The distribution of type IV collagen alpha chains in the mouse ovary and its correlation with follicular development.

The present study aims to identify alpha chains of type IV collagen in the basement membrane of the mouse ovarian follicle and examine their changes during follicular development using immunofluorescence microscopy with specific monoclonal antibodies. The basement membrane of the serous mesothelium enveloping the ovary contained all alpha chains of type IV collagen, alpha1(IV) through alpha6(IV) chains. Primordial follicles showed a distinct immunoreactivity against all six alpha chains in their basement membranes. Immunolabeling for alpha3(IV) and alpha4(IV) chains was almost eliminated in the primary follicles. In basement membranes of secondary and Graafian follicles, the immunofluorescent reaction of alpha3(IV) and alpha4(IV) chains disappeared in Graafian follicles, a partial reduction in fluorescent immunostaining intensity to alpha5(IV) and alpha6(IV) chains was observed; only alpha1(IV) and alpha2(IV) chains were not degraded throughout follicular development. On atretic follicles, in addition to alpha1(IV) and alpha2(IV) chains, alpha3(IV), alpha4(IV), alpha5(IV) and alpha6(IV) chains frequently persisted. A basement membrane-like matrix within the follicular granulosa cell layer, such as the focimatrix (focal intraepithelial matrix) and/or Call-Exner body, was also recognized in mouse secondary and Graafian follicles and contained alpha1(IV), alpha2(IV), alpha5(IV) and alpha6(IV) chains but not alpha3(IV) and alpha4(IV) chains. We expect that the decrease in alpha(IV) chains prompts follicular development and is a prerequisite condition for follicular maturation.