
pmid: 2169760
Based on the concept of sequence conservation around the active sites of serine proteinases, polymerase chain reaction applied to mRNA amplification allowed us to obtain a 260-bp probe which was used to screen a mouse pituitary cDNA library. The primers used derived from the cDNA sequence of active sites Ser* and Asn* of human furin. Two cDNA sequences were obtained from a number of positive clones. These code for two similar but distinct structures (mPC1 and mPC2), each being homologous to yeast Kex2 and human furin. In situ hybridization (mPC1) and Northern blots (mPC1 = 3.0 kb and mPC2 = 2.8 and 4.8 kb) demonstrated tissue and cellular specificity of expression, only within endocrine and neuroendocrine cells. These data suggest that mPC1 and mPC2 represent prime candidates for tissue-specific pro-hormone converting proteinases.
Furin, Saccharomyces cerevisiae Proteins, Base Sequence, Molecular Sequence Data, Blotting, Northern, Polymerase Chain Reaction, Mice, Pituitary Hormones, Proprotein Convertase 2, Proprotein Convertase 1, Organ Specificity, Pituitary Gland, Endopeptidases, Animals, Humans, Nucleic Acid Conformation, Amino Acid Sequence, Proprotein Convertases, RNA, Messenger, Protein Processing, Post-Translational
Furin, Saccharomyces cerevisiae Proteins, Base Sequence, Molecular Sequence Data, Blotting, Northern, Polymerase Chain Reaction, Mice, Pituitary Hormones, Proprotein Convertase 2, Proprotein Convertase 1, Organ Specificity, Pituitary Gland, Endopeptidases, Animals, Humans, Nucleic Acid Conformation, Amino Acid Sequence, Proprotein Convertases, RNA, Messenger, Protein Processing, Post-Translational
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