Alitalo K, Myllyla R, Sage H, Pritzl P, Vaheri A, Bornstein P
J Biol Chem. 1982 Aug 10;257(15):9016-24.
The A204 cell line, derived from a human rhabdomyosarcoma, was studied in culture for its capacity to synthesize collagen types and other extracellular matrix proteins. The cells synthesized and secreted into the culture medium collagenous proteins with apparent molecular weights of 220,000 and 150,000. These were identified as the pro alpha 1 and pro alpha 2 chains of type V collagen by immunoprecipitation and by peptide mapping. The pro alpha 1(V) chain was made in excess of a 2:1 ratio for pro alpha 1(V) to pro alpha 2(V), and a fraction of the pro alpha 1(V) chains together with all of the pro alpha 2(V) chains participated in intermolecular disulfide bonding. The chains were extensively glycosylated at hydroxylysyl residues in ascorbate-supplemented cultures. A fraction of the secreted pro alpha 1(V) chains was processed to the p alpha 1(V) form, but further processing in the culture medium was very slow and the type V collagen molecules deposits in the extracellular matrix apparently retained large non-triple helical domains. Since the A204 cell line does not produce other collagen types, it may prove useful in further studies of the biosynthesis of type V procollagen.
对源自人横纹肌肉瘤的A204细胞系进行培养研究，以观察其合成各型胶原蛋白及其他细胞外基质蛋白的能力。这些细胞合成并分泌到培养基中的胶原蛋白，其表观分子量分别为220,000和150,000。通过免疫沉淀和肽图谱分析，将其鉴定为V型胶原蛋白的前α1链和前α2链。前α1（V）链的合成量超过前α1（V）与前α2（V）2:1的比例，一部分前α1（V）链与所有前α2（V）链参与分子间二硫键的形成。在添加抗坏血酸的培养物中，这些链在羟赖氨酸残基处被广泛糖基化。一部分分泌的前α1（V）链被加工成pα1（V）形式，但在培养基中的进一步加工非常缓慢，V型胶原蛋白分子在细胞外基质中的沉积显然保留了大的非三螺旋结构域。由于A204细胞系不产生其他类型的胶原蛋白，它可能在V型前胶原生物合成的进一步研究中证明是有用的。
