ArticleJournal of cell science2022
Characterization of lipoprotein lipase storage vesicles in 3T3-L1 adipocytes.
Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- Cryogenic electron tomography reveals helical organization of lipoprotein lipase in storage vesicles.Science advances · 2025Article
- Secretion and transfer of adipose lipoprotein lipase utilizes neutral sphingomyelinase 2 generated exosomes.bioRxiv : the preprint server for biology · 2025Article
- The mechanisms to dispose of misfolded proteins in the endoplasmic reticulum of adipocytes.Nature communications · 2023Article
- Structure of dimeric lipoprotein lipase reveals a pore adjacent to the active site.Nature communications · 2023Article
- Transcriptome Profiling of Developing Ovine Fat Tail Tissue Reveals an Important Role forFrontiers in cell and developmental biology · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lipoprotein lipase (LPL) is a secreted triglyceride lipase involved in the clearance of very-low-density lipoproteins and chylomicrons from circulation. LPL is expressed primarily in adipose and muscle tissues and transported to the capillary lumen. LPL secretion is regulated by insulin in adipose tissue; however, few studies have examined the regulatory and trafficking steps involved in secretion. Here, we describe the intracellular localization and insulin-dependent trafficking of LPL in 3T3-L1 adipocytes. We compared LPL trafficking to the better characterized trafficking pathways taken by leptin and GLUT4 (also known as SLC2A4). We show that the LPL trafficking pathway shares some characteristics of these other pathways, but that LPL subcellular localization and trafficking are distinct from those of GLUT4 and leptin. LPL secretion occurs slowly in response to insulin and rapidly in response to the Ca2+ ionophore ionomycin. This regulated trafficking is dependent on Golgi protein kinase D and the ADP-ribosylation factor GTPase ARF1. Together, these data give support to a new trafficking pathway for soluble cargo that is active in adipocytes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.