In higher plants, a large number of isoforms for the actin monomer-binding
protein profilin have been identified, whereas other organisms express only
few profilins. Furthermore, plant profilin isoforms are expressed in a tis
sue-specific manner. These observations raise questions concerning function
al and locational differences between isoforms of plant profilins. In this
paper, we introduce three polyclonal antisera and one monoclonal antibody d
eveloped against purified pollen profilins from Zea mays and against recomb
inant maize profilin. Immunoblot analyses of native profilins and four reco
mbinant maize pollen profilin isoforms show that three of the antibodies di
splay a preference for certain isoforms. In situ immunofluorescence of poll
en of Zea mays and two developmental stages of microspores of Betula pumila
indicates that all antibodies label plasma membrane-associated domains. Th
us, we show that at least some profilin isoforms are located at a distinct
subcellular domain within developing microspores and, less distinctly, in m
ature pollen. This contrasts previously reported uniform distributions thro
ughout the cytoplasm of mature pollen and pollen tubes. The results are dis
cussed in light of the large number of profilins co-expressed in plants and
with reference to accumulating evidence for functional differences between
profilin isoforms.