Association of apo B lipoproteins with arterial proteoglycans: pathological significance and molecular basis.
Level 5 - mechanism / opinion, no new human data
Narrative review of in vitro, ex vivo, and mechanistic studies without systematic review methodology.
PubMed 9712326 · doi:10.1016/s0021-9150(98)00107-5
What was done
This narrative review summarizes in vitro, ex vivo, and observational mechanistic evidence on how apolipoprotein B-100 (apo B-100) lipoproteins, primarily LDL and Lp(a), bind to arterial intima proteoglycans and promote atherogenesis.
What was found
The abstract reports no numerical values, effect estimates, or sample sizes. Qualitatively, it reports that: - Specific positively charged regions of apo B-100 bind negatively charged glycosaminoglycans (chondroitin sulfate, dermatan sulfate, and likely heparan sulfate) in the arterial intima. - Small, dense LDL exhibits a higher affinity for chondroitin sulfate proteoglycans than larger buoyant LDL. - Proteoglycan binding induces irreversible structural alterations in LDL, enhancing oxidative and hydrolytic modification and accelerating uptake by macrophages and smooth muscle cells. - LDL from patients with coronary heart disease or an atherogenic lipoprotein phenotype shows higher affinity for arterial proteoglycans, which can be modified by diet or pharmacological interventions.
Why it matters
It outlines the molecular basis of the response-to-retention model of atherosclerosis, linking small, dense LDL subfractions to increased arterial matrix entrapment and lesion development.
Limits
No quantitative data, sample sizes, or statistical metrics are reported in the abstract. The paper is a narrative synthesis of in vitro and ex vivo bench models lacking systematic review methodology.
Cited by
- supports Smaller, dense LDL particles have a greater tendency to enter the arterial wall, bind more tightly to artery tissue, and oxidize more rapidly compared to large LDL particles.