D. Linnemann et al., CHARACTERIZATION OF N-CADHERIN MESSENGER-RNA AND POLYPEPTIDE EXPRESSION IN RAT, International journal of developmental neuroscience, 12(5), 1994, pp. 441-450
The cell adhesion molecule N-cadherin is a member of the cadherin gene
superfamily. The protein is involved in morphogenetic processes, incl
uding neurite extension. In this study, N-cadherin mRNA and polypeptid
e expression were investigated in rat brain, liver, muscle, heart, kid
ney and lung during postnatal development and aging. Six synthetic oli
gonucleotide probes covering different parts of mouse N-cadherin cDNA
all hybridized to 5.2, 4.3-4.4 and 3.5 kb mRNAs in rat tissues. The mR
NA pattern differed between tissues and, furthermore, the amount of N-
cadherin mRNA and polypeptides in brain, liver and heart was higher th
an in muscle, kidney and lung. N-cadherin expression decreased slightl
y during early postnatal development in all tissues, whereas no change
s in N-cadherin expression were observed during aging. Antibodies agai
nst a fusion protein containing the transmembrane and cytoplasmic sequ
ence of chick N-cadherin were produced. These antibodies, termed anti-
N-cad-cyt, were compared to the R-156 antibodies which recognize the 2
4 C-terminal amino acids of N-cadherin and which have been shown to re
act with a broad spectrum of cadherins. Using these two antibodies, it
was shown that the 130 kDa N-cadherin polypeptide was subject to calc
ium-dependent cleavage of the cytoplasmic domain. Conversely, in the a
bsence of calcium the polypeptide was cleaved extracellularly, produci
ng two C-terminal fragments of 85 and 95 kDa. A 122 kDa polypeptide wa
s recognized by both antibodies and may be either an alternatively spl
iced form of N-cadherin or a closely related cadherin.