Thyroid functions of mouse cathepsins B, K, and L
J. Clin. Invest. Bianca Friedrichs, et al. 111:1733 doi:10.1172/JCI15990 [
Go to this article.]

Figure 2Localization of cathepsins K and L. Confocal fluorescence micrographs of cryosections of thyroid glands from WT mice (+/+) or cathepsin-deficient mice of the indicated genotypes were immunolabeled with antibodies against cathepsin K (
a–
c) or cathepsin L (
d–
f). Compared with the WT (
a, inset, arrows), cathepsin K–positive vesicles were smaller in cathepsin
B–/– (
b, top inset, arrows) and larger in cathepsin
L–/– thyroid epithelial cells (
c, inset, arrows). Cathepsin K was absent from thyroid follicle lumina of cathepsin
B–/– mice but was detectable within lumina of WT or cathepsin
L–/– thyroids (asterisks). Immunolabeling of cathepsin K was also observed at the apical plasma membrane of cathepsin
B–/– thyroid epithelial cells (
b, bottom inset, arrowheads). In addition, cathepsin K–positive inclusions were frequently detected within the luminal content of cathepsin
L–/– mice (
c, open circles). In WT mice, cathepsin L was detected mainly within endocytic vesicles (
d, arrows) and, in a few follicles, in association with the apical plasma membrane of thyroid epithelial cells (
d and inset in
d, arrowheads). Deficiencies in cathepsin B and/or cathepsin K demonstrated a lack of cathepsin L at the apical plasma membrane and resulted in an enhancement of immunolabeling of thyroid follicle lumina (
e and
f, asterisks). The redistribution of cathepsin L was less obvious than that of cathepsin B (compare with Figure
1). Bars: 50 μm; in insets: 20 μm.