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Biomedical subjects

N Sala

Publications and source records attributed to N Sala.

At least 55 records · Page 3Linked to original sources
PubMed1994

[The procollagen-III peptide in the clinical surveillance of alcoholic hepatopathy and other chronic hepatopathies].

Liver fibrosis determines the course and prognosis of alcoholic liver disease. Evaluation of serum concentration of procollagen-III peptides (sPIIIP) is considered a biochemical test useful for evaluating a fibrotic process. We have investigated 30 healthy subjects and 53 patients with alcoholic liver disease, histologically diagnosed by percutaneous liver biopsy in four clusters: steatosis (11), fibrosteatosis (11), chronic active hepatitis (11) and cirrhosis (20). SPIIIP levels were increased in patients with cirrhosis and chronic active hepatitis; while they were regular in patients with steatosis and fibrosteatosis. Evaluation of serum concentration of sPIIIP by radioimmunoassay seems to be an useful test for identifying patients with alcoholic liver disease with a good prognosis and patients in progress to cirrhosis and it is an useful test for control the course and evolution of chronic liver disease.

Adult↗
PubMed1994

[Hepatitis C and chronic alcoholic hepatopathy].

We evaluated hepatitis C virus prevalence in 105 patients with chronic alcoholic liver disease by research of antibodies to hepatitis C virus (anti-HCV) by second generation recombinant based enzyme immunosorbent to assay and immunoblot to assay. 46 patients of 105 (43.7%) were anti-HCV positive: 2 in steatosis group (9.5%), 3 in steatofibrosis (23%), 10 in chronic active hepatitis (66.6%), 22 in cirrhosis (59.4%) and 9 in hepatocellular carcinoma (47.3%). These patients had higher levels of serum gammaglobulin and transaminases than seronegative patients. We think that there is a correlation between high prevalence of antibodies anti-HCV and the evolution of damage in chronic alcoholic liver disease.

Adult↗
PubMed1994

Severe homozygous protein C deficiency: identification of a splice site missense mutation (184, Q-->H) in exon 7 of the protein C gene.

Single strand conformation polymorphism (SSCP) analysis of exon 7 of the protein C gene has identified a novel splice site missense mutation (184, Q-->H), in a newborn child with purpura fulminans and undetectable protein C levels. The mutations, seen in the homozygous state in the child and in the heterozygous state in her mother, was characterized and found to be a G to C nucleotide substitution at the -1 position of the donor splice site of intron 7 of the protein C gene, which changes histidine 184 for glutamine (184, Q-->H). According to analysis of the normal and mutated sequences, this mutation should also abolish the function of the donor splice site of intron 7 of the protein C gene. Since such a mutation is compatible with the absence of gene product in plasma and since DNA sequencing of all protein C gene exons in this patient did not reveal any other mutation, we postulate that mutation 184, Q-->H results in the absence of protein C gene product in plasma, which could be the cause of the severe phenotype observed in this patient.

Base Sequence↗
PubMed1993

Acceptor splice site mutation in the invariant AG of intron 5 of the protein C gene, causing type I protein C deficiency.

An acceptor splice-site mutation (3318, A-->G) in the invariant AG of intron 5 of the human protein C gene has been identified in a Spanish family with heterozygous type I protein C (PC) deficiency and thromboembolic disease. Family studies confirmed cosegregation of the mutation with type I PC deficiency. Computer analysis of the mutated sequence predicted the normal splicing site to be abolished by this mutation, whereas a cryptic splice site located two nucleotides downstream, in exon 6, is probably activated. According to this, 3318, A-->G should result in a frameshift with a stop at codon 119, in agreement with the presence of a type I or quantitative PC deficient phenotype in the affected members of the family.

Adult↗
PubMed1992

[Polymorphism MI detected through the enzyme MspI in the study of congenital protein C deficiency].

BACKGROUND: In order to find alternatives for the diagnosis of hereditary protein C (PC) deficiency, we have studied the diagnostic informativity of the restriction fragment length polymorphism (RFLP) MI, located 7 kb upstream of the PC gene and detected with the restriction enzyme MspI. METHODS: The RFLP MI has been analysed in 77 individuals belonging to 27 families with congenital PC deficiency, as well as in a control group of 46 healthy donors. The analysis has been performed by PCR amplification and MspI digestion of the polymorphic DNA fragment. RESULTS: The allelic frequencies of the RFLP MI in the population studied are 0.69 for the allele A1, without the MspI restriction site, and 0.31 for the allele A2, with the MspI site. No differences have been found between the control and the PC deficient groups. The informativity of the polymorphism has been calculated to be 33.8%. Consegregation studies between this RFLP and PC deficiency have allowed the determination of the allele associated to the polymorphism in 21 out of the 27 studied families. Furthermore, an asymptomatic PC deficient carrier, with normal PC levels, has been identified. CONCLUSIONS: The study of this RFLP in families with hereditary PC deficiency may be useful for the identification of PC deficient carriers as well as for the prenatal diagnosis of the deficiency.

Alleles↗
PubMed1992

Immunoglobulin fractions isolated from patients with antiphospholipid antibodies prevent the inactivation of factor Va by activated protein C on human endothelial cells.

