Regulated mucin secretion from airway epithelial cells
Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is propelled by neighboring ciliated cells, providing a mobile barrier which removes inhaled particles and pathogens from the lungs. Several fea...
Saved in:
Published in | Frontiers in endocrinology (Lausanne) Vol. 4; p. 129 |
---|---|
Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Switzerland
Frontiers Media S.A
18.09.2013
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is propelled by neighboring ciliated cells, providing a mobile barrier which removes inhaled particles and pathogens from the lungs. Several features of the intracellular trafficking of mucins make the airway secretory cell an interesting comparator for the cell biology of regulated exocytosis. Polymeric mucins are exceedingly large molecules (up to 3 × 10(6) Da per monomer) whose folding and initial polymerization in the ER requires the protein disulfide isomerase Agr2. In the Golgi, mucins further polymerize to form chains and possibly branched networks comprising more than 20 monomers. The large size of mucin polymers imposes constraints on their packaging into transport vesicles along the secretory pathway. Sugar side chains account for >70% of the mass of mucins, and their attachment to the protein core by O-glycosylation occurs in the Golgi. Mature polymeric mucins are stored in large secretory granules ∼1 μm in diameter. These are translocated to the apical membrane to be positioned for exocytosis by cooperative interactions among myristoylated alanine-rich C kinase substrate, cysteine string protein, heat shock protein 70, and the cytoskeleton. Mucin granules undergo exocytic fusion with the plasma membrane at a low basal rate and a high stimulated rate. Both rates are mediated by a regulated exocytic mechanism as indicated by phenotypes in both basal and stimulated secretion in mice lacking Munc13-2, a sensor of the second messengers calcium and diacylglycerol (DAG). Basal secretion is induced by low levels of activation of P2Y2 purinergic and A3 adenosine receptors by extracellular ATP released in paracrine fashion and its metabolite adenosine. Stimulated secretion is induced by high levels of the same ligands, and possibly by inflammatory mediators as well. Activated receptors are coupled to phospholipase C by Gq, resulting in the generation of DAG and of IP3 that releases calcium from apical ER. Stimulated secretion requires activation of the low affinity calcium sensor Synaptotagmin-2, while a corresponding high affinity calcium sensor in basal secretion is not known. The core exocytic machinery is comprised of the SNARE proteins VAMP8, SNAP23, and an unknown Syntaxin protein, together with the scaffolding protein Munc18b. Common and distinct features of this exocytic system in comparison to neuroendocrine cells and neurons are highlighted. |
---|---|
AbstractList | Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is propelled by neighboring ciliated cells, providing a mobile barrier which removes inhaled particles and pathogens from the lungs. Several features of the intracellular trafficking of mucins make the airway secretory cell an interesting comparator for the cell biology of regulated exocytosis. Polymeric mucins are exceedingly large molecules (up to 3 × 10(6) Da per monomer) whose folding and initial polymerization in the ER requires the protein disulfide isomerase Agr2. In the Golgi, mucins further polymerize to form chains and possibly branched networks comprising more than 20 monomers. The large size of mucin polymers imposes constraints on their packaging into transport vesicles along the secretory pathway. Sugar side chains account for >70% of the mass of mucins, and their attachment to the protein core by O-glycosylation occurs in the Golgi. Mature polymeric mucins are stored in large secretory granules ∼1 μm in diameter. These are translocated to the apical membrane to be positioned for exocytosis by cooperative interactions among myristoylated alanine-rich C kinase substrate, cysteine string protein, heat shock protein 70, and the cytoskeleton. Mucin granules undergo exocytic fusion with the plasma membrane at a low basal rate and a high stimulated rate. Both rates are mediated by a regulated exocytic mechanism as indicated by phenotypes in both basal and stimulated secretion in mice lacking Munc13-2, a sensor of the second messengers calcium and diacylglycerol (DAG). Basal secretion is induced by low levels of activation of P2Y2 purinergic and A3 adenosine receptors by extracellular ATP released in paracrine fashion and its metabolite adenosine. Stimulated secretion is induced by high levels of the same ligands, and possibly by inflammatory mediators as well. Activated receptors are coupled to phospholipase C by Gq, resulting in the generation of DAG and of IP3 that releases calcium from apical ER. Stimulated secretion requires activation of the low affinity calcium sensor Synaptotagmin-2, while a corresponding high affinity calcium sensor in basal secretion is not known. The core exocytic machinery is comprised of the SNARE proteins VAMP8, SNAP23, and an unknown Syntaxin protein, together with the scaffolding protein Munc18b. Common and distinct features of this exocytic system in comparison to neuroendocrine cells and neurons are highlighted. Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is propelled by neighboring ciliated cells, providing a mobile barrier which removes inhaled particles and pathogens from the lungs. Several features of the intracellular trafficking of mucins make the airway secretory cell an interesting comparator for the cell biology of regulated exocytosis. Polymeric mucins are exceedingly large molecules (up to 3x10^6 D per monomer) whose folding and initial polymerization in the ER requires the protein disulfide isomerase Agr2. In the Golgi, mucins further polymerize to form chains and possibly branched networks comprising more than 20 monomers. The large size of mucin polymers imposes constraints on their packaging into transport vesicles along the secretory pathway. Sugar side chains account for >70% of the mass of mucins, and their attachment to the protein core by O-glycosylation occurs in the Golgi. Mature polymeric mucins are stored in large secretory granules ~1 um in diameter. These are translocated to the apical membrane to be positioned for exocytosis by cooperative interactions among MARCKS, cysteine string protein (CSP), HSP70 and the cytoskeleton. Mucin granules undergo exocytic fusion with the plasma membrane at a low basal rate and a high stimulated rate. Both rates are mediated by a regulated exocytic mechanism as indicated by phenotypes in both basal and stimulated secretion in mice lacking Munc13-2, a sensor of the second messengers calcium and diacylglycerol (DAG). Basal secretion is induced by low levels of activation of P2Y2 purinergic and A3 adenosine receptors by extracellular ATP released in paracrine fashion and its metabolite adenosine. Stimulated secretion is induced by high levels of the same ligands, and possibly by inflammatory mediators as well. Activated receptors are coupled to phospholipase C by Gq, resulting in the generation of DAG and of Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is propelled by neighboring ciliated cells, providing a mobile barrier which removes inhaled particles and pathogens from the