Molecular cloning of PARP (proline/arginine-rich protein) from human cartilage and subsequent demonstration that PARP is a fragment of the NH2-terminal domain of the collagen alpha 2(XI) chain.
We report the molecular cloning of a proline/arginine-rich protein (called PARP) from human cartilage using the polymerase chain reaction (PCR) and degenerate oligonucleotides based on the previously published amino acid sequence of bovine PARP [1]. Subsequently, a reverse transcription-polymerase chain reaction (RT-PCR) was performed with poly(A)-rich RNA from human cartilage using a sense oligonucleotide derived from PARP and an anti-sense oligonucleotide derived from the known sequence of the human collagen alpha 2(XI) chain [2]. Nucleotide sequencing of the PCR product demonstrated that PARP is a fragment of the NH2-terminal non-collagenous (NC3) domain of the collagen alpha 2(XI) chain.
Zhidkova
N I
NI
Department of Cell Biology, University of Alabama, Birmingham 35294.
Brewton
R G
RG
Mayne
R
R
D000595:Amino Acid Sequence; D001483:Base Sequence; D002356:Cartilage / Q000737:chemistry*; D002648:Child; D003001:Cloning, Molecular; D003094:Collagen / Q000737:chemistry*; D024161:Collagen Type XI; D005260:Female; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
C499319:COL11A2 protein, human; D024161:Collagen Type XI; C066455:PARP protein, Bos taurus; D010446:Peptide Fragments; D011506:Proteins; D003094:Collagen