Transcripts encoding the sperm surface protein tMDC II are non-functional in the human.
Five members of the MDC (metalloproteinase-like,disintegrin-like cysteine-rich domain) family of proteins (fertilin alpha, fertilin beta, tMDC I, tMDC II and tMDC III) are expressed on the surface of macaque (Macaca fascicularis) sperm, where they have been proposed to play a role in sperm-egg binding via an interaction between their disintegrin-like domain and one or more integrins on the egg plasma membrane. Of these, two (fertilin alpha and tMDC I) have recently been shown to be non-functional in the human. Here we report the existence of multiple isoforms of human tMDC II transcripts in the human, all of which are also non-functional owing to the presence of deletions and in-frame termination codons, when compared with the macaque orthologue, a finding which is further supported by the lack of immunoreactivity on Western blots of human testis and sperm extracts probed with a macaque anti-tMDC II polyclonal antiserum. These results are discussed in the context of our proposed model for multiple proteins implicated in sperm-egg interactions.
Department of Biochemistry, University of Bristol, School of Medical Sciences, Bristol BS8 1TD, U.K.
J
J
Frayne
E A
EA
Dimsey
J A
JA
Jury
L
L
Hall
D051722:ADAM Proteins; D000595:Amino Acid Sequence; D015153:Blotting, Western; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D011506:Proteins / Q000235:genetics*; D012326:RNA Splicing; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013094:Spermatozoa / Q000378:metabolism*
D011506:Proteins; D012333:RNA, Messenger; D051722:ADAM Proteins