Thromb Haemost 1984; 51(01): 024-026
DOI: 10.1055/s-0038-1661011
Original Article
Schattauer GmbH Stuttgart

Protease Inhibitors in Haementeria Leech Species

E H Murer
1   The section of Hematology-Oncology, Pennsylvania Hospital, Philadelphia, PA
,
H L James
2   The Department of Medicine, Philadelphia, PA, U.S.A.
,
A Z Budzynski
3   The Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, U.S.A.
,
S M Malinconico
3   The Thrombosis Research Center, Temple University School of Medicine, Philadelphia, PA, U.S.A.
,
G J Gasic
1   The section of Hematology-Oncology, Pennsylvania Hospital, Philadelphia, PA
› Author Affiliations
Further Information

Publication History

Received 17 June 1983

Accepted 04 November 1983

Publication Date:
19 July 2018 (online)

Summary

Inhibitors, of trypsin, plasmin, α-chymotrypsin and granulocyte elastase were demonstrated in salivary gland extracts from two species of leeches, Haementeria ghilianii and Haementeria officinalis. Preliminary fractionation of salivary gland extracts from Haementeria ghilianii allowed separation of protease inhibitors from hementin a fibrinogenolytic blood anticoagulant. It was found that the anticoagulant activity resided only in hementin-containing fractions and did not parallel protease inhibitory activity.

 
  • References

  • 1 Markwardt F. Hirudin as an inhibitor of thrombin. Methods Enzymol 1970; 19: 924-932
  • 2 Fritz H, Krejci K. Trypsin-plasmin inhibitors (bdellins) from leeches. Methods Enzymol 1976; 45: 797-805
  • 3 Seemuller U, Meier M, Ohlsson K, Muller H-P, Fritz H. Isolation and characterization of a low molecular weight inhibitor (of chymotrypsin and human granulocyte elastase and cathepsin G) from leeches. Hoppe-Seyler’s Z Physiol Chem 1977; 358: 1105-1117
  • 4 Budzynski AZ, Olexa SA, Sawyer RT. Composition of salivary gland extracts from the leech Haementeria ghilianii. Proc Soc Exp Biol Med 1981; 168: 259-265
  • 5 Budzynski AZ, Olexa SA, Brizuela BS, Sawyer RT, Stent GS. Anticoagulant and fibrinolytic properties of salivary proteins from the leech Haementeria ghilianii. Proc Soc Exp Biol Med 1981; 168: 266-275
  • 6 Kelen EM A, Rosenfeld G. Fibrinogenolytic substance (hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto 1920). Haemostasis 1975; 4: 51-64
  • 7 Baugh RJ, Schnebli HP. Role and potential therapeutic value of proteinase inhibitors in tissue destruction. In: Proteinase and Tumor Invasion. Strauli P, Barrett AJ, Baici A. (eds) Raven Press; New York: 1980. pp 157-180
  • 8 Gasic GJ, Viner ED, Budzynski AZ, Gasic GP. Inhibition of lung tumor colonization by leech salivary gland extracts from Haementeria ghilianii. Cancer Res 1983; 43: 1633-1636
  • 9 Gasic GJ, Viner ED, Gasic TB. Inhibition of experimental metastases in mice by leech salivary gland extracts and their mechanism of action. Thirty-Sixth Annual Symposium on Fundamental Cancer Research, Cancer Invasion and Metastasis. 28.02.1983. Houston, Texas:
  • 10 Sawyer RT, Lepont F, Stuart DK, Kramer AP. Growth and reproduction of the giant glossiphonid leech Haementeria ghilianii. Biol Bull 1981; 160: 322-331
  • 11 Caballero E. Revision de los hirudineos mexicanos. II. Haementeria officinalis. Ann Inst Biol Mexico 1930; 1: 319-325
  • 12 Baugh RJ, Travis J. Human leukocyte granule elastase: rapid isolation and characterization. Biochemistry 1976; 15: 836-841
  • 13 Spector T. Refinement of the Coomassie blue method of protein quantitation. Anal Biochem 1978; 86: 142-146
  • 14 Lowry OH, Rosenbrought NJ, Far AL, Randall RJ. Protein measurement with the Folin phenol reagent. J Biol Chem 1951; 193: 265-275
  • 15 Fritz H, Trauschold I, Werle E. Protease inhibitors. In: Methods of Enzymatic Analysis. Second English edition. Bergmeyer HU. (ed) Academic Press + Verlag Chemie; New York - London: 1974. 1 1064-1080
  • 16 Castillo MJ, Nakajima K, Zimmerman M, Powers JC. Sensitive substrates for human leukocyte and porcine pancreatic elastase: A study of the merits of various chromophoric and fluorogenic leaving groups in assays of serine proteases. Anal Biochem 1979; 99: 53-64