Aj. North et al., DISTINCT DESMOCOLLIN ISOFORMS OCCUR IN THE SAME DESMOSOMES AND SHOW RECIPROCALLY GRADED DISTRIBUTIONS IN BOVINE NASAL EPIDERMIS, Proceedings of the National Academy of Sciences of the United Statesof America, 93(15), 1996, pp. 7701-7705
The adhesive core of the desmosome is composed of cadherin like glycop
roteins of two families, desmocollins and desmogleins. Three isoforms
of each are expressed in a tissue-specific and developmentally regulat
ed pattern. In bovine nasal epidermis, the three desmocollin (Dsc) iso
forms are expressed in overlapping domains; Dsc3 expression is stronge
st in the basal layer, while Dsc2 and Dsc1 are strongly expressed in t
he suprabasal layers. Herein we have investigated whether different is
oforms are assembled into the same or distinct desmosomes by performin
g double immunogold labeling using isoform-specific antibodies directe
d against Dsc1 and Dsc3. The results show that individual desmosomes h
arbor both isoforms in regions where their expression territories over
lap, Quantification showed that the ratio of the proteins in each desm
osome altered gradually from basal to immediately suprabasal and upper
suprabasal layers, labeling for Dsc1 increasing acid Dsc3 decreasing.
Thus desmosomes are constantly modified as cells move up the epidermi
s, with continuing turnover of the desmosomal glycoproteins. Statistic
al analysis of the quantitative data showed a possible relationship be
tween the distributions of the two isoforms. This gradual change in de
smosomal composition may constitute a vertical adhesive gradient withi
n the epidermis, having important consequences for cell positioning an
d differentiation.