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Immunohistochemical analysis of paraoxonase-1,2 and 3 expression in normal mouse tissues

Centre de Recerca Biomèdica, Hospital Universitari de Sant Joan, Institut d'Investigacions Sanitàries Pere Virgili, Universitat Rovira i Virgili, Reus, Spain.
Free Radical Biology and Medicine (Impact Factor: 5.71). 08/2008; 45(2):146-57. DOI: 10.1016/j.freeradbiomed.2008.03.023
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ABSTRACT The paraoxonase (PON) enzyme family, comprising PON1, PON2, and PON3, are antioxidant enzymes that degrade oxidised phospholipids. We describe the immunohistochemical localisation of the PON proteins in the normal mouse. Antibodies were obtained by inoculating rabbits with peptides derived from specific sequences of mature PONs. PON1 and PON3 were detected in the skin external epithelium, acini of the sebaceous glands, tongue epithelium, acini of the submandibular gland, surface epithelia of the stomach and the intestine, hepatocytes, exocrine pancreas acini, fibre tracts of the encephalon and the spinal cord, skeletal and cardiac muscle, eye lens epithelium and retinal layers, adipocytes, chondrocytes, epithelial cells of the trachea and bronchiole, ovary follicular fluid, seminiferous tubules, spermatozoa, and kidney proximal tubules. PON2 expression was weaker than that of PON1 and PON3, and was absent in some of the tissues studied, such as submandibular gland, nerve cells, and adipocytes. In muscle cells, PON2 expression was restricted to the endomysium. Apolipoprotein A-I did not colocalise with PONs, suggesting local synthesis. This study provides an experimental model to investigate the role played by these enzymes as antioxidants and their relationship with the development of a variety of diseases.

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    • "The signal at 55 kDa (Tubulin) demonstrates that comparable amounts of protein were used. Since PON2 is known to be expressed regularly in nearly all organs and tissues in mice (except submandibular gland, nerve cells and adipocytes), a regular expression in human OSCC cells was anticipated (Marsillach et al. 2008). Hence, a quantitative analysis of the actual PON2 amount in the different cell lines normalized to Tubulin was of interest. "
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    • "As P1 has the highest sperm concentration while P3 has the lowest (Saravia et al., 2009), there seems to be a relationship between the sperm numbers and SP-PON-1 activity, which is difficult to demonstrated from the results of this study. However, that P1 have the highest levels of SP-PON-1 could indicate a testicular or epididymal origin of the enzyme, considering the P1 spermatozoa bathe in an epididymal tail-dominating fluid, barely mixed with prostatic secretions (Saravia et al., 2009) and by a high PON-1 synthesis was found in the seminiferous tubules in mice (Marsillach et al., 2008). Spermatozoa in P1 better sustain several biotechnological procedures, such as liquid storage and freezing–thawing, than those contained in the rest of SRF (P2) and post-spermatic fraction (P3) (Pe~ na et al., 2006; Saravia et al., 2010; Siqueira et al., 2011). "
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    • "Molecular Reproduction & Development Marsillach et al . ( 2008 ) first immunohistochemically localised the PON proteins ( including PON - 1 , - 2 , and - 3 ) in mouse testis to spermatogonia , spermatocytes , and round and elongated spermatids . We extended these findings , and found PON - 2 enriched in the post - acroso - mal region of ejaculated boar spermatozoa . PON - 2 is considered a cytoplas"
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