Study of the expression of myelin proteolipid protein (lipophilin) using a cloned complementary DNA | Zendy

Angela Naismith | Zendy; E. Hoffman-Chudzik | Zendy; L.-C. Tsui | Zendy; J.R. Riordan | Zendy

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Study of the expression of myelin proteolipid protein (lipophilin) using a cloned complementary DNA

Author(s) -

Angela Naismith,

E. Hoffman-Chudzik,

L.-C. Tsui,

J.R. Riordan

Publication year - 1985

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/13.20.7413

Subject(s) - proteolipid protein 1 , biology , complementary dna , myelin proteolipid protein , myelin , microbiology and biotechnology , cdna library , messenger rna , myelin basic protein , oligonucleotide , peptide sequence , untranslated region , dna , biochemistry , gene , central nervous system , neuroscience

We have prepared a lambda gt10 cDNA library with the mRNA isolated from fetal calf brains which were actively myelinating. Using two oligonucleotides made according to the known amino acid sequence of myelin proteolipid protein (PLP or lipophilin), we have isolated several cDNA clones for this major intrinsic membrane protein of myelin. One of these clones, designated as pLP1, is found to contain 444 bp of coding sequence for the C-terminal half of PLP and 486 bp of 3' untranslated sequence. Using pLP1 as a hybridization probe, we have studied the regulation of PLP at the mRNA level during rat brain development. Our results show that the relative amounts of mRNA for PLP and that for the major extrinsic protein of the myelin membrane, myelin basic protein, increase coordinately during the course of myelination in the brain.

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