Cyanogen bromide peptides of the fibrillar collagens I, III, and V and their mass spectrometric characterization: Detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils
Cyanogen bromide peptides of the fibrillar collagens I, III, and V and their mass spectrometric characterization: Detection of linear peptides, peptide glycosylation, and cross-linking peptides involved in formation of homo- and heterotypic fibrils
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DOI：
10.1021/pr070318r
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发表时间：
2007-11-01
影响因子：
4.4
通讯作者：
Dreisewerd, Klaus
中科院分区：
文献类型：
--
作者：
Henkel, Werner;Dreisewerd, Klaus
用紫外基质辅助激光解吸电离飞行时间质谱（UV-MALDI MS）研究了从胎牛皮肤中提取并用溴化氰裂解的纤维状胶原I、III和V的网络结构。几乎所有预期的不同α链的溴化氰肽都被检测到。鉴别出不同的肽，其可用作单个α链的参考信号。通过将质谱数据与记录的氨基酸序列进行比较，表明了同型和异型交联模式，其中一些在牛胶原蛋白之前没有描述过。潜在的交联机制进行了讨论。例如，质谱数据表明，异型I/III和I/V原纤维的形成基本上是由I型胶原的末端区决定的，所述末端区通过4D或0 D交错键共价连接到相邻分子的相应螺旋和非螺旋交联结构域。可以得出交联的化学性质。数据还表明异型原纤维的形成受到干扰。最后，还可以鉴定胶原蛋白糖基化。
The network of the fibrillar collagens I, III, and V, extracted from fetal calf skin and cleaved with cyanogen bromide, was studied by means of ultraviolet matrix-assisted laser desorption ionization time-of-flight mass spectrometry (UV-MALDI MS). Nearly all of the expected cyanogen bromide peptides of the different alpha chains were detected. Distinct peptides are identified that can serve as a reference signal for the individual alpha-chains. Homo- and heterotypic cross-linking patterns, some of which have not been described before for bovine collagen, are indicated by comparison of the mass spectrometric data with documented amino acid sequences. Potential cross-linking mechanisms are discussed. For example, the mass spectrometric data suggest that the formation of heterotypic I/III and I/V fibrils is substantially determined by the telo-regions of type I collagen, which are covalently connected to the corresponding helical and nonhelical cross-linking domains of adjacent molecules either by 4D or 0D-stagger bonds. The chemical nature of the cross-links can be concluded. The data also indicate a disturbed formation of heterotypic fibrils. Finally, collagen glycosylation can also be identified.