Acetylated alpha tubulin is reduced in individuals with poor sperm motility

This study establishes association of acetyl a-tubulin with asthenozoospermia, suggests the isoforms determining the acetylation, and provides insight into potential mechanism of transcriptional regulation of a-tubulin isoforms.


Shweta Bhagwat, M.Sc., Veena Dalvi, M.Sc., Darshan Chandrashekar, M.Sc., Tinsu Matthew, M.Sc., Kshitish Acharya, Ph.D., Rahul Gajbhiye, M.B.B.S., Vijay Kulkarni, M.S., Shobha Sonawane, M.Sc., Manish Ghosalkar, B.Sc., Priyanka Parte, Ph.D.

Volume 101, Issue 1, Pages 95-104.e3, January 2014



To determine the status of α-tubulin acetylation and of testis-specific acetylable α-tubulin isoforms in asthenozoospermia.


Research study.


Research institute and an infertility clinic.


50 men with normal sperm parameters, and 50 men with asthenozoospermia.



Main Outcome Measure(s):

Western blot analyses of α-tubulin, acetylated α-tubulin, and isoforms TUBA3C, TUBA4A, and TUBA8 in Percoll separated sperm and flow cytometry, real-time reverse-transcription polymerase chain reaction, and immunofluorescent localization.


A statistically significant decrease in the expression of acetylated α-tubulin in asthenozoosperm was seen with Western blot analysis, double immunostaining by direct immunofluorescence, and flow cytometric analysis. The transcript and protein of testis-specific acetylable α-tubulin isoform TUBA3C was decreased and TUBA4A was statistically significantly increased in asthenozoosperm as compared with normal spermatozoa. TUBA8 was reduced in asthenozoosperm. Similar observations were noted by indirect immunofluorescent localization. The potential transcription factors involved in the differential expression of TUBA4A and TUBA3C have been identified.


Data suggest an association of α-tubulin acetylation with asthenozoospermia. Ours is the first report to demonstrate α-tubulin isoforms in sperm, implicating their role in motility. The differential expression of TUBA3C and TUBA4A suggests that tubulin acetylation may be governed by the isoform of α-tubulin that is expressed or silenced and that this in turn is transcriptionally controlled.

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