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Titolo:
ALKALINE-PHOSPHATASE - PLACENTAL AND TISSUE-NONSPECIFIC ISOENZYMES HYDROLYZE PHOSPHOETHANOLAMINE, INORGANIC PYROPHOSPHATE, AND PYRIDOXAL 5'-PHOSPHATE - SUBSTRATE ACCUMULATION IN CARRIERS OF HYPOPHOSPHATASIA CORRECTS DURING PREGNANCY
Autore:
WHYTE MP; LANDT M; RYAN LM; MULIVOR RA; HENTHORN PS; FEDDE KN; MAHUREN JD; COBURN SP;
Indirizzi:
SHRINERS HOSP CRIPPLED CHILDREN,METAB RES UNIT,2001 S LINDBERGH BLVD ST LOUIS MO 63131 WASHINGTON UNIV,JEWISH HOSP ST LOUIS,MED CTR,DIV BONE & MINERAL DIS ST LOUIS MO 63110 WASHINGTON UNIV,SCH MED,DEPT PEDIAT ST LOUIS MO 63110 MED COLL WISCONSIN,DEPT RHEUMATOL MILWAUKEE WI 53226 CORIELL INST MED RES CAMDEN NJ 08103 UNIV PENN,SCH VET MED,MED GENET SECT PHILADELPHIA PA 19104 FT WAYNE STATE DEV CTR FT WAYNE IN 46835
Titolo Testata:
The Journal of clinical investigation
fascicolo: 4, volume: 95, anno: 1995,
pagine: 1440 - 1445
SICI:
0021-9738(1995)95:4<1440:A-PATI>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
INFANTILE HYPOPHOSPHATASIA; ADULT HYPOPHOSPHATASIA; MISSENSE MUTATIONS; LETHAL FORM; GENE; PYRIDOXAL-5'-PHOSPHATE; SERUM; BONE; PLASMA; VITAMIN-B6;
Keywords:
ENZYME; MINERALIZATION; RICKETS; PHOSPHOCOMPOUNDS; VITAMIN-B6;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
M.P. Whyte et al., "ALKALINE-PHOSPHATASE - PLACENTAL AND TISSUE-NONSPECIFIC ISOENZYMES HYDROLYZE PHOSPHOETHANOLAMINE, INORGANIC PYROPHOSPHATE, AND PYRIDOXAL 5'-PHOSPHATE - SUBSTRATE ACCUMULATION IN CARRIERS OF HYPOPHOSPHATASIA CORRECTS DURING PREGNANCY", The Journal of clinical investigation, 95(4), 1995, pp. 1440-1445

Abstract

Hypophosphatasia features selective deficiency of activity of the tissue-non-specific (liver/bone/kidney) alkaline phosphatase (ALP) isoenzyme (TNSALP); placental and intestinal ALP isoenzyme (PALP and IALP, respectively) activity is not reduced, Three phosphocompounds (phosphoethanolamine [PEA], inorganic pyrophosphate [PPI], and pyridoxal 5'-phosphate [PLP]) accumulate endogenously and appear, therefore, to be natural substrates for TNSALP. Carriers for hypophosphatasia may have decreased serum ALP activity and elevated substrate levels. To test whether human PALP and TNSALP are physiologically active toward the same substrates, we studied PEA, PPI, and PLP levels during and after pregnancy in three women who are carriers for hypophosphatasia, Hypophosphatasemia corrected during the third trimester because of PALP in maternalblood, Blood or urine concentrations of PEA, PPI, and PLP diminished substantially during that time. After childbirth, maternal circulatinglevels of PALP decreased, and PEA, PPi, and PLP levels abruptly increased. In serum, unremarkable concentrations of IALP and low levels of TNSALP did not change during the study period, We conclude that PALP, like TNSALP, is physiologically active toward PEA, PPI, and PLP in humans. We speculate from molecular/crystallographic information, indicating significant similarity of structure of the substrate-binding site of ALPs throughout nature, that all ALP isoenzymes recognize these same three phosphocompound substrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/09/20 alle ore 09:07:53