lungs. Several features of the intracellular trafficking of mucins make the airway secretory cell an interesting comparator for the cell biology of regulated exocytosis. Polymeric mucins are exceedingly large molecules (up to 3 × 10 6 Da per monomer) whose folding and initial polymerization in the ER requires the protein disulfide isomerase Agr2. In the Golgi, mucins further polymerize to form chains and possibly branched networks comprising more than 20 monomers. The large size of mucin polymers imposes constraints on their packaging into transport vesicles along the secretory pathway. Sugar side chains account for >70% of the mass of mucins, and their attachment to the protein core by O-glycosylation occurs in the Golgi. Mature polymeric mucins are stored in large secretory granules ∼1 μm in diameter. These are translocated to the apical membrane to be positioned for exocytosis by cooperative interactions among myristoylated alanine-rich C kinase substrate, cysteine string protein, heat shock protein 70, and the cytoskeleton. Mucin granules undergo exocytic fusion with the plasma membrane at a low basal rate and a high stimulated rate. Both rates are mediated by a regulated exocytic mechanism as indicated by phenotypes in both basal and stimulated secretion in mice lacking Munc13-2, a sensor of the second messengers calcium and diacylglycerol (DAG). Basal secretion is induced by low levels of activation of P 2 Y 2 purinergic and A3 adenosine receptors by extracellular ATP released in paracrine fashion and its metabolite adenosine. Stimulated secretion is induced by high levels of the same ligands, and possibly by inflammatory mediators as well. Activated receptors are coupled to phospholipase C by Gq, resulting in the generation of DAG and of IP 3 that releases calcium from apical ER. Stimulated secretion requires activation of the low affinity calcium sensor Synaptotagmin-2, while a corresponding high affinity calcium sensor in basal secretion is not known. The core exocytic machinery is comprised of the SNARE proteins VAMP8, SNAP23, and an unknown Syntaxin protein, together with the scaffolding protein Munc18b. Common and distinct features of this exocytic system in comparison to neuroendocrine cells and neurons are highlighted. |
Author | Tuvim, Michael J Adler, Kenneth B Dickey, Burton F |
AuthorAffiliation | 2 Department of Pulmonary Medicine, The University of Texas MD Anderson Cancer Center , Houston, TX , USA 1 Department of Molecular Biomedical Sciences, North Carolina State University College of Veterinary Medicine , Raleigh, NC , USA |
AuthorAffiliation_xml | – name: 1 Department of Molecular Biomedical Sciences, North Carolina State University College of Veterinary Medicine , Raleigh, NC , USA – name: 2 Department of Pulmonary Medicine, The University of Texas MD Anderson Cancer Center , Houston, TX , USA |
Author_xml | – sequence: 1 givenname: Kenneth B surname: Adler fullname: Adler, Kenneth B organization: Department of Molecular Biomedical Sciences, North Carolina State University College of Veterinary Medicine , Raleigh, NC , USA – sequence: 2 givenname: Michael J surname: Tuvim fullname: Tuvim, Michael J – sequence: 3 givenname: Burton F surname: Dickey fullname: Dickey, Burton F |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24065956$$D View this record in MEDLINE/PubMed |
BookMark | eNpVkUtLJDEQgIMovu-epI97mTHvx0UQWR8gCKLnkE6qx0h3Z0y6d5l_b8-MitYlRVL1VajvCO32qQeEzgieM6bNRQN9SHOKCZtjTKjZQYdESj6jzNDdH_kBOi3lDU_BMTFG76MDyrEURshDJJ9gMbZugFB1o499VcBnGGLqqyanrnIx_3erCpZxeIU2urby0LblBO01ri1w-nkeo5ebv8_Xd7OHx9v766uHmeecmVmQUjWMCqIJU8yAkUQEDDpQxmVNPBbSa0_rQEF4VYOpCSeskUqJoLgz7Bjdb7khuTe7zLFzeWWTi3ZzkfLCujxE34J1gStRA9EqCE6M0LVTGjzDjePeazexLres5Vh3EDz0Q3btL-jvlz6-2kX6Z5lSkio6Af58AnJ6H6EMtotlvQ7XQxqLJWJaMJZKqqkUb0t9TqVkaL7HEGzX9uzGnl3bsxt7U8v5z-99N3y5Yh_F1ZfU |
