ABSTRACT
We describe a case of a patient affected by a chronic myeloproliferative disorder with t(8;21)(q22;q22) and trisomy 8 at diagnosis. At the time of blastic metamorphosis, 2 months later, trisomy 8 metaphases were significantly reduced, while a predominance of t(8;21) was present. Finally, in the phase of leukemic regrowth following chemotherapy administration, monosomy 8 associated with der(21)t(8;21) was the predominant cytogenetic abnormality.
Subject(s)
Chromosome Aberrations , Chromosomes, Human, Pair 8 , Leukemia, Myeloid, Acute/genetics , Leukemia, Myeloid/genetics , Translocation, Genetic , Chromosomes, Human, Pair 21 , Female , Humans , Karyotyping , Monosomy , TrisomyABSTRACT
We report the disease characteristics and therapeutic results for 25 patients suffering from essential thrombocythaemia (ET), treated with recombinant interferon-alpha-2b (IFN-alpha 2b). ET was diagnosed according to the criteria of the Polycythaemia Vera Study Group. All patients were programmed to receive a subcutaneous induction treatment consisting of 3 MU of IFN-alpha 2b daily for 6 months. In responding patients, treatment was continued for a further 6 months with 3 MU of IFN-alpha 2b three times a week. Complete response was achieved in 13 of 25 patients, partial response in 10 of 25. In 2 cases, therapy was unsuccessful. Side effects were usually mild, consisting of flu-like symptoms in most cases, and were easily controlled by paracetamol. After a median follow-up of 14 months after discontinuation of the treatment, most patients retained the therapeutic response in the absence of toxicity.
Subject(s)
Interferon-alpha/therapeutic use , Thrombocythemia, Essential/drug therapy , Adolescent , Adult , Aged , Aged, 80 and over , Child , Female , Humans , Interferon alpha-2 , Male , Middle Aged , Recombinant ProteinsABSTRACT
The reactive center of C1-inhibitor, a plasma protease inhibitor that belongs to the serpin superfamily, is located on a peptide loop which is highly susceptible to proteolytic cleavage. With plasma kallikrein, C1s and beta-Factor XIIa, this cleavage occurs at the reactive site residue P1 (Arg444); with neutrophil elastase, it takes place near P1, probably at residue P3 (Val442). After these cleavages, C1-inhibitor is inactivated and its conformation is modified. Moreover, in vivo, cleaved C1-inhibitor is removed from the blood stream more rapidly than the intact serpin, which suggests that proteolysis unmasks sites responsible for cellular recognition and the uptake of the cleaved inhibitor. In the study reported here, we show, using an MAb, that an identical neoepitope is created on C1-inhibitor after the cleavage of its exposed loop by plasma kallikrein, C1s, beta-Factor XIIa, and by neutrophil elastase.
