Abstract
The members of the ADAM (a disintegrin and metalloprotease) family are membrane-anchored multi-domain proteins that play prominent roles in male reproduction. ADAM2, which was one of the first identified ADAMs, is the best studied ADAM in reproduction. In the male germ cells of mice, ADAM2 and other ADAMs form complexes that contribute to sperm-sperm adhesion, sperm-egg interactions, and the migration of sperm in the female reproductive tract. Here, we generated specific antibodies against mouse and human ADAM2, and investigated various features of ADAM2 in mice, monkeys and humans. We found that the cytoplasmic domain of ADAM2 might enable the differential association of this protein with other ADAMs in mice. Western blot analysis with the anti-human ADAM2 antibodies showed that ADAM2 is present in the testis and sperm of monkeys. Monkey ADAM2 was found to associate with chaperone proteins in testis. In humans, we identified ADAM2 as a 100-kDa protein in the testis, but failed to detect it in sperm. This is surprising given the results in mice and monkeys, but it is consistent with the failure of ADAM2 identification in the previous proteomic analyses of human sperm. These findings suggest that the reproductive functions of ADAM2 differ between humans and mice. Our protein analysis showed the presence of potential ADAM2 complexes involving yet-unknown proteins in human testis. Taken together, our results provide new information regarding the characteristics of ADAM2 in mammalian species, including humans.
Highlights
The a disintegrin and metalloprotease domain-containing protein (ADAM) family includes membrane-anchored proteins that share a conserved multidomain structure comprising an Nterminal signal sequence, a pro-domain, and metalloprotease, disintegrin, cysteine-rich, epidermal growth factor (EGF)-like, transmembrane, and cytoplasmic tail domains
We found a relationship between the differential types of ADAM2 complex formation and a change in the cytoplasmic domain in mice
We investigated and characterized mouse, monkey, and human ADAM2 proteins
Summary
The a disintegrin and metalloprotease domain-containing protein (ADAM) family includes membrane-anchored proteins that share a conserved multidomain structure comprising an Nterminal signal sequence, a pro-domain, and metalloprotease, disintegrin, cysteine-rich, epidermal growth factor (EGF)-like, transmembrane, and cytoplasmic tail domains. The ADAM family members are widely distributed in different species and are present in a variety of tissues. At least 34 and 26 ADAM genes have been identified in mice and humans, respectively. More than half of the ADAM genes are known to be expressed exclusively or predominantly in mammalian male reproductive tissues, such as the testis or epididymis [1].
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