CitedBy_id | crossref_primary_10_1093_rheumatology_kev026 crossref_primary_10_2147_JIR_S280958 crossref_primary_10_1155_2016_7984853 crossref_primary_10_1155_2019_7084734 crossref_primary_10_1038_s41522_018_0067_0 crossref_primary_10_1073_pnas_2205277119 crossref_primary_10_1016_j_prp_2021_153533 crossref_primary_10_1152_ajpgi_00198_2015 crossref_primary_10_3892_mmr_2018_9015 crossref_primary_10_1242_dmm_049266 crossref_primary_10_36106_gjra_5907463 crossref_primary_10_1021_acsanm_2c03887 crossref_primary_10_1186_s13578_024_01220_w crossref_primary_10_1371_journal_pone_0127267 crossref_primary_10_1172_JCI123524 crossref_primary_10_1183_09031936_00141514 crossref_primary_10_1042_BSR20150004 crossref_primary_10_2174_1568009620666201116113334 crossref_primary_10_1038_mt_2016_182 crossref_primary_10_1186_s12931_016_0446_0 crossref_primary_10_1038_s41578_021_00396_8 crossref_primary_10_1055_s_0043_1769919 crossref_primary_10_1111_jgh_15596 crossref_primary_10_1513_AnnalsATS_201806_368AW crossref_primary_10_3389_fmicb_2020_589501 crossref_primary_10_1016_j_crtox_2020_08_002 crossref_primary_10_1002_jcp_25044 crossref_primary_10_1016_j_mam_2016_11_009 crossref_primary_10_1021_acs_biomac_3c01170 crossref_primary_10_1016_j_ajpath_2017_07_009 crossref_primary_10_1016_j_toxlet_2017_08_079 crossref_primary_10_1165_rcmb_2022_0334LE crossref_primary_10_1159_000442794 crossref_primary_10_3389_fendo_2014_00048 crossref_primary_10_1016_j_pupt_2018_11_006 crossref_primary_10_1007_s10555_017_9699_4 crossref_primary_10_1089_ars_2018_7647 crossref_primary_10_3892_ijo_2015_3090 crossref_primary_10_1089_jamp_2014_1190 crossref_primary_10_1002_chem_201800790 crossref_primary_10_1152_ajplung_00123_2019 crossref_primary_10_1177_0192623319873872 crossref_primary_10_1038_mi_2015_53 crossref_primary_10_1186_s12906_023_04251_x crossref_primary_10_1152_ajpcell_00073_2016 crossref_primary_10_3389_fevo_2023_1202410 crossref_primary_10_1128_mBio_01323_17 crossref_primary_10_1007_s13258_014_0203_z crossref_primary_10_3390_v10050225 crossref_primary_10_1152_ajplung_00487_2021 crossref_primary_10_1186_s12931_016_0378_8 crossref_primary_10_2131_jts_44_107 crossref_primary_10_1016_j_ceca_2015_10_002 crossref_primary_10_3390_cells11050812 crossref_primary_10_1016_j_addr_2017_09_023 crossref_primary_10_7554_eLife_73926 crossref_primary_10_4049_jimmunol_1400978 crossref_primary_10_2147_JIR_S318327 crossref_primary_10_1165_rcmb_2015_0171OC crossref_primary_10_3390_ijms24119560 crossref_primary_10_1007_s40265_014_0235_3 crossref_primary_10_1371_journal_pgen_1008306 crossref_primary_10_1007_s11302_020_09700_7 crossref_primary_10_1016_j_yexmp_2017_02_016 crossref_primary_10_7554_eLife_84375 crossref_primary_10_1016_j_redox_2014_01_004 crossref_primary_10_7554_eLife_39729 crossref_primary_10_1016_j_semcancer_2015_04_005 crossref_primary_10_1074_jbc_RA117_000848 crossref_primary_10_1152_ajplung_00157_2018 crossref_primary_10_1016_j_ejps_2023_106567 crossref_primary_10_1177_15330338211043328 crossref_primary_10_3389_fphys_2023_1323865 crossref_primary_10_2147_JIR_S271292 crossref_primary_10_3389_fphys_2024_1392443 crossref_primary_10_1042_BST20170455 crossref_primary_10_3892_ijmm_2015_2133 crossref_primary_10_1021_acs_langmuir_0c02410 crossref_primary_10_3389_fmicb_2018_01939 crossref_primary_10_26508_lsa_201900462 crossref_primary_10_1007_s00011_023_01786_0 crossref_primary_10_1177_03946320221106504 crossref_primary_10_1016_j_taap_2024_116886 crossref_primary_10_1513_AnnalsATS_201806_371AW crossref_primary_10_1038_mi_2015_32 crossref_primary_10_1097_MIB_0000000000000117 crossref_primary_10_1165_rcmb_2018_0285TR crossref_primary_10_1007_s00795_020_00274_2 |
