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Acaciain peptidase: the first South American pollen peptidase potentially involved in respiratory allergy.

Abstract

Acacia caven (Mol.) Molina pollen causes pollinosis in South America. The aim of this work was to isolate, purify and characterize the proteolytic enzymes of A. caven pollen, and study their influence on allergy. A series of chromatographic steps was applied to purify the proteolytic extract of A. caven pollen. The purified fraction was partially characterized and then, it was assayed on airway bioactive peptides (Substance P, Vasoactive Intestinal Peptide and Bradykinin) and peptide degradation was visualized by direct protein sequencing. The cellular detachment of an airway-derived epithelial cell line (A-549) was measured by methylene blue binding assay. The degradation of proteins from intercellular junctions (Occludin, Claudin and E-cadherin) was visualized by Western blot. A 75-kDa peptidase, named Acaciain peptidase, was purified and classified as a serine peptidase. Acaciain peptidase degraded bioactive peptides involved in the maintenance and recovery of the bronchomotor tone; it caused cellular detachment of A-549 cell line and degradation of intercellular junction proteins. Acaciain peptidase can alter the integrity of the epithelium barrier, causing cell permeability, increasing the allergic sensitization and exacerbating the overall bronchoconstrictive effect detected in asthmatic lungs. This novel serine peptidase constitutes a relevant therapeutic target in the treatment of allergic disorders. This article is protected by copyright. All rights reserved.

Authors+Show Affiliations

Bromatology Laboratory, Faculty of Chemistry, Biochemistry and Pharmacy, National University of San Luis, Chacabuco 917, 5700, San Luis, Argentina.Center of Neuroscience and Cell Biology of Coimbra, Department of Zoology, University of Coimbra, Rua Larga 3004-535, 3004-517, Coimbra, Portugal.Bromatology Laboratory, Faculty of Chemistry, Biochemistry and Pharmacy, National University of San Luis, Chacabuco 917, 5700, San Luis, Argentina. National Council of Scientific and Technical Research, Institute of Applied Physics (INFAP, CCT- San Luis- CONICET), Ejército de los Andes 950, Block 2, Floor 2, 5700, San Luis, Argentina.Center of Neuroscience and Cell Biology of Coimbra, Department of Zoology, University of Coimbra, Rua Larga 3004-535, 3004-517, Coimbra, Portugal. Departament of Life Science, Faculty of Science and Technology, University of Coimbra, Rua Larga 3004-535, 3004-517, Coimbra, Portugal.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31628771

Citation

Barcia, Cristina, et al. "Acaciain Peptidase: the First South American Pollen Peptidase Potentially Involved in Respiratory Allergy." Biotechnology and Applied Biochemistry, 2019.
Barcia C, Coelho AS, Barberis S, et al. Acaciain peptidase: the first South American pollen peptidase potentially involved in respiratory allergy. Biotechnol Appl Biochem. 2019.
Barcia, C., Coelho, A. S., Barberis, S., & Veríssimo, P. (2019). Acaciain peptidase: the first South American pollen peptidase potentially involved in respiratory allergy. Biotechnology and Applied Biochemistry, doi:10.1002/bab.1837.
Barcia C, et al. Acaciain Peptidase: the First South American Pollen Peptidase Potentially Involved in Respiratory Allergy. Biotechnol Appl Biochem. 2019 Oct 19; PubMed PMID: 31628771.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Acaciain peptidase: the first South American pollen peptidase potentially involved in respiratory allergy. AU - Barcia,Cristina, AU - Coelho,Ana Sofia, AU - Barberis,Sonia, AU - Veríssimo,Paula, Y1 - 2019/10/19/ PY - 2019/02/28/received PY - 2019/10/13/accepted PY - 2019/10/20/entrez PY - 2019/10/20/pubmed PY - 2019/10/20/medline KW - Acacia caven KW - allergy KW - purification KW - serine protease JF - Biotechnology and applied biochemistry JO - Biotechnol. Appl. Biochem. N2 - Acacia caven (Mol.) Molina pollen causes pollinosis in South America. The aim of this work was to isolate, purify and characterize the proteolytic enzymes of A. caven pollen, and study their influence on allergy. A series of chromatographic steps was applied to purify the proteolytic extract of A. caven pollen. The purified fraction was partially characterized and then, it was assayed on airway bioactive peptides (Substance P, Vasoactive Intestinal Peptide and Bradykinin) and peptide degradation was visualized by direct protein sequencing. The cellular detachment of an airway-derived epithelial cell line (A-549) was measured by methylene blue binding assay. The degradation of proteins from intercellular junctions (Occludin, Claudin and E-cadherin) was visualized by Western blot. A 75-kDa peptidase, named Acaciain peptidase, was purified and classified as a serine peptidase. Acaciain peptidase degraded bioactive peptides involved in the maintenance and recovery of the bronchomotor tone; it caused cellular detachment of A-549 cell line and degradation of intercellular junction proteins. Acaciain peptidase can alter the integrity of the epithelium barrier, causing cell permeability, increasing the allergic sensitization and exacerbating the overall bronchoconstrictive effect detected in asthmatic lungs. This novel serine peptidase constitutes a relevant therapeutic target in the treatment of allergic disorders. This article is protected by copyright. All rights reserved. SN - 1470-8744 UR - https://www.unboundmedicine.com/medline/citation/31628771/Acaciain_peptidase:_the_first_South_American_pollen_peptidase_potentially_involved_in_respiratory_allergy L2 - https://doi.org/10.1002/bab.1837 DB - PRIME DP - Unbound Medicine ER -