G. Aumuller et al., DISTRIBUTION AND SUBCELLULAR-LOCALIZATION OF A LYSOSOME-ASSOCIATED PROTEIN IN HUMAN GENITAL ORGANS, Cell and tissue research, 287(2), 1997, pp. 335-342
The tissue distribution, preferentially in the human male genital syst
em, and the subcellular localization of the lysosome-associated membra
ne protein 2 (lamp 2) was studied immunohistochemically using a mouse
monoclonal antibody, 2D5. Strong immunoreactivity was present in the t
ubular system of the kidney, in acinar cells of salivary glands and pa
ncreas, prostate, mammary glands, placenta and in cutaneous sweat glan
ds. Moderate immunoreactivity was observed in cerebral neuronal cells,
epidermal cells, testis, epididymis, seminal vesicle and endometrium.
Very low immunoreactivity was found in liver. In some of the tissues
mentioned, the distribution pattern of immunoreactivity is smooth and
homogeneous, while in others it is granular and concentrated in the su
pra- or perinuclear cytoplasm. The subcellular distribution was studie
d on ultracryosections and on pre-embedding-processed chopper sections
of human prostate. In the latter gland, the protein is not restricted
to epithelium, but is also present in stromal cells. Ultrastructurall
y, the immunoreactivity in secretory cells was localized in electron-t
ranslucent vacuoles and granules, including the secretory granules. A
close association with cell membranes was not generally the case. Only
part of the immunoreactive material was linked to the apical plasma m
embrane pointing to a biosynthesis independent from an association ste
p with the apical plasma membrane. As shown by immunoelectron microsco
py and Western blotting, a high amount of lamp 2 is secreted and is fo
und in so-called prostasomes. The findings indicate that in the human
prostate most of the membrane-bound lamp 2 is released from the secret
ory cells, presumably in an apocrine fashion.