We have previously described an atypical lipoprotein-binding protein of about 105 kDa (p105) in membranes of vascular smooth muscle cells (VSMCs) that is distinct from currently known lipoprotein receptors. In the present work we have developed a procedure for purification of p105 from human aortic media. Partial sequencing of purified protein has revealed identity of p105 with human T-cadherin. Anti-peptide antisera raised against human T-cadherin recognized a protein spot corresponding to the purified p105 on two-dimensional Western blots. The antisera also inhibited LDL binding to p105 on ligand blots. We conclude that the 105 kDa lipoprotein-binding protein present in human VSMCs is T-cadherin, an unusual glycosylphosphatidylinositol-anchored member of the cadherin family of cell-cell adhesion proteins.
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http://dx.doi.org/10.1016/s0014-5793(97)01562-7 | DOI Listing |
Mol Carcinog
January 2025
Department of Hepatobiliary Surgery, The Central Hospital of Wuhan, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei Province, China.
Hepatocellular carcinoma (HCC) is a common primary malignancy of the liver and has a high mortality. Major facilitator superfamily domain containing 2 (MFSD2A) was previously demonstrated to inhibit tumor progression in several cancers. Here, we elucidated the association between MFSD2A expression and HCC progression and also investigated the underlying mechanism.
View Article and Find Full Text PDFJ Clin Lipidol
October 2024
Department of Biomedical Sciences, Western University of Health Sciences, Pomona, CA, USA. Electronic address:
Background: The genetic basis of hypertriglyceridemia (HTG) is complex and includes variants in Lipase Maturation Factor 1 (LMF1), an endoplasmic reticulum (ER)-chaperone involved in the post-translational activation of lipoprotein lipase (LPL).
Objective: The objective of this study was to identify and functionally characterize biallelic LMF1 variants in patients with HTG.
Methods: Genomic DNA sequencing was used to identify biallelic LMF1 variants in HTG patients without deleterious variants in LPL, apolipoprotein C-II (APOC2), glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1 (GPIHBP1) or apolipoprotein A-V (APOA5).
J Lipid Res
November 2024
Institute of Clinical Chemistry, University of Zurich and University Hospital of Zurich, Zurich, Switzerland.
Atherosclerosis
October 2024
School of Pharmacy, The University of Queensland, Brisbane, Queensland, 4102, Australia; Institute for Biomedicine and Glycomics, Griffith University, Nathan, Queensland, 4111, Australia; Discovery Biology, School of Environment and Science, Griffith University, Nathan, Queensland, 4111, Australia. Electronic address:
The subendothelial retention of circulating lipoproteins on extracellular matrix proteins and proteoglycans is one of the earliest events in the development of atherosclerosis. Multiple factors, including the size, type, composition, surrounding pH, and chemical modifications to lipoproteins, influence the electrostatic interactions between relevant moieties of the apolipoproteins on lipoproteins and the glycosaminoglycans of proteoglycans. The length and chemical composition of glycosaminoglycan chains attached to proteoglycan core proteins determine the extent of initial lipoprotein binding and retention in the artery wall.
View Article and Find Full Text PDFAtherosclerosis
September 2024
Saha Cardiovascular Research Center, University of Kentucky, Lexington, KY, USA; Department of Physiology, University of Kentucky, Lexington, KY, USA. Electronic address:
Background And Aims: Inflammatory cells within atherosclerotic lesions secrete proteolytic enzymes that contribute to lesion progression and destabilization, increasing the risk for an acute cardiovascular event. Elastase is a serine protease, secreted by macrophages and neutrophils, that may contribute to the development of unstable plaque. We previously reported interaction of endogenous protease-inhibitor proteins with high-density lipoprotein (HDL), including alpha-1-antitrypsin, an inhibitor of elastase.
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