Abstract
A cDNA encoding the mouse cartilage matrix protein (CMP) was cloned following the reverse-transcription polymerase chain reaction and rapid amplification of cDNA ends procedures using mRNA isolated from trachea. The open reading frame encodes a product of 500 amino acids. Large parts of the protein have been completely conserved when compared to chicken and human sequences, including all 12 cysteine residues of the mature CMP. In situ hybridization reveals an even distribution of the CMP mRNA in the developing skeleton, which is followed by a zonal distribution paralleling hypertrophy and calcification. From early cartilage differentiation and onwards, CMP transcript is absent in the forming articular surfaces and intervertebral discs. Extraskeletal expression of CMP mRNA was detected in the adult eye.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Bone and Bones / metabolism
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Cartilage / enzymology
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Cartilage / metabolism
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Cartilage Oligomeric Matrix Protein
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Chickens
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Cloning, Molecular
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Conserved Sequence
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DNA, Complementary / biosynthesis
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DNA, Complementary / chemistry
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DNA, Complementary / metabolism*
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Embryo, Mammalian / cytology
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Embryo, Mammalian / metabolism
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Embryo, Nonmammalian
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Extracellular Matrix Proteins*
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Gene Expression*
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Glycoproteins / analysis
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Glycoproteins / biosynthesis*
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Glycoproteins / genetics
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Humans
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In Situ Hybridization
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Matrilin Proteins
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Mice
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Molecular Sequence Data
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Oligodeoxyribonucleotides
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Open Reading Frames
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Organ Specificity
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Polymerase Chain Reaction
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RNA Probes
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Recombinant Proteins / analysis
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Recombinant Proteins / biosynthesis
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Sequence Homology, Amino Acid
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Trachea / metabolism
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Transcription, Genetic
Substances
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Cartilage Oligomeric Matrix Protein
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DNA, Complementary
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Extracellular Matrix Proteins
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Glycoproteins
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Matn1 protein, mouse
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Matrilin Proteins
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Oligodeoxyribonucleotides
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RNA Probes
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Recombinant Proteins
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TSP5 protein, human