August 19, 2008Journal of Biological ChemistryOpen Access

The Acidic Domain of GPIHBP1 Is Important for the Binding of Lipoprotein Lipase and Chylomicrons

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Population

pgsA-745 Chinese hamster ovary cells overexpressing GPIHBP1

Comparison

Polyaspartate or polyglutamate peptides, rabbit… vs Wild-type GPIHBP1 or absence of blocking agents

Design

Preclinical

Authors

PGPeter GinUniversity of California, Los Angeles LYLiya YinUniversity of Phoenix BDBrandon S.J. DaviesUniversity of Iowa

Discussion

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Implication

Identifies key GPIHBP1 residues for LPL binding in animal models; extends mechanistic insight but leaves open human therapeutic translation.

Structured PICO

Population

pgsA-745 Chinese hamster ovary cells overexpressing GPIHBP1

Intervention

Polyaspartate or polyglutamate peptides, rabbit antiserum against the acidic domain, mutation of acidic amino acids (residues 38-48) to alanine, and mutation of heparin-binding domains in LPL and apolipoprotein AV

Comparator

Wild-type GPIHBP1 or absence of blocking agents

Outcome

Binding of lipoprotein lipase (LPL) and chylomicrons to GPIHBP1surrogate

The acidic domain of GPIHBP1 is essential for the binding of lipoprotein lipase and chylomicrons via electrostatic interactions, providing mechanistic insight into triglyceride-rich lipoprotein lipolysis.

Cite This Study

Gin et al. (2008) studied this question.

synapsesocial.com/papers/6a73dc53f4f9256fee8de997 https://doi.org/10.1074/jbc.m802579200

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Implication

Identifies key GPIHBP1 residues for LPL binding in animal models; extends mechanistic insight but leaves open human therapeutic translation.

The Acidic Domain of GPIHBP1 Is Important for the Binding of Lipoprotein Lipase and Chylomicrons

Discussion

Member takes

Implication

Structured PICO

Cite This Study

The Acidic Domain of GPIHBP1 Is Important for the Binding of Lipoprotein Lipase and Chylomicrons

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider