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Titolo:
IDENTIFICATION OF STRUCTURAL DOMAINS IN INTER-ALPHA-TRYPSIN INHIBITORINVOLVED IN CALCIUM-OXALATE CRYSTALLIZATION
Autore:
KOBAYASHI H; SHIBATA K; FUJIE M; SUGINO D; TERAO T;
Indirizzi:
HAMAMATSU UNIV,SCH MED,DEPT OBSTET & GYNECOL,HANDACHO 3600 HAMAMATSU SHIZUOKA 43131 JAPAN HAMAMATSU UNIV,SCH MED,EQUIPMENT CTR HAMAMATSU SHIZUOKA 43131 JAPAN NISSAN FOOD PROD CO LTD,NISSIN CENT RES INST SHIGA JAPAN
Titolo Testata:
Kidney international
fascicolo: 6, volume: 53, anno: 1998,
pagine: 1727 - 1735
SICI:
0085-2538(1998)53:6<1727:IOSDII>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-CELL INVASION; ACID-RICH PROTEIN; SOLUBLE ORGANIC MATRIX; UNDILUTED HUMAN URINE; CRYSTAL-GROWTH; LIGHT-CHAIN; RAT URINE; IN-VITRO; NEPHROCALCIN; STONE;
Keywords:
CRYSTAL FORMATION; NEPHROCALCINOSIS; URINARY TRYPSIN INHIBITOR; PROTHROMBIN FRAGMENT 1; GLYCOPROTEIN; INTER-ALPHA-TRYPSIN INHIBITOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
H. Kobayashi et al., "IDENTIFICATION OF STRUCTURAL DOMAINS IN INTER-ALPHA-TRYPSIN INHIBITORINVOLVED IN CALCIUM-OXALATE CRYSTALLIZATION", Kidney international, 53(6), 1998, pp. 1727-1735

Abstract

The urinary glycoprotein that inhibits calcium oxalate (CaOx) crystallization in vitro shows a structural similarity to urinary trypsin inhibitor (UTI; recently termed bikunin), the light chain of inter-alpha-trypsin inhibitor (I alpha I). The functional domains of I alpha I involved in its inhibitory activity of CaOx crystallization have been investigated using isolated intact domains of I alpha I produced from controlled proteolytic digests of the protein. The fragments investigatedinclude the heavy chains of I alpha I UTI, chondroitinase AC-treated UTI, and the carboxyl-terminal domain of UTI (termed H1-8). The effects of I alpha I and its fragments on the inhibitory activity of CaOx crystallization were evaluated in vitro using CaOx crystal aggregation and growth assays, and seeded crystal generation assay as well as usingcrystal matrix protein generation assay. UTI, but not the heavy chains of I alpha I, had a discernible effect on CaOx crystallization inhibitory activity. Less requirement of the carbohydrate moiety of UTI is implicated by the observation that chondroitinase AC-treated UTI fragment was also found to inhibit CaOx crystallization with almost the same activity as UTI. HI-8 also efficiently inhibited CaOx crystallization, while I alpha I showed a weak inhibitory activity. The results are almost consistent with a seed crystal generation assay and a crystal adsorption inhibition assay, in which I alpha I or its derivatives inhibits prothrombin fragment 1 (F1) adsorption to CaOx crystals. In conclusion, these results suggest that the part of the I alpha I protein responsible for inhibition of CaOx crystallization is the carboxyl-terminal domain of UTI.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 01:25:23