Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits
Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits
复制标题
鸡肌腱抗原。
DOI:
--
复制
发表时间:
1984
影响因子:
7.8
通讯作者:
D. Fambrough
中科院分区:
文献类型:
--
作者:
M. Chiquet;D. Fambrough
This report describes the biochemical characterization of a novel extracellular matrix component, " myotendinous antigen," which appears early in chick limb morphogenesis at sites connecting developing muscle fibers, tendons, and bone ( Chiquet , M., and D. Fambrough , 1984; J. Cell Biol., 98:1926-1936). This extracellular matrix antigen is a major component of the secretory proteins released into the medium by fibroblast and muscle cultures; the soluble form is characterized here. This form of myotendinous antigen is a large glycoprotein complex consisting of several disulfide linked subunits (Mr approximately 150,000-240,000). The differently sized antigen subunits are related, since they yielded very similar proteolytic cleavage patterns. M1 antibody can bind to the denatured subunits. The antigen subunits, as well as a Mr approximately 80,000 pepsin-resistant antigenic domain derived from them, are resistant to bacterial collagenase. Despite possessing subunits similar in size to fibronectin, myotendinous antigen appears to be both structurally and antigenically unrelated to fibronectin or to other known extracellular matrix components. About seven times more M1 antigen per cell nucleus was released into the medium in fibroblast as compared to muscle cultures. In muscle conditioned medium, myotendinous antigen is noncovalently complexed to very high molecular weight material that could be heavily labeled by [3H]glucosamine and [35S]sulfate. This material is sensitive to chondroitinase ABC and hence appears to contain sulfated glycosaminoglycans. We speculate that myotendinous antigen might interact with proteoglycans on the surface of muscle fibers, thereby acting as a link to tendons.
登录
查看更多内容
DOI:
--
发表时间:
1981-05
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
B. Carlin;R. Jaffe;B. Bender;A. Chung
通讯作者:
B. Carlin;R. Jaffe;B. Bender;A. Chung
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Fessler,LI;Fessler,JH
通讯作者:
Fessler,JH
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Bächinger,HP;Fessler,LI;Fessler,JH
通讯作者:
Fessler,JH
DOI:
--
发表时间:
1981
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Fessler,LI;Kumamoto,CA;Meis,ME;Fessler,JH
通讯作者:
Fessler,JH