Ala-Kokko L, Baldwin C T, Moskowitz R W, Prockop D J
Department of Biochemistry and Molecular Biology, Jefferson Medical College, Thomas Jefferson University, Philadelphia, PA 19107-6799.
Proc Natl Acad Sci U S A. 1990 Sep;87(17):6565-8. doi: 10.1073/pnas.87.17.6565.
A cosmid clone was isolated that contained an allele for the type II procollagen gene previously shown to be coinherited with primary generalized osteoarthritis in a large family. Affected members of the family had evidence of a mild chondrodysplasia, but they developed progressive osteoarthritic changes in many joints that had no epiphyseal deformities. The clone contained 52 of the 54 exons of the gene. Nucleotide sequencing of greater than 20,000 base pairs from the clone demonstrated that all the coding sequences and all the intron-exon boundaries were normal except for a single base mutation that converted the codon for arginine at position 519 of the alpha 1(II) chain to a codon for cysteine, an amino acid not found in type II collagen from humans or a variety of other species. The mutation was found in all affected members of the family but not in unaffected members or in 57 unrelated individuals.
分离出一个黏粒克隆,它含有II型原胶原基因的一个等位基因,此前在一个大家庭中已表明该等位基因与原发性全身性骨关节炎共同遗传。该家族的患病成员有轻度软骨发育不良的证据,但他们在许多没有骨骺畸形的关节中出现了进行性骨关节炎变化。该克隆包含该基因54个外显子中的52个。对来自该克隆的超过20,000个碱基对进行核苷酸测序表明,除了一个单碱基突变外,所有编码序列和所有内含子-外显子边界均正常,该突变将α1(II)链第519位的精氨酸密码子转换为半胱氨酸密码子,半胱氨酸是在人类或多种其他物种的II型胶原中未发现的一种氨基酸。该突变在该家族的所有患病成员中都存在,但在未患病成员或57名无关个体中未发现。