TY - JOUR
T1 - MUC1 in normal and impaired spermatogenesis
AU - Franke, Folker E.
AU - Kraus, Sigurd
AU - Eiermann, Claus
AU - Pauls, Katharina
AU - Lalani, El Nasir
AU - Bergmann, Martin
PY - 2001
Y1 - 2001
N2 - The MUC1 mucin [also known as episialin, epithelial membrane antigen (EMA) or polymorphic epithelial mucin (PEM)] is a component of the mucosal glycocalyx, contributing to anti-adhesive and protective cell functions. MUC1 has been shown in a variety of epithelial cell types in the reproductive tracts of males and females, but this is the first report of its expression in human testis and non-epithelial cells of the germ cell lineage. Analysing 65 testes with normal or impaired spermatogenesis, we identified MUC1 protein in maturing germ cells by immunohistochemistry using the monoclonal antibodies HMFG1, HMFG2 and SM3 binding to different glycosylation variants. MUC1 expression was confirmed by reverse transcription-polymerase chain reaction (RT-PCR) and Western blot analysis on tissue extracts of human testis, and RT-PCR of selected germ cells after UV laser-assisted cell picking. MUC1 glycosylation variants were selectively distributed during normal spermatogenesis. Whereas HMFG1 labelled certain groups of pachytene spermatocytes, HMFG2 labelled only spermatids. Low glycosylated forms of MUC1 mucin, recognized by SM3, were not found. In contrast to its weak expression during normal spermatogenesis, the HMFG1 glycosylation variant accumulated markedly in all spermatocytes showing abnormal or arrested maturation. These results suggest a variable glycosylation of MUC1 mucin in differentiating germ cells, which is aberrant in pathological conditions.
AB - The MUC1 mucin [also known as episialin, epithelial membrane antigen (EMA) or polymorphic epithelial mucin (PEM)] is a component of the mucosal glycocalyx, contributing to anti-adhesive and protective cell functions. MUC1 has been shown in a variety of epithelial cell types in the reproductive tracts of males and females, but this is the first report of its expression in human testis and non-epithelial cells of the germ cell lineage. Analysing 65 testes with normal or impaired spermatogenesis, we identified MUC1 protein in maturing germ cells by immunohistochemistry using the monoclonal antibodies HMFG1, HMFG2 and SM3 binding to different glycosylation variants. MUC1 expression was confirmed by reverse transcription-polymerase chain reaction (RT-PCR) and Western blot analysis on tissue extracts of human testis, and RT-PCR of selected germ cells after UV laser-assisted cell picking. MUC1 glycosylation variants were selectively distributed during normal spermatogenesis. Whereas HMFG1 labelled certain groups of pachytene spermatocytes, HMFG2 labelled only spermatids. Low glycosylated forms of MUC1 mucin, recognized by SM3, were not found. In contrast to its weak expression during normal spermatogenesis, the HMFG1 glycosylation variant accumulated markedly in all spermatocytes showing abnormal or arrested maturation. These results suggest a variable glycosylation of MUC1 mucin in differentiating germ cells, which is aberrant in pathological conditions.
KW - Immunohistochemistry
KW - MUC1
KW - Mucins
KW - RT-PCR
KW - Spermatogenesis
UR - http://www.scopus.com/inward/record.url?scp=0034965652&partnerID=8YFLogxK
U2 - 10.1093/molehr/7.6.505
DO - 10.1093/molehr/7.6.505
M3 - Article
C2 - 11385106
AN - SCOPUS:0034965652
SN - 1360-9947
VL - 7
SP - 505
EP - 512
JO - Molecular Human Reproduction
JF - Molecular Human Reproduction
IS - 6
ER -