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Unique alternative translation from two open reading frames on Acpin1 mRNA yields an acrosomal protein and a salivary‐gland‐specific protein
Author(s) -
Ueda Tomohiro,
Manabe Hiroyuki,
Tokuhiro Keizo,
Hirose Mika,
Matsuoka Yasuhiro,
Miyagawa Yasushi,
Tsujimura Akira,
Fujita Kyoko,
Wada Morimasa,
Okuyama Akihiko,
Nishimune Yoshitake,
Tanaka Hiromitsu
Publication year - 2009
Publication title -
international journal of urology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.172
H-Index - 67
eISSN - 1442-2042
pISSN - 0919-8172
DOI - 10.1111/j.1442-2042.2009.02325.x
Subject(s) - open reading frame , orfs , gene , messenger rna , alternative splicing , homology (biology) , biology , microbiology and biotechnology , genetics , germline , exon , peptide sequence
Objective: To examine the expression profiles of the proteins translated from Acpin1 mRNA in germ cells. Methods: Northern and western blotting of various tissues and immunohistochemical analysis of germ cells were carried out in a mouse model. Results: ACPIN1 protein was transcribed from the longer, 3′ open reading frame (ORF) of Acpin1. An alternative‐splicing variant, Acpin1vs , contained only the smaller, 5′ ORF of the full‐length Acpin1 gene. Its gene product, SAGSIN1, was expressed specifically in salivary glands. Retrotransposed regions of Acpin1 homology were also detected in various chromosomes, and intronless paralogous genes on the X chromosome were expressed in the testis and other tissues. The genomic structure of Acpin1 is highly conserved in mammals. Conclusion: The two ORFs on the Acpin1 mRNA are independently translated in differentiated cells. Analysis of gene Acpin1 might clarify the molecular mechanism of spermatogenesis.