IN-VITRO INHIBITION OF THE BIOLOGICAL-ACTIVITY OF FOLLICLE-STIMULATING-HORMONE BY ANTIPEPTIDE ANTISERA REPRESENTING THE HUMAN FOLLICLE-STIMULATING-HORMONE BETA-SUBUNIT SEQUENCE-33-53
We. Westhoff et al., IN-VITRO INHIBITION OF THE BIOLOGICAL-ACTIVITY OF FOLLICLE-STIMULATING-HORMONE BY ANTIPEPTIDE ANTISERA REPRESENTING THE HUMAN FOLLICLE-STIMULATING-HORMONE BETA-SUBUNIT SEQUENCE-33-53, Biology of reproduction, 56(2), 1997, pp. 460-468
There are few male contraceptive methods, and research is required to
broaden the scope of available male antifertility methods, Two approac
hes toward hormonal contraception are currently being investigated, Th
e first relies on elimination of testosterone while the second is base
d upon immunizations against FSH. However, most anti-whole FSH antiser
a cross-react with LH, thereby possibly inhibiting testosterone and le
ading to potential loss of libido, Therefore, a more effective alterna
tive would be to define an FSH peptide that differs significantly from
LH in order to prevent cross-reactivity between anti-FSH antisera and
LH. Two peptides were selected from the beta subunit of FSH that were
considered to be inducers of anti-FSH activity but not anti-LH activi
ty. The first peptide (sequence beta 33-53) is a linear antigenic site
of human FSH found only in anti-FSH antisera that do not cross-react
with LH. The second peptide (sequence beta 81-95) is a part of FSH tha
t confers receptor specificity. These peptides, in monomer and tandem
form, were used to immunize rabbits. The antisera were tested for inhi
bition of FSH activity in a bioassay; they were also tested in a Leydi
g cell assay to detect anti-LH activity. It was found that antisera ra
ised against the beta 33-53 tandem could inhibit the FSH bioactivity b
ut not that of LH. Antisera against the beta 33-53 monomer or the beta
81-95 monomer or tandem did not inhibit FSH, Thus, the tandem peptide
beta 33-53 is an attractive candidate for use as antigen in a male co
ntraceptive vaccine, The better results obtained with tandem vaccinati
ons might be related to the ability of the tandem peptide to direct th
e antibody response toward the N-terminal end of the peptide and to ra
ise antisera with the ability to react with shorter chains of amino ac
ids.