Sociedad Americana de Hirudoterapia

Cystatin-Hv

Recombinant cystatin / cysteine protease inhibitor from Haementeria vizottoi leech — Linhares 2021 potent CatL inhibitor (Ki 7.9 nM).

Preclínico / mecanísticoLast updated: 2026-05-27 · Reviewed by ASH Editorial Board
Molecular weight of Cystatin-Hv 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 kDaCystatin-Hv11.5 kDa
Molecular weight (kilodaltons) of Cystatin-Hv (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
Recombinant cystatin / cysteine protease inhibitor from Haementeria vizottoi leech — Linhares 2021 potent CatL inhibitor (Ki 7.9 nM).
Evidence level
In vitro
Drug vs leech
Recombinant (genetically expressed)

Clinical translation limit

Cystatin-Hv's in vitro CatL inhibition does NOT establish clinical efficacy in cancer or cardiovascular disease where CatL is implicated. No FDA-approved derivative exists; Haementeria vizottoi is not the FDA-cleared K040187 medicinal leech species.

Molecular Profile

Category
Proteinase Inhibitor
Evidence tier
Preclinical
Molecular weight
11,500 Da
Source species
Haementeria vizottoi
Discovered
2021 · Linhares DC et al.
Cystatin-Hv molecular structure

Biological Targets

  • cathepsin L (lysosomal cysteine protease; Ki 7.9 nM)

Key Citations

  1. Linhares DC et al. (2021), Toxins (Basel) · PMID 34941695

External Resources

    Related Proteinase Inhibitor Compounds

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