Premium
Characterization of N‐cadherin messenger RNA and polypeptide expression in rat
Author(s) -
Linnemann Dorte,
Gaardsvoll Henrik,
Dalseg AnneMarie,
Zhernosekov Dmitri,
Lundgren Torben,
Edvardsen Klaus,
Bock Elisabeth
Publication year - 1994
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(94)90028-0
Subject(s) - cadherin , biology , messenger rna , microbiology and biotechnology , complementary dna , cell adhesion molecule , peptide sequence , gene , biochemistry , cell
The cell adhesion molecule N‐cadherin is a member of the cadherin gene superfamily. The protein is involved in morphogenetic processes, including neurite extension. In this study, N‐cadherin mRNA and polypeptide expression were investigated in rat brain, liver, muscle, heart, kidney and lung during postnatal development and aging. Six synthetic oligonucleotide 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 mRNA pattern differed between tissues and, furthermore, the amount of N‐cadherin mRNA and polypeptides in brain, liver and heart was higher than in muscle, kidney and lung. N‐cadherin expression decreased slightly during early postnatal development in all tissues, whereas no changes in N‐cadherin expression were observed during aging. Antibodies against a fusion protein containing the transmembrane and cytoplasmic sequence of chick N‐cadherin were produced. These antibodies, termed anti‐N‐cad‐cyt, were compared to the R‐156 antibodies which recognize the 24 C‐terminal amino acids of N‐cadherin and which have been shown to react with a broad spectrum of cadherins. Using these two antibodies, it was shown that the 130 kDa N‐cadherin polypeptide was subject to calcium‐dependent cleavage of the cytoplasmic domain. Conversely, in the absence of calcium the polypeptide was cleaved extracellularly, producing two C‐terminal fragments of 85 and 95 kDa. A 122 kDa polypeptide was recognized by both antibodies and may be either an alternatively spliced form of N‐cadherin or a closely related cadherin.