Sear C H, Jones C J, Knight K R, Grant M E
Connect Tissue Res. 1981;8(3-4):167-70. doi: 10.3109/03008208109152368.
Cell cultures propagated from fetal bovine ligamentum nuchae were found to accumulate an extensive extracellular matrix containing collagen and elastic fibers when maintained for periods up to 8 weeks. The synthesis by these cells of two glycoproteins, designated MFP I and MFP II, which are immunologically related to components of the elastic fiber microfibrils was investigated. MFP II, apparent mol. t. 300,000, was shown to be a non-collagenous glycoprotein whereas MFP I, apparent mol. wt. 150,000, was found to be a novel collagenous glycoprotein containing hydroxyproline and glycosylated hydroxylysine residues but exhibiting properties of distinct from the known collagens. Two glycoproteins having characteristics similar to MFP I and MFP II were also identified in an extract of the cell layer and in a "microfibrillar protein preparation" from intact nuchal ligament.
从胎牛项韧带繁殖的细胞培养物,在培养长达8周的时间里,被发现会积累一种含有胶原蛋白和弹性纤维的广泛细胞外基质。对这些细胞合成的两种糖蛋白(命名为MFP I和MFP II)进行了研究,它们在免疫学上与弹性纤维微原纤维的成分相关。MFP II的表观分子量为300,000,被证明是一种非胶原糖蛋白,而MFP I的表观分子量为150,000,被发现是一种新型胶原糖蛋白,含有羟脯氨酸和糖基化羟赖氨酸残基,但具有与已知胶原蛋白不同的特性。在细胞层提取物和完整项韧带的“微原纤维蛋白制剂”中也鉴定出了两种特性与MFP I和MFP II相似的糖蛋白。