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Characterization of NADPH oxidase 5 in equine testis and spermatozoa.
Reproduction 2007; 134(2):263-70R

Abstract

Reactive oxygen species (ROS) play an important role in normal sperm function, and spermatozoa possess specific mechanisms for ROS generation via an NAD(P)H-dependent oxidase. The aim of this study was to identify the presence of an NADPH oxidase 5 (NOX5) in equine testis and spermatozoa. The mRNA of NOX5 was expressed in equine testis as detected by northern blot probed with human NOX5 cDNA and by RT-PCR. Immunoblotting with affinity purified alpha-NOX5 revealed one major protein in equine testis and other tissues. Immunolocalization of NOX5 showed labeling over the rostral sperm head with some labeling in the equatorial and post-acrosomal regions. In the testis, there was abundant staining in the adluminal region of the seminiferous tubules associated with round and elongating spermatids. The RT-PCR and sequence analysis revealed a high homology with human NOX5. This study demonstrates that NOX5 is present in equine spermatozoa and testes and therefore represents a potential mechanism for ROS generation in equine spermatozoa.

Authors+Show Affiliations

Department of Population Health and Reproduction, University of California, Davis, California 95616, USA.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

17660236

Citation

Sabeur, K, and B A. Ball. "Characterization of NADPH Oxidase 5 in Equine Testis and Spermatozoa." Reproduction (Cambridge, England), vol. 134, no. 2, 2007, pp. 263-70.
Sabeur K, Ball BA. Characterization of NADPH oxidase 5 in equine testis and spermatozoa. Reproduction. 2007;134(2):263-70.
Sabeur, K., & Ball, B. A. (2007). Characterization of NADPH oxidase 5 in equine testis and spermatozoa. Reproduction (Cambridge, England), 134(2), pp. 263-70.
Sabeur K, Ball BA. Characterization of NADPH Oxidase 5 in Equine Testis and Spermatozoa. Reproduction. 2007;134(2):263-70. PubMed PMID: 17660236.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Characterization of NADPH oxidase 5 in equine testis and spermatozoa. AU - Sabeur,K, AU - Ball,B A, PY - 2007/7/31/pubmed PY - 2007/12/6/medline PY - 2007/7/31/entrez SP - 263 EP - 70 JF - Reproduction (Cambridge, England) JO - Reproduction VL - 134 IS - 2 N2 - Reactive oxygen species (ROS) play an important role in normal sperm function, and spermatozoa possess specific mechanisms for ROS generation via an NAD(P)H-dependent oxidase. The aim of this study was to identify the presence of an NADPH oxidase 5 (NOX5) in equine testis and spermatozoa. The mRNA of NOX5 was expressed in equine testis as detected by northern blot probed with human NOX5 cDNA and by RT-PCR. Immunoblotting with affinity purified alpha-NOX5 revealed one major protein in equine testis and other tissues. Immunolocalization of NOX5 showed labeling over the rostral sperm head with some labeling in the equatorial and post-acrosomal regions. In the testis, there was abundant staining in the adluminal region of the seminiferous tubules associated with round and elongating spermatids. The RT-PCR and sequence analysis revealed a high homology with human NOX5. This study demonstrates that NOX5 is present in equine spermatozoa and testes and therefore represents a potential mechanism for ROS generation in equine spermatozoa. SN - 1470-1626 UR - https://www.unboundmedicine.com/medline/citation/17660236/Characterization_of_NADPH_oxidase_5_in_equine_testis_and_spermatozoa_ L2 - https://rep.bioscientifica.com/doi/10.1530/REP-06-0120 DB - PRIME DP - Unbound Medicine ER -