• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

II型原胶原蛋白中较高的翻译后修饰水平并非三螺旋形成缓慢的结果。

High post-translational modification levels in type II procollagen are not a consequence of slow triple-helix formation.

作者信息

Keller H, Eikenberry E F, Winterhalter K H, Bruckner P

出版信息

Coll Relat Res. 1985 Jun;5(3):245-51. doi: 10.1016/s0174-173x(85)80014-5.

DOI:10.1016/s0174-173x(85)80014-5
PMID:4042601
Abstract

The kinetics of triple helix formation of newly synthesized type II procollagen in chick embryo sternal cartilage cells were determined. The data obtained were in agreement with a model for triple helix formation in cellulo proposed recently (Bruckner et al., 1981). The time required to produce fully triple helical type II procollagen in cartilage cells was only 30% longer than for type I procollagen in tendon cells. Therefore, the several-fold increase in post-translational modification observed for type II collagen as compared to type I collagen cannot be attributed solely to slow helix formation but rather is a result of higher levels of enzymic activity of post-translational modification present in cartilage cells.

摘要

测定了鸡胚胸骨软骨细胞中新合成的II型前胶原三螺旋形成的动力学。所得数据与最近提出的细胞内三螺旋形成模型(Bruckner等人,1981年)一致。软骨细胞中产生完全三螺旋的II型前胶原所需的时间仅比肌腱细胞中I型前胶原的时间长30%。因此,与I型胶原相比,II型胶原翻译后修饰增加的几倍不能仅仅归因于螺旋形成缓慢,而是软骨细胞中存在的翻译后修饰酶活性水平较高的结果。

相似文献

1
High post-translational modification levels in type II procollagen are not a consequence of slow triple-helix formation.II型原胶原蛋白中较高的翻译后修饰水平并非三螺旋形成缓慢的结果。
Coll Relat Res. 1985 Jun;5(3):245-51. doi: 10.1016/s0174-173x(85)80014-5.
2
Mechanism for the regulation of post-translational modifications of procollagens synthesized by matrix-free cells from chick embryos.鸡胚无基质细胞合成的前胶原蛋白翻译后修饰的调控机制。
J Biol Chem. 1983 Jun 25;258(12):7779-87.
3
Formation of the triple helix of type I procollagen in cellulo. Temperature-dependent kinetics support a model based on cis in equilibrium trans isomerization of peptide bonds.细胞内I型前胶原三螺旋的形成。温度依赖性动力学支持一种基于肽键顺反异构平衡的模型。
Eur J Biochem. 1984 Apr 16;140(2):391-5. doi: 10.1111/j.1432-1033.1984.tb08114.x.
4
Addition of mannose to both the amino- and carboxy-terminal properties of type II procollagen occurs without formation of a triple helix.甘露糖添加到II型原胶原的氨基末端和羧基末端特性上,且不形成三螺旋。
Biochem Biophys Res Commun. 1978 Oct 16;84(3):691-8. doi: 10.1016/0006-291x(78)90760-x.
5
Regulation of the glycosylations of collagen hydroxylysine in chick embryo tendon and cartilage cells.鸡胚肌腱和软骨细胞中胶原蛋白羟赖氨酸糖基化的调控
Biochim Biophys Acta. 1980 Oct 15;632(3):417-27. doi: 10.1016/0304-4165(80)90237-8.
6
Effect of prevention of procollagen triple-helix formation on proline 3-hydroxylation in freshly isolated chick-embryo tendon cells.预防原胶原三螺旋形成对新鲜分离的鸡胚肌腱细胞中脯氨酸3-羟化作用的影响。
Biochem J. 1981 Apr 15;196(1):203-6. doi: 10.1042/bj1960203.
7
Kinetics for the secretion of nonhelical procollagen by freshly isolated tendon cells.新鲜分离的肌腱细胞分泌非螺旋原胶原的动力学。
J Biol Chem. 1979 Apr 10;254(7):2234-43.
8
Demonstration of cellular retinoic acid binding protein (CRABP) in chick embryo tendon cells and effects of retinoids on collagen synthesis in tendon and sterna.鸡胚肌腱细胞中细胞视黄酸结合蛋白(CRABP)的证实以及类视黄醇对肌腱和胸骨中胶原蛋白合成的影响
Biochem Pharmacol. 1986 Oct 1;35(19):3393-400. doi: 10.1016/0006-2952(86)90441-7.
9
Formation of the triple helix of type I procollagen in cellulo. A kinetic model based on cis-trans isomerization of peptide bonds.细胞内I型前胶原三螺旋的形成。基于肽键顺反异构化的动力学模型。
Eur J Biochem. 1981 Sep 1;118(3):607-13. doi: 10.1111/j.1432-1033.1981.tb05562.x.
10
Underhydroxylated minor cartilage collagen precursors cannot form stable triple helices.羟基化不足的次要软骨胶原前体无法形成稳定的三螺旋结构。
Biochem J. 1988 Feb 15;250(1):65-70. doi: 10.1042/bj2500065.

引用本文的文献

1
Basic Structure, Physiology, and Biochemistry of Connective Tissues and Extracellular Matrix Collagens.结缔组织和细胞外基质胶原的基本结构、生理学和生物化学。
Adv Exp Med Biol. 2021;1348:5-43. doi: 10.1007/978-3-030-80614-9_2.