A single point mutation (Trp72 → Arg) in human apo(a) kringle 4-37 associated with a lysine binding defect in Lp(a)
| Autor: | Ditta Pfaffinger, Angelo M. Scanu, Janet Hinman, John C. Lee |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Adult
Male Molecular Sequence Data Lysine Mutant medicine.disease_cause complex mixtures Kringle domain Kringles medicine Humans Point Mutation Amino Acid Sequence Binding site Molecular Biology Apolipoproteins A Aged Aged 80 and over chemistry.chemical_classification Mutation Base Sequence biology Chemistry Sepharose Point mutation Tryptophan Lipoprotein(a) Middle Aged Biochemistry Cardiovascular Diseases biology.protein bacteria Molecular Medicine Female Glycoprotein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1227:41-45 |
| ISSN: | 0925-4439 |
| DOI: | 10.1016/0925-4439(94)90104-x |
| Popis: | Human lipoprotein(a) or Lp(a) binds, like plasminogen, to lysine Sepharose. However, contrary to plasminogen in which kringles 1 and 4 have been implicated, the binding site or sites on apo(a), the specific glycoprotein of Lp(a), have not been determined. For the first time we now report the occurrence of a human Lp(a) that has a mutant form of apo(a) where Arg has replaced Trp in position 72 of kringle 4-37 and is unable to bind to lysine Sepharose. This observation suggests that Trp72 of apo(a) kringle 4-37 may play a dominant role in lysine binding. Lysine binding has been associated with the thrombogenic potential of Lp(a). Thus, the Trp72 → Arg mutation may render Lp(a) ‘benign’ from the cardiovascular viewpoint. |
| Databáze: | OpenAIRE |
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