Interaction of apolipoprotein[a] with apolipoproteinB-100 Cys3734 region in lipoprotein[a] is confirmed immunochemically

Guevara, J.; Valentinova, Natalia V.; García, Oscar Sacristán; Gotto, Antonio M.; Yang, Chao; Gaubatz, John W.; Sparrow, James T.

doi:10.1007/bf01886807

Cited by 12 publications

(7 citation statements)

References 31 publications

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“…ApoB-100 is a multipotential molecule with a role in signaling processes (10) and has several functional regions (8,(23)(24)(25)(26) that can all be affected by key modifications of selected protein domains. We did not explore the functional consequences of the new structural arrangement of the protein.…”

Section: Discussionmentioning

confidence: 99%

One site on the apoB‐100 specifically binds 17‐β‐estradiol and regulates the overall structure of LDL

et al. 2003

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The major protein component (apoB-100) of low-density lipoprotein (LDL) is known as a multipotential molecule the several functional regions of which can all be affected by key structural modifications driven by specific domains. Based on our previous report on structural and conformational modifications of apoB-100 in the presence of 17-beta-estradiol (E2), we characterized the interaction between E2 and the apoB-100 and further explored the induced alterations in terms of the structural arrangement of the whole LDL particle. We report evidence for the existence on apoB-100 of a single specific and saturable binding site for E2, the occupancy of which modifies the overall structure of the protein, inducing an increase in the alpha-helix fraction. As a consequence, the structure of the LDL particle is deeply perturbed, with a change in the arrangement of both the outer shell and lipid core and an overall volume shrinkage. The evidence of a regulation of apoB-100 structure by a physiological ligand opens new perspectives in the study of the biological addressing of the LDL particle and suggests a novel rationale in the search for mechanisms underlying the beneficial role of E2 in decreasing the risk of early lesions in atherosclerosis.

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Section: Discussionmentioning

confidence: 99%

One site on the apoB‐100 specifically binds 17‐β‐estradiol and regulates the overall structure of LDL

et al. 2003

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“…The final assembly of Lp(a) occurs trough a two-step mechanism where a noncovalent interaction between apo(a) and apoB-100 precedes the disulfide linkage formation. [25] Lp(a) catabolism still remains unclear, but there is evidence against a great involvement of LDL receptors in this process. [26] The most widely used methods to measure Lp(a) in the clinical laboratory are the commercially available immunoassays (immunoturbidimetric analysis and ELISA method).…”

Section: Lipoprotein(a): a Suis Generis Moleculementioning

confidence: 99%

Lipoprotein(a) as a potential marker of residual liver function in hepatocellular carcinoma

Uccello

Malaguarnera

Pelligra

et al. 2011

Indian Journal of Medical and Paediatric Oncology

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The residual liver function is a major clinical index in hepatocellular carcinoma (HCC) patients. As the liver plays a crucial role in lipid and lipoprotein metabolism, the significant impairment of the hepatic function occurring during chronic liver diseases, such as HCC, can influence plasma lipoprotein profiles. Although, lipoprotein(a) (Lp(a)) circulating concentrations are mostly determined by genetic factors, in the majority of reports they have shown a correlation with the hepatic status and a significant decrease in HCC and liver cirrhosis patients than among the controls. In such a way, Lp(a) may represent a new additional and useful marker for a more complete assessment and monitoring of the liver function in patients with HCC and liver cirrhosis. Further studies are needed in order to evaluate the clinical significance of Lp(a) in HCC.

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“…This interaction most likely takes place on the cell surface [18]and later in the circulation, whereby one or few distinct K-IVs form a dissociable complex with lysine or proline residues of apoB-100 [15, 16, 19]. In a second step, a disulphide bridge is linked between two distinct cysteines in apo(a) and in apoB-100 [15, 16, 18, 19, 20, 21, 22]. …”

Section: Introductionmentioning

confidence: 99%

An Increased Serum Level of Free Apo(a) in Renal Patients Is More Striking than that of Lp(a) and Is Influenced by Homocysteine

Herrmann

Quast²,

Ellgass³

et al. 2000

Nephron

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Lipoprotein(a) [Lp(a)] excess combined with hyperhomocysteinaemia and hyperfibrinogenaemia may contribute to the high incidence of vascular diseases in dialysis patients. This study is aimed at investigating the role of free apolipoprotein(a) [fapo(a)] in renal patients. We have been able to show that, as compared with controls (0.53 mg/l), the median serum concentrations of fapo(a) in patients with nephrotic syndrome (2.58 mg/l) and with peritoneal dialysis (3.40 mg/l) were strongly elevated (5- to 7-fold), while the fapo(a) levels in patients undergoing haemodialyis (1.02 mg/l) and after renal transplantation (0.90 mg/l) were about doubled. The observed differences in fapo(a) levels indicate that several mechanisms may increase the level of fapo(a), i.e., reduced renal clearance, enhanced hepatic synthesis, or homocysteine releasing apolipoprotein(a) from Lp(a). In the study collective, the median total homocysteine levels were significantly elevated in all patient groups, stronger in patients on haemodialysis (31.4 µmol/l) and peritoneal dialysis (31.2 µmol/l) than in patients with nephrotic syndrome (19.7 µmol/l) and after renal transplantation (19.5 µmol/l). In transplant patients with adequate renal function and without other apolipoprotein(a)-increasing factors, fapo(a) was significantly increased when total homocysteine exceeded 22 µmol/l. In conclusion, our findings let us presume that an increased fapo(a) level in renal patients possibly could be one of the reasons contributing to the high incidence of vascular diseases in these patients, because fapo(a) not covalently linked with Lp(a) is even more easily able to inhibit the fibrinolytic system than the complete Lp(a). These preliminary results have to be confirmed by further investigations.

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Interaction of apolipoprotein[a] with apolipoproteinB-100 Cys3734 region in lipoprotein[a] is confirmed immunochemically

Cited by 12 publications

References 31 publications

One site on the apoB‐100 specifically binds 17‐β‐estradiol and regulates the overall structure of LDL

One site on the apoB‐100 specifically binds 17‐β‐estradiol and regulates the overall structure of LDL

Lipoprotein(a) as a potential marker of residual liver function in hepatocellular carcinoma

An Increased Serum Level of Free Apo(a) in Renal Patients Is More Striking than that of Lp(a) and Is Influenced by Homocysteine

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