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Titolo:
Abnormal propeptide processing resulting in the presence of two abnormal species of protein C in plasma - Characterization of the dysfunctional protein C Padua(3) (Protein CR-1L/propeptide)
Autore:
Simioni, P; Kalafatis, M; Tormene, D; Luni, S; Zerbinati, P; Barzon, L; Palu, G; Girolami, A;
Indirizzi:
Univ Padua, Dept Med & Surg Sci, Chair Med 2, I-35100 Padua, Italy Univ Padua Padua Italy I-35100 rg Sci, Chair Med 2, I-35100 Padua, Italy Cleveland State Univ, Dept Chem, Cleveland, OH 44115 USA Cleveland State Univ Cleveland OH USA 44115 Chem, Cleveland, OH 44115 USA Cleveland Clin Fdn, Dept Mol Cardiol, Cleveland, OH 44195 USA Cleveland Clin Fdn Cleveland OH USA 44195 ardiol, Cleveland, OH 44195 USA Univ Padua, Dept Microbiol, I-35100 Padua, Italy Univ Padua Padua Italy I-35100 dua, Dept Microbiol, I-35100 Padua, Italy
Titolo Testata:
THROMBOSIS AND HAEMOSTASIS
fascicolo: 4, volume: 86, anno: 2001,
pagine: 1017 - 1022
SICI:
0340-6245(200110)86:4<1017:APPRIT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAMMA-CARBOXYGLUTAMIC-ACID; FACTOR-VA; ANTICOAGULANT ACTIVITY; ASYMPTOMATIC CARRIERS; POINT MUTATIONS; DEFICIENCY; GENE; IX; BIOSYNTHESIS; SUBSTITUTION;
Keywords:
dysfunctional protein C; type II defect; propeptide clearage; thrombophilia; factor V;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Simioni, P Univ Padua, Dept Med & Surg Sci, Chair Med 2, Via Opsedale 105,I-35100 Padua, Italy Univ Padua Via Opsedale 105 Padua Italy I-35100 0 Padua, Italy
Citazione:
P. Simioni et al., "Abnormal propeptide processing resulting in the presence of two abnormal species of protein C in plasma - Characterization of the dysfunctional protein C Padua(3) (Protein CR-1L/propeptide)", THROMB HAEM, 86(4), 2001, pp. 1017-1022

Abstract

A heterozygous G --> T transversion at position 1388 of the protein C (PC)gene which predicted the substitution of Arg(-1) to a Len (PCR.IL) was identified in a thrombophilic patient. The PCR-IL was purified from the patient's plasma by immunoaffinity chromatography using Ca++-independent and Ca++-dependent monoclonal antibodies. NH.-terminal sequencing of the light chain of PCR-IL revealed two amino acid sequences: one was identical to the complete propeptide sequence of PC, while the other matched the normal PC light chain sequence elongated by one amino acid (Leucine at position 1). Activated PCR-IL/propeptide exhibited normal amidolytic and impaired anticoagulant activity, Thus, the substitution of a Leu for an Ara at position -1 of PC shifts the propeptidase cleavage site by one amino acid. In addition, in PCR-ILpropeptide, the propeptide cleavage at LyS(-2) is less efficient since approximately 60% of PC variant molecules present in patient's plasma retained the entire propeptide. Our findings suggest that depending on the specific amino acid substitution at position-1, PC can be secreted in plasma containing the entire propeptide attached to the light chain. Impaired interaction of elongated APC molecules with a membrane-surface and/or factor Va which is the physiological substrate for APC, is manifested in vivo by thrombophilia.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:31:59