Valosine-containing proteins (VCP ) in an annelid: Identification of a novel spermatogenesis related factor

• Published in: Gene 2005-12, Vol.362, p.11-18
• Main Authors: Suzuki, Tomoharu, Honda, Makoto, Matsumoto, Seiji, Stürzenbaum, Stephen R., Gamou, Shinobu
• Format: Article
• Language: English
• Subjects: AAA protein family; Adenosine Triphosphatases; Amino Acid Sequence; Animals; Annelida; Cell Cycle Proteins - genetics; Cell Cycle Proteins - isolation & purification; Cell Cycle Proteins - metabolism; Cell Cycle Proteins - physiology; Earthworm; Eisenia fetida; Male; Molecular Sequence Data; Oligochaeta - genetics; Phylogeny; Seminal vesicle; Seminal Vesicles - metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Spermatogenesis - genetics; Valosin Containing Protein
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/j.gene.2005.07.039

Two cDNAs similar to mammalian valosine-containing proteins (VCPs) were isolated from the common lumbricid earthworm Eisenia fetida (Savigny, 1826). The primary sequences, referred to as eVCP-1 and eVCP-2, display a similarity of 74%. Despite of the variable C-termini, both eVCPs have a conserved intron/exon organization spanning 14 kb, which is also conserved to their mammalian counterparts. Although this finding strongly suggests VCPs have a common ancestral origin, phylogenetic analysis predicts that eVCP-2 may be distinct. An investigation by reverse transcription-polymerase chain reaction (RT-PCR) revealed that, whilst evcp-1 was ubiquitously expressed during all developmental stages, evcp-2 was specifically expressed in the anterior segments of sexually mature earthworms. In situ hybridization clearly demonstrated that evcp-2 is expressed in the seminal vesicles, the location of spermatogenesis, and more precisely within the cytophores surrounded by secondary spermatocytes or spermatids. Taken together, this evidence leads to the notion that eVCP-2 is a likely component involved in the final modulation of spermatogenesis.