Schneider S, Reissig J, Weisbach VG, Achenbach S, Hackstein H, Strobel J (2022)
Publication Type: Journal article
Publication year: 2022
Book Volume: 33
Pages Range: 224-227
Journal Issue: 4
DOI: 10.1097/MBC.0000000000001120
The members of a Caucasian family were genetically analyzed on suspicion of hereditary protein S deficiency. A novel mutation, c.1904T>C, associated with severe quantitative protein S deficiency was found. The novel PROS1 mutation was identified by sequencing of the PROS1 gene coding sequence. The identified c.1904T>C point mutation results in p.Phe635Ser amino acid exchange, which is located in the Laminin G-like 2 domain of protein S. Computational analysis indicates that this amino acid exchange affects the correct folding of the protein S antigen. Furthermore, this mutation is located in a region of the Laminin G-like 2 domain where changes in the amino acid sequence often result in decreased secretion. We postulate that the novel p.Phe635Ser mutation might lead to an incorrect folding, and thus, to a strongly impaired secretion of this protein S variant. We named this novel variant protein.
APA:
Schneider, S., Reissig, J., Weisbach, V.G., Achenbach, S., Hackstein, H., & Strobel, J. (2022). Protein S Erlangen: a novel PROS1 gene mutation associated with quantitative protein S deficiency. Blood Coagulation & Fibrinolysis, 33(4), 224-227. https://doi.org/10.1097/MBC.0000000000001120
MLA:
Schneider, Sabine, et al. "Protein S Erlangen: a novel PROS1 gene mutation associated with quantitative protein S deficiency." Blood Coagulation & Fibrinolysis 33.4 (2022): 224-227.
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