alexa Identification of the 37kda Annexin-A1 Protein in Tears of Normal Subjects and Association of its 33kda Inactive Form with Active Vernal Keratoconjunctivitis Patients | Abstract
ISSN: 2155-6121

Journal of Allergy & Therapy
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Research Article

Identification of the 37kda Annexin-A1 Protein in Tears of Normal Subjects and Association of its 33kda Inactive Form with Active Vernal Keratoconjunctivitis Patients

Samia Yazid1*, Andrea Leonardi2, Virginia Calder3 and Roderick Flower1

1William Harvey Research Institute, Queen Mary University, London, UK

2University of Padua, Italy

3UCL, University of Ophthalmology, London, UK

*Corresponding Author:
Dr. SamiaYazid, PhD
Molecular Therapy Department
Institute of Ophthalmology
University College London, 11/43 Bath street
London, UK, EC1V 9EL
E-mail: [email protected]

Received Date:November 26, 2011; Accepted Date: January 21, 2012; Published January 26, 2012

Citation: Yazid S, Leonardi A, Calder V, Flower R (2012) Identification of the 37kda Annexin-A1 Protein in Tears of Normal Subjects and Association of its 33kda Inactive Form with Active Vernal Kerato Conjunctivitis Patients. J Aller Ther S7:007.doi: 10.4172/2155-6121.S7-007

Copyright: © 2012 Yazid S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Background: Annexin-A1 (Anx-A1) is a glucocorticoid-regulated 37kDa protein with powerful anti-inflammatory actions: enhanced release from target cells occurs following addition of the anti-allergic cromone drugs. Anx-A1 is inactivated by proteolytic cleavage of the N-terminus and increased amounts of the cleaved 33kDa product correlate with inflammatory responses.

Aim: To investigate if Anx-A1 is detectable in human tear specimens from patients with vernal keratoconjunctivitis (VKC).

Methods: Tear specimens were collected from patients affected by active VKC (n=23) before and after therapy with Alomide (equivalent to Lodoxamide) 0.1%(n=11) for 10 daysand non-inflammatory control tear specimens from healthy volunteers (n=17) who gave informed consent. Anx-A1 protein levels were measured by ELISA and by Western blotting.

Results: In cell-free tear specimens from healthy donors, the concentration of Anx-A1 was 433.6 ± 54.3 pg/ ml (n=17) and >90% was in the intact form. In tears from VKC patients however, total Anx-A1 increased to 1908 ± 319.3pg/ml (n=23; p<0.05) but only 48% (921.5 ± 193.5 pg/ml) of this was the intact biologically active species. Proteolytic cleavage of the protein was reduced in the group treated with Alomide (>80% is intact form, n=11, p<0.01).

Conclusion: Anx-A1 is constitutively present in normal human tears and is proteolytically cleaved to inactivation during chronic allergic disease. Alomide treatment decreased the proportion of cleaved protein in VKC patients, and this is perhaps related to its therapeutic action.

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