ArticleTraffic (Copenhagen, Denmark)2015
Functional Roles of N-Linked Glycosylation of Human Matrix Metalloproteinase 9.
Article in Traffic (Copenhagen, Denmark), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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
19 citing papers in PubMed, 27 citations in OpenAlex.
- Metformin Directly Binds to MMP-9 to Improve Plaque Stability.Journal of cardiovascular development and disease · 2023Article
- MMP9: A Tough Target for Targeted Therapy for Cancer.Cancers · 2022Review
- Protein post-translational modifications after spinal cord injury.Neural regeneration research · 2021Review
- Infarct in the Heart: What's MMP-9 Got to Do with It?Biomolecules · 2021Review
- The HSP GRP94 interacts with macrophage intracellular complement C3 and impacts M2 profile during ER stress.Cell death & disease · 2021Article
- Thermal stability of human matrix metalloproteinases.Heliyon · 2020Article
- Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases.International journal of molecular sciences · 2019Review
- Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.The FEBS journal · 2019Article
- An Interplay Between Reaction-Diffusion and Cell-Matrix Adhesion Regulates Multiscale Invasion in Early Breast Carcinomatosis.Frontiers in physiology · 2019Article
- Assigning matrix metalloproteinase roles in ischaemic cardiac remodelling.Nature reviews. Cardiology · 2018Review
- NEDD9 stimulated MMP9 secretion is required for invadopodia formation in oral squamous cell carcinoma.Oncotarget · 2018Article
- Nucleic acid-induced potentiation of matrix metalloproteinase-9 enzymatic activity.The Biochemical journal · 2018Article
- Acute- and late-phase matrix metalloproteinase (MMP)-9 activity is comparable in female and male rats after peripheral nerve injury.Journal of neuroinflammation · 2018Article
- Role of N-glycosylation in activation of proMMP-9. A molecular dynamics simulations study.PloS one · 2018Article
- The secretion and biological function of tumor suppressor maspin as an exosome cargo protein.Oncotarget · 2017Article
- Secreted dual reporter assay with Gaussia luciferase and the red fluorescent protein mCherry.PloS one · 2017Article
- Endoplasmic Reticulum Malfunction in the Nervous System.Frontiers in neuroscience · 2017Article
- Effects of Glycosylation on the Enzymatic Activity and Mechanisms of Proteases.International journal of molecular sciences · 2016Review
- Glycosylation of matrix metalloproteases and tissue inhibitors: present state, challenges and opportunities.The Biochemical journal · 2016Review
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
Matrix metalloproteinase-9 (MMP-9) is a secreted endoproteinase with a critical role in the regulation of the extracellular matrix and proteolytic activation of signaling molecules. Human (h)MMP-9 has two well-defined N-glycosylation sites at residues N38 and N120; however, their role has remained mostly unexplored partly because expression of the N-glycosylation-deficient N38S has been difficult due to a recently discovered single nucleotide polymorphism-dependent miRNA-mediated inhibitory mechanism. hMMP-9 cDNA encoding amino acid substitutions at residues 38 (modified-S38, mS38) or 120 (N120S) were created in the background of a miRNA-binding site disrupted template and expressed by transient transfection. hMMP-9 harboring a single mS38 replacement secreted well, whereas N120S, or a double mS38/N120S hMMP-9 demonstrated much reduced secretion. Imaging indicated endoplasmic reticulum (ER) retention of the non-secreted variants and co-immunoprecipitation confirmed an enhanced strong interaction between the non-secreted hMMP-9 and the ER-resident protein calreticulin (CALR). Removal of N-glycosylation at residue 38 revealed an amino acid-dependent strong interaction with CALR likely preventing unloading of the misfolded protein from the ER chaperone down the normal secretory pathway. As with other glycoproteins, N-glycosylation strongly regulates hMMP-9 secretion. This is mediated, however, through a novel mechanism of cloaking an N-glycosylation-independent strong interaction with the ER-resident CALR.
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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.