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Necator americanus (human hookworm) aspartyl proteinases and digestion of skin macromolecules during skin penetration.
Am J Trop Med Hyg. 1999 May; 60(5):840-7.AJ

Abstract

The infective larvae of Necator americanus were shown to secrete all mechanistic classes of proteolytic enzymes with two overall pH optima of 6.5 and 8.5 using fluorescein isothiocyanate-labeled casein as the substrate. Since infective larvae are obligate skin penetrators, the effect of each of these enzyme classes against macromolecules derived from human skin was examined. Larval secretions were shown to degrade collagen types I, III, IV, and V, fibronectin, laminin, and elastin. All the skin macromolecules tested were hydrolyzed by aspartyl proteinase activity, which was inhibitable by pepstatin A. Collagen and elastin was also hydrolyzed by metalloproteinase activity, while the serine proteinase activity hydrolyzed only elastin. As a consequence of these experiments, the effect of proteinase inhibitors on the penetration of live larvae through hamster skin was tested. Larval penetration was significantly inhibited only by pepstatin A, confirming the importance of the aspartyl proteinase activity during the skin penetration process.

Authors+Show Affiliations

Department of Life Sciences, Nottingham Trent University, Nottingham, United Kingdom.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10344662

Citation

Brown, A, et al. "Necator Americanus (human Hookworm) Aspartyl Proteinases and Digestion of Skin Macromolecules During Skin Penetration." The American Journal of Tropical Medicine and Hygiene, vol. 60, no. 5, 1999, pp. 840-7.
Brown A, Girod N, Billett EE, et al. Necator americanus (human hookworm) aspartyl proteinases and digestion of skin macromolecules during skin penetration. Am J Trop Med Hyg. 1999;60(5):840-7.
Brown, A., Girod, N., Billett, E. E., & Pritchard, D. I. (1999). Necator americanus (human hookworm) aspartyl proteinases and digestion of skin macromolecules during skin penetration. The American Journal of Tropical Medicine and Hygiene, 60(5), 840-7.
Brown A, et al. Necator Americanus (human Hookworm) Aspartyl Proteinases and Digestion of Skin Macromolecules During Skin Penetration. Am J Trop Med Hyg. 1999;60(5):840-7. PubMed PMID: 10344662.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Necator americanus (human hookworm) aspartyl proteinases and digestion of skin macromolecules during skin penetration. AU - Brown,A, AU - Girod,N, AU - Billett,E E, AU - Pritchard,D I, PY - 1999/5/27/pubmed PY - 1999/5/27/medline PY - 1999/5/27/entrez SP - 840 EP - 7 JF - The American journal of tropical medicine and hygiene JO - Am J Trop Med Hyg VL - 60 IS - 5 N2 - The infective larvae of Necator americanus were shown to secrete all mechanistic classes of proteolytic enzymes with two overall pH optima of 6.5 and 8.5 using fluorescein isothiocyanate-labeled casein as the substrate. Since infective larvae are obligate skin penetrators, the effect of each of these enzyme classes against macromolecules derived from human skin was examined. Larval secretions were shown to degrade collagen types I, III, IV, and V, fibronectin, laminin, and elastin. All the skin macromolecules tested were hydrolyzed by aspartyl proteinase activity, which was inhibitable by pepstatin A. Collagen and elastin was also hydrolyzed by metalloproteinase activity, while the serine proteinase activity hydrolyzed only elastin. As a consequence of these experiments, the effect of proteinase inhibitors on the penetration of live larvae through hamster skin was tested. Larval penetration was significantly inhibited only by pepstatin A, confirming the importance of the aspartyl proteinase activity during the skin penetration process. SN - 0002-9637 UR - https://www.unboundmedicine.com/medline/citation/10344662/Necator_americanus__human_hookworm__aspartyl_proteinases_and_digestion_of_skin_macromolecules_during_skin_penetration_ L2 - https://ajtmh.org/doi/10.4269/ajtmh.1999.60.840 DB - PRIME DP - Unbound Medicine ER -