THE ROLE OF COLLAGEN CROSSLINKING IN THE INCREASED STIFFNESS OF AVIAN DYSTROPHIC MUSCLE
THE ROLE OF COLLAGEN CROSSLINKING IN THE INCREASED STIFFNESS OF AVIAN DYSTROPHIC MUSCLE
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DOI：
10.1002/mus.880120609
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发表时间：
1989-06-01
期刊：
影响因子：
3.4
通讯作者：
MOSTAFAPOUR, AS
中科院分区：
文献类型：
--
作者：
FEIT, H;KAWAI, M;MOSTAFAPOUR, AS
在高度近交的正常和营养不良的鸡胸肌束中研究了肌节长度2.4 - 3.6 μ m范围内的静息张力和刚度，并将结果与胶原蛋白含量和胶原蛋白的交联程度进行比较。所有参数均按正常纯合子（003/003）<杂合子（003/433）<营养不良纯合子（433/433）的顺序增加，杂合子的数据介于两个纯合子之间，因此表现出半显性遗传模式。在单独的实验中，通过用α-羟色胺处理正常（412/412）和营养不良（413/413）鸡来诱导山莴苣中毒。乙酰氨基腈，赖氨酰氧化酶的抑制剂，赖氨酰氧化酶负责引发胶原交联形成。这些实验表明，在被动拉伸的张力和刚度并没有改变正常肌肉的lathyrism，而张力和刚度显着降低lathyrism在营养不良的肌肉。胶原蛋白含量没有改变，在正常和营养不良的肌肉与lathyrism。这些结果表明，胶原交联含量的增加是鸡的营养不良肌肉中的静息张力和刚度增加的基础，并且该作用可以通过用胶原交联形成的抑制剂处理来逆转。
The resting tension and stiffness in the range of sarcomere lengths 2.4-3.6 .mu.m were studied in highly inbred normal and dystrophic chicken pectoral muscle bundles, and the results were compared with the collagen content and the extent of crosslinkage of the collagen. All parameters increased in the order normal homozygote (003/003) < heterozygote (003/433) < dystrophic homozygote (433/433) chickens, with the data from the heterozygotes being halfway between the two homozygotes, thus exhibiting a semidominant inheritance pattern. In separate experiments, lathyrism was induced by treating normal (412/412) and dystrophic (413/413) chickens with .alpha.-acetoaminonitrile, an inhibitor of lysyl oxidase, the enzyme responsible for the initiation of collagen crosslinkage formation. These experiments showed that the tension and stiffness in response to passive stretch did not change with lathyrism in normal muscles, whereas the tension and stiffness decreased significantly with lathyrism in dystrophic muscles. The collagen content did not change with lathyrism in both normal and dystrophic muscles. These results indicate that the increased content of collagen crosslinkages is the basis for the increased resting tension and stiffness in the dystrophic muscles of the chicken, and that the effects can be reversed by treatment with an inhibitor of collagen crosslinkage formation.