American Society of Hirudotherapy

Collagenolytic Fibrinolysin

Dual-function protease degrading both fibrin clot scaffolds and collagen extracellular matrix.

Preclinical / mechanisticLast updated: 2026-05-26 · Reviewed by ASH Editorial Board
Molecular weight of Collagenolytic Fibrinolysin compared with other characterized leech-derived compoundsHementerin80 kDaHementin80 kDaHementin-Like Protein (HLP-1)80 kDaLeech Collagenase70 kDaHaemadipsa yanyuanensis Progr…70 kDaLeech Apyrase67 kDaCalin65 kDaHyaluronidase60 kDaAntithrombin III binding prot…58 kDaCollagenolytic Fibrinolysin55 kDaLeech Thrombospondin-Like Pro…50 kDaLHyal (Leech Hyaluronidase)50 kDa
Molecular weight (kilodaltons) of Collagenolytic Fibrinolysin (highlighted) alongside other characterized leech salivary compounds. Smaller proteins/peptides generally diffuse and act faster.

Mechanistic Evidence Box

Preclinical / mechanistic
Page type
Compound profile
Evidence type
Dual-function protease degrading both fibrin clot scaffolds and collagen extracellular matrix.
Evidence level
Mechanistic discussion
Drug vs leech
Purified natural compound
Safety domains
Bleeding

Clinical translation limit

Collagenolytic fibrinolysin is documented mechanistically only; no human evidence. Reported activity does NOT establish clinical thrombolytic or ECM-modulating efficacy, and no FDA-approved derivative exists.

Molecular Profile

Category
Fibrinolytic
Evidence tier
Preclinical
Molecular weight
55,000 Da
Source species
Hirudo medicinalis
Discovered
2013
Collagenolytic Fibrinolysin molecular structure

Biological Targets

  • → fibrin
  • → collagen

Key Citations

  1. Liu Z et al. (2019), Parasit Vectors

External Resources

    Related Fibrinolytic Compounds

    Destabilase

    Lysozyme with isopeptidase activity that dissolves stabilized fibrin clots — including aged thrombi resistant to tPA.

    Hementerin

    Direct fibrinogenolytic enzyme — degrades fibrinogen independently of plasmin.

    Hementin

    Direct fibrinogenolytic enzyme cleaving fibrinogen alpha-chain at unique sites — independent of plasmin.

    Destabilase Isopeptidase Activity

    Isopeptidase domain of destabilase that cleaves cross-linked fibrin — distinct from lysozyme domain.

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    This website provides educational information and does not constitute medical advice, diagnosis, or treatment recommendations. Medicinal leech therapy carries clinically meaningful risks and should be performed only by qualified clinicians under institutionally approved protocols. FDA 510(k) clearance for medicinal leeches is limited to specific indications; investigational and off-label discussions are labeled accordingly. For patient-specific guidance, consult a qualified healthcare provider.