We studied the effect of purified immunoglobulins (Ig) from 21 patients with antiphospholipid antibodies (aPL) on factor Va degradation by activated protein C (aPC) on cultured human umbilical vein endothelial cells (HUVEC). Sera from patients were tested on an ELISA aPL assay to determine the isotype with aPL activity. HUVEC were incubated with purified IgG or IgM fraction from controls or patients. Activated PC and factor Va were then added and factor Va degradation was measured after several reaction times. 13 of 14 IgM and 8 of 10 IgG from patients showed an inhibitory effect on factor Va degradation by aPC when compared with control Ig. We also observed the same inhibitory effect with patients' Ig on studying the degradation of factor Va by aPC in a purified system containing aPC, protein S and phospholipids. These results suggest that aPL antibodies disturb the anticoagulant activity of aPC, which may contribute to the thrombotic tendency of these patients.

Antibodies↗
PubMed1992

Multicenter evaluation of three commercial methods for measuring protein S antigen.

This collaborative study was designed to assess the performance of commercial methods for protein S (PS) antigen measurement. Twenty-five different samples were distributed deep-frozen (24 plasmas) or lyophilized (one plasma) to five laboratories. They were analyzed blind in each laboratory by the method used locally and by three commercial methods which included two electroimmunoassays (EIA), Asseraplate-PS (Diagnostica Stago), Rellplate-S (American Diagnostica) and an ELISA system, Asserachrom-PS (Diagnostica Stago). 1. Reproducibility. Average between-laboratory coefficients of variation were 15.4%, 17.6% and 25.3% for Asserachrom-PS, Asseraplate-PS and Rellplate-S. 2. Specificity. Results of all methods showed that PS is underestimated when C4b binding protein is high. This influence was particularly evident for the ELISA Asserachrom-PS and disappeared when the antibody-antigen incubation period was prolonged to overnight. 3. Sensitivity. In all laboratories ELISA detected even the lowest PS concentration (4 U/dl), whereas the two EIAs were less sensitive (lower detection limit 14 U/dl). All methods and laboratories correctly diagnosed a plasma sample from a PS congenitally deficient patient. Conclusions. This study shows that better standardization of PS immunoassays is necessary to improve accuracy and reduce interlaboratory variability before a candidate plasma standard can be successfully calibrated in an international collaborative study.

Anticoagulants↗
PubMed1992

Protein C deficiency: identification of a novel two-base pair insertion and two point mutations in exon 7 of the protein C gene in Spanish families.

We have applied single-strand conformation polymorphism (SSCP) to the analysis of exon 7 of the anticoagulant protein C (PC) gene, in 13 PC-deficient Spanish families. Abnormal patterns were visualized in three samples from type I or quantitative PC deficient proposita. A previously undescribed mutation due to a TT insertion after nucleotide 6139, between codons Gly-142 and Arg-143 was found in one family. The mutation (6139,ins TT) should result in a frameshift with a stop at codon 156, which agrees with the presence of a type I or quantitative PC deficiency in the affected members of the family. The second mutation identified was a C to T transition at nucleotide 6274, 9 base pairs into intron G. This mutation (6274,C-->T), found for the first time in a Spanish family, is identical to the previously characterized PC Sant Louis. The third mutation was a G to A transition that replaces arginine 178 with glutamine (178,R-->Q). This is the third case of 178,R-->Q mutation in 17 apparently unrelated Spanish families with type I PC deficiency. Furthermore, SSCP analysis allowed the detection of another previously described mutation in a PC-deficient Spanish family (178,R-->W).

Base Sequence↗
PubMed1987

Dysfunctional activated protein C (PC Cádiz) in a patient with thrombotic disease.

The partial characterization of a dysfunctional protein C (PC), provisionally named "PC Cádiz", in a 45-year-old male patient suffering from recurrent venous thrombosis is described. The only defect found in laboratory assays for haemostasis and hepatic function was a half normal level of both amidolytic and anticoagulant protein C activity, measured by different functional assays that use thrombin-thrombomodulin complex and a snake venom to activate protein C. Protein C antigen was always found to be within normal levels. Two young daughters of the propositus were found to have the same defect. Double-crossed immunoelectrophoresis, performed in the presence and absence of Ca2+ in the first dimension, showed no clear differences between patient and control PC. PC adsorption to barium salts was also found to be normal. Measurement of the PC activation peptide in the barium citrate eluates after PC activation showed no significant differences between patient and 10 normal controls, the concentration of this peptide being very similar to that of PC zymogen in the same eluates before PC activation. These results indicate that this abnormal PC is able to be normally activated by thrombin-thrombomodulin complex but does not exhibit serine protease activity, probably due to a defect in the PC molecule near the active site center.

Humans↗
PubMed1985

Protein C deficiency--response to danazol and DDAVP.

We studied a Spanish family in which one of the female members presented recurrent thrombophlebitis in both legs after three different deliveries. Biological and antigenic activity of protein C was decreased (35% and 42% respectively). Reduced protein C levels were also observed in 6 other family members. Administration of danazol (600 mg/day) in two patients with protein C deficiency elevated this protein and discontinuation of the drug resulted in a reduction of protein C to pretreatment values. The proposita showed a normal fibrinolytic activity and infusion of DDAVP produced a similar response of FVIII/VWF and plasminogen activator to those observed in healthy subjects.

Antithrombin III↗