ArticleThe Biochemical journal2002
Synthesis and secretion of Muc4/sialomucin complex: implication of intracellular proteolysis.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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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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.
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Who cites it
17 citing papers in PubMed, 46 citations in OpenAlex.
- VWD domain stabilization by autocatalytic Asp-Pro cleavage.Protein science : a publication of the Protein Society · 2024Article
- Mucin in cancer: a stealth cloak for cancer cells.BMB reports · 2021Review
- MUC4-ErbB2 Oncogenic Complex: Binding studies using Microscale Thermophoresis.Scientific reports · 2019Article
- SUSD2 Proteolytic Cleavage Requires the GDPH Sequence and Inter-Fragment Disulfide Bonds for Surface Presentation of Galectin-1 on Breast Cancer Cells.International journal of molecular sciences · 2019Article
- Mucin-Microbiota Interaction During Postnatal Maturation of the Intestinal Ecosystem: Clinical Implications.Digestive diseases and sciences · 2016Review
- The adenocarcinoma cell surface mucin receptor for alpha-fetoprotein: is the same receptor present on circulating monocytes and macrophages? A commentary.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Review
- MUC16 (CA125): tumor biomarker to cancer therapy, a work in progress.Molecular cancer · 2014Review
- Review of the adenocarcinoma cell surface receptor for human alpha-fetoprotein; proposed identification of a widespread mucin as the tumor cell receptor.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Review
- Membrane-tethered mucins have multiple functions on the ocular surface.Experimental eye research · 2010Review
- Regulation of the membrane mucin Muc4 in corneal epithelial cells by proteosomal degradation and TGF-beta.Journal of cellular physiology · 2010Article
- Muc4/MUC4 functions and regulation in cancer.Future oncology (London, England) · 2009Review
- Release of membrane-associated mucins from ocular surface epithelia.Investigative ophthalmology & visual science · 2008Article
- Structure, evolution, and biology of the MUC4 mucin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008Review
- Mucin dynamics in intestinal bacterial infection.PloS one · 2008Article
- Review
- Evidence for a second peptide cleavage in the C-terminal domain of rodent intestinal mucin Muc3.The Biochemical journal · 2004Article
- Selectin-mucin interactions as a probable molecular explanation for the association of Trousseau syndrome with mucinous adenocarcinomas.The Journal of clinical investigation · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Muc4/sialomucin complex (SMC) is a heterodimeric glycoprotein complex implicated in epithelial protection and overexpressed in some tumours. It is encoded by a single gene, and the two subunits are produced by proteolytic cleavage at a time before substantial O-glycosylation, near the time of transit from the endoplasmic reticulum to the Golgi. Although Muc4/SMC is translated as a membrane protein, it is produced as a soluble form in many epithelia. Transfection experiments using Cos-7, HBL-100 human epithelial, MCF-7 human breast tumour and HC11 mouse mammary cell lines showed that soluble rat Muc4/SMC is produced by a proteolytic cleavage mechanism and released by secretion from multiple cell lines, including both human and mouse normal epithelial cells and tumour cells. Similar transfection experiments demonstrated the same mechanism for the human analogue MUC4. Gel electrophoresis analyses of deglycosylated membrane and soluble transmembrane subunits and of the membrane-associated cleavage fragment indicated a released cleavage product of 25 kDa, resulting from cleavage between two epidermal growth factor-like domains. Further evidence for this site was obtained from deletion mutants removing this region of the protein, which blocked secretion. Finally, pulse-chase analyses of Muc4/SMC biosynthesis indicated no kinetic difference between the timing of the cleavage to release the soluble form and that to produce the two subunits, indicating that the soluble form is created early in transit to the cell surface. These studies provide the first clear evidence that membrane mucins can be released from cells by an intracellular proteolytic mechanism that leads to secretion of the soluble form of the mucin.
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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.