Cystatin domains in alpha‐2‐HS‐glycoprotein and fetuin

FEBS Letters

Elzanowski, Andrzej¹  Seibel-Ross, Elizabeth¹  Hunt, Lois T.¹  Barker, Winona C.¹ 

[1] Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, 3900 Reservoir Road, N.W., Washington, DC 20007, USA

关键词: Cysteine proteinase inhibitor;    α2-HS-glycoprotein;    Kininogen;    Plasma protein;    Bone resorption;    Fetuin;   

DOI  :  10.1016/0014-5793(88)80890-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have found that chain A of alpha-2-HS-glycoprotein contains two cystatin domains that show closest similarity to those of kininogen. Most likely, the two proteins diverged after the primary duplication of a single cystatin domain as the two cystatin domains of alpha-2-HS-glycoprotein are more similar, especially in disulfide bonding, to the corresponding domains of kininogen than to each other. We also propose that the carboxyl-terminal (non-cystatin) parts of kininogen and alpha-2-HS-glycoprotein contain homologous segments. We suggest that alpha-2-HS-glycoprotein may act as an inhibitor of the cysteine proteinases responsible for bone resorption. We have also found that fetuin is closely related to alpha-2-HS-glycoprotein.

【 授权许可】

Unknown