Andrikopoulos K, Liu X, Keene D R, Jaenisch R, Ramirez F
Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, New York 10029.
Nat Genet. 1995 Jan;9(1):31-6. doi: 10.1038/ng0195-31.
The tissue-specific organization of collagen molecules into tridimensional macroaggregates determines the physiomechanical properties of most connective tissues, but the factors and mechanisms controlling this process are unknown. It has been postulated that quantitatively minor types V and XI collagen regulate the growth of type I and II collagen fibrils, respectively. To test this hypothesis, we created mice that produce a structurally abnormal alpha 2(V) collagen chain. Homozygous mutant mice survive poorly, possibly because of complications from spinal deformities, and exhibit skin and eye abnormalities caused by disorganized type I collagen fibrils. Our results demonstrate that type V collagen is a key determinant in the assembly of tissue-specific matrices, and provide an animal model for human connective tissue disorders.
胶原蛋白分子组织成三维大聚集体的组织特异性决定了大多数结缔组织的生理力学特性，但控制这一过程的因素和机制尚不清楚。据推测，数量较少的V型和XI型胶原蛋白分别调节I型和II型胶原纤维的生长。为了验证这一假设，我们培育出了产生结构异常的α2(V)胶原链的小鼠。纯合突变小鼠存活能力较差，可能是由于脊柱畸形的并发症所致，并且表现出由紊乱的I型胶原纤维引起的皮肤和眼睛异常。我们的结果表明，V型胶原蛋白是组织特异性基质组装的关键决定因素，并为人类结缔组织疾病提供了一个动物模型。
