ArticleJournal of cellular biochemistry2003
Profibrillin-1 maturation by human dermal fibroblasts: proteolytic processing and molecular chaperones.
Article in Journal of cellular biochemistry, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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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.
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Who cites it
16 citing papers in PubMed, 45 citations in OpenAlex.
- Structural studies of elastic fibre and microfibrillar proteins.Matrix biology plus · 2021Article
- Assembly assay identifies a critical region of human fibrillin-1 required for 10-12 nm diameter microfibril biogenesis.PloS one · 2021Article
- Placensin is a glucogenic hormone secreted by human placenta.EMBO reports · 2020Article
- Fibrillin-1 and fibrillin-1-derived asprosin in adipose tissue function and metabolic disorders.Journal of cell communication and signaling · 2020Review
- Review
- The role of fibrillin and microfibril binding proteins in elastin and elastic fibre assembly.Matrix biology : journal of the International Society for Matrix Biology · 2019Review
- Expression of FBN1 during adipogenesis: Relevance to the lipodystrophy phenotype in Marfan syndrome and related conditions.Molecular genetics and metabolism · 2016Article
- Fibrillin-containing microfibrils are key signal relay stations for cell function.Journal of cell communication and signaling · 2015Article
- Genetic ablation of N-linked glycosylation reveals two key folding pathways for R345W fibulin-3, a secreted protein associated with retinal degeneration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- MFAP5 loss-of-function mutations underscore the involvement of matrix alteration in the pathogenesis of familial thoracic aortic aneurysms and dissections.American journal of human genetics · 2014Article
- C-terminal propeptide is required for fibrillin-1 secretion and blocks premature assembly through linkage to domains cbEGF41-43.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- Assembly of fibrillin microfibrils governs extracellular deposition of latent TGF beta.Journal of cell science · 2010Article
- Biogenesis and function of fibrillin assemblies.Cell and tissue research · 2010Review
- Cell-surface processing of the metalloprotease pro-ADAMTS9 is influenced by the chaperone GRP94/gp96.The Journal of biological chemistry · 2010Article
- Tissue elasticity and the ageing elastic fibre.Age (Dordrecht, Netherlands) · 2009Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Fibrillin-1 is synthesized as a proprotein that undergoes proteolytic processing in the unique C-terminal domain by a member of the PACE/furin family of endoproteases. This family of endoproteases is active in the trans-Golgi network (TGN), but metabolic labeling studies have been controversial as to whether profibrillin-1 is processed intracellularly or after secretion. This report provides evidence that profibrillin-1 processing is not an intracellular event. Bafilomycin A(1) and incubation of dermal fibroblasts at 22 degrees C were used to block secretion in the TGN to confirm that profibrillin-1 processing did not occur in this compartment. Profibrillin-1 immunoprecipitation studies revealed that two endoplasmic reticulum-resident molecular chaperones, BiP and GRP94, interacted with profibrillin-1. To determine the proprotein convertase responsible for processing profibrillin-1, a specific inhibitor of furin, alpha-1-antitrypsin, Portland variant, was both expressed in the cells and added to cells exogenously. In both cases, the inhibitor blocked the processing of profibrillin-1, providing evidence that furin is the enzyme responsible for profibrillin-1 processing. These studies delineate the secretion and proteolytic processing of profibrillin-1, and identify the proteins that interact with profibrillin-1 in the secretory pathway.
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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.