Abstract
By single strand conformational polymorphism, nucleotide sequencing and enzyme restriction, we analyzed the protein S α gene in 17 protein S-deficient probands and in their available family members. The relationship between genotype and phenotype was also evaluated. Twelve different sequence variations were identified in 17 probands. Ten were putative causal mutations distributed in 16 probands: 4 were nonsense, 5 missense and one a splice site mutation. In most families in which a mutation was identified, more than one phenotype of PS deficiency was present. The same splice site mutation (intron j G-A, exon 10 + 5) was associated with type I deficiency in one family and with type I/III in another unrelated family. A phenotypic discrepancy was also observed for the Arg474Pro, Gly597Asp and Arg410stop mutations. Glu26Ala, previously reported in kindreds with type I deficiencies, was found in association with I, II and III phenotypes in four unrelated kindreds. Phenotypic analysis of protein S deficiency is poorly related to the underlying genetic defect.
| Original language | English |
|---|---|
| Pages (from-to) | 1634-1638 |
| Number of pages | 5 |
| Journal | Thrombosis and Haemostasis |
| Volume | 82 |
| Issue number | 6 |
| Publication status | Published - 1999 |
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Keywords
- Mutations
- Phenotype
- Protein S α gene
- Protein S Heerlen
ASJC Scopus subject areas
- Hematology
Cite this
Poor relationship between phenotypes of protein S deficiency and mutations in the protein S alpha gene. / Hermida, José; Faioni, Elena M.; Mannucci, Pier Mannuccio.
In: Thrombosis and Haemostasis, Vol. 82, No. 6, 1999, p. 1634-1638.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Poor relationship between phenotypes of protein S deficiency and mutations in the protein S alpha gene
AU - Hermida, José
AU - Faioni, Elena M.
AU - Mannucci, Pier Mannuccio
PY - 1999
Y1 - 1999
N2 - By single strand conformational polymorphism, nucleotide sequencing and enzyme restriction, we analyzed the protein S α gene in 17 protein S-deficient probands and in their available family members. The relationship between genotype and phenotype was also evaluated. Twelve different sequence variations were identified in 17 probands. Ten were putative causal mutations distributed in 16 probands: 4 were nonsense, 5 missense and one a splice site mutation. In most families in which a mutation was identified, more than one phenotype of PS deficiency was present. The same splice site mutation (intron j G-A, exon 10 + 5) was associated with type I deficiency in one family and with type I/III in another unrelated family. A phenotypic discrepancy was also observed for the Arg474Pro, Gly597Asp and Arg410stop mutations. Glu26Ala, previously reported in kindreds with type I deficiencies, was found in association with I, II and III phenotypes in four unrelated kindreds. Phenotypic analysis of protein S deficiency is poorly related to the underlying genetic defect.
AB - By single strand conformational polymorphism, nucleotide sequencing and enzyme restriction, we analyzed the protein S α gene in 17 protein S-deficient probands and in their available family members. The relationship between genotype and phenotype was also evaluated. Twelve different sequence variations were identified in 17 probands. Ten were putative causal mutations distributed in 16 probands: 4 were nonsense, 5 missense and one a splice site mutation. In most families in which a mutation was identified, more than one phenotype of PS deficiency was present. The same splice site mutation (intron j G-A, exon 10 + 5) was associated with type I deficiency in one family and with type I/III in another unrelated family. A phenotypic discrepancy was also observed for the Arg474Pro, Gly597Asp and Arg410stop mutations. Glu26Ala, previously reported in kindreds with type I deficiencies, was found in association with I, II and III phenotypes in four unrelated kindreds. Phenotypic analysis of protein S deficiency is poorly related to the underlying genetic defect.
KW - Mutations
KW - Phenotype
KW - Protein S α gene
KW - Protein S Heerlen
UR - http://www.scopus.com/inward/record.url?scp=0032700739&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032700739&partnerID=8YFLogxK
M3 - Article
C2 - 10613647
AN - SCOPUS:0032700739
VL - 82
SP - 1634
EP - 1638
JO - Thrombosis and Haemostasis
JF - Thrombosis and Haemostasis
SN - 0340-6245
IS - 6
ER -