplifies a biochemical trade-off in venom resource allocation-highlighting how distinct molecular solutions evolve to meet similar ecological demands. From a pharmacological perspective, the comparable nephroprotective efficacy across species suggests that scorpion venoms contain bioactive constituents capable of modulating key molecular pathways involved in drug-induced renal injury. In a pharmacoepidemiologic context, these findings highlight the potential of venom-derived compounds as adjunctive or protective agents to mitigate chemotherapy-associated nephrotoxicity, supporting further investigation into their safety, efficacy, and translational applicability.

PMID 42729245
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