ContentType | Journal Article |
Copyright | Copyright © 2013 Adler, Tuvim and Dickey. 2013 |
Copyright_xml | – notice: Copyright © 2013 Adler, Tuvim and Dickey. 2013 |
DBID | NPM AAYXX CITATION 7X8 5PM DOA |
DOI | 10.3389/fendo.2013.00129 |
DatabaseName | PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) Directory of Open Access Journals |
DatabaseTitle | PubMed CrossRef MEDLINE - Academic |
DatabaseTitleList | PubMed |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website – sequence: 2 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Medicine |
EISSN | 1664-2392 |
EndPage | 129 |
ExternalDocumentID | oai_doaj_org_article_ad475be187d541958ba78ec30fa4cc8a 10_3389_fendo_2013_00129 24065956 |
Genre | Journal Article Review |
GrantInformation_xml | – fundername: NHLBI NIH HHS grantid: R01 HL097000 – fundername: NHLBI NIH HHS grantid: R21 HL094848 – fundername: NHLBI NIH HHS grantid: R37 HL036982 – fundername: NHLBI NIH HHS grantid: R01 HL036982 |
GroupedDBID | 53G 5VS 9T4 AAFWJ AAKDD ACGFO ACGFS ACXDI ADBBV ADRAZ AFPKN ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BCNDV DIK EMOBN GROUPED_DOAJ GX1 HYE IAO IHR IPNFZ KQ8 M48 M~E NPM OK1 PGMZT RIG RPM AAYXX CITATION IEA IHW 7X8 5PM |
ID | FETCH-LOGICAL-c4439-d667f3251813739e9615d0e8d2346b1c056c8c2bd2e5c7be9b1413f6775d74a93 |
IEDL.DBID | RPM |
ISSN | 1664-2392 |
IngestDate | Fri Oct 04 13:12:15 EDT 2024 Tue Sep 17 21:24:37 EDT 2024 Fri Aug 16 09:05:47 EDT 2024 Thu Sep 26 18:16:32 EDT 2024 Sat Sep 28 07:52:35 EDT 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Keywords | MARCKS secretion Munc13 mucin exocytosis synaptotagmin Munc18 mucus |
Language | English |
License | This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c4439-d667f3251813739e9615d0e8d2346b1c056c8c2bd2e5c7be9b1413f6775d74a93 |
Notes | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 Edited by: Rafael Vazquez-Martinez, University of Cordoba, Spain Reviewed by: Ricardo Borges, University of La Laguna, Spain; Gunnar C. Hansson, University of Gothenburg, Sweden This article was submitted to Neuroendocrine Science, a section of the journal Frontiers in Endocrinology. |
OpenAccessLink | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3776272/ |
PMID | 24065956 |
PQID | 1540106767 |
PQPubID | 23479 |
PageCount | 1 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_ad475be187d541958ba78ec30fa4cc8a pubmedcentral_primary_oai_pubmedcentral_nih_gov_3776272 proquest_miscellaneous_1540106767 crossref_primary_10_3389_fendo_2013_00129 pubmed_primary_24065956 |
PublicationCentury | 2000 |
PublicationDate | 20130918 |
PublicationDateYYYYMMDD | 2013-09-18 |
PublicationDate_xml | – month: 9 year: 2013 text: 20130918 day: 18 |
PublicationDecade | 2010 |
PublicationPlace | Switzerland |
PublicationPlace_xml | – name: Switzerland |
PublicationTitle | Frontiers in endocrinology (Lausanne) |
PublicationTitleAlternate | Front Endocrinol (Lausanne) |
PublicationYear | 2013 |
Publisher | Frontiers Media S.A |
Publisher_xml | – name: Frontiers Media S.A |
References | 16127146 - Am J Pathol. 2005 Sep;167(3):651-61 23012413 - Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16528-33 18055557 - Am J Pathol. 2007 Dec;171(6):1822-30 16371599 - Physiol Rev. 2006 Jan;86(1):245-78 19208631 - J Biol Chem. 2009 Apr 10;284(15):9781-7 2726763 - Proc Natl Acad Sci U S A. 1989 Jun;86(11):4012-6 18258655 - J Physiol. 2008 Apr 1;586(7):1977-92 9729478 - Biochem J. 1998 Sep 15;334 ( Pt 3):685-93 23602830 - Arch Biochem Biophys. 2013 Jul 15;535(2):234-40 22403803 - Am J Respir Cell Mol Biol. 2012 Aug;47(2):178-85 18314541 - Am J Respir Cell Mol Biol. 2008 Jul;39(1):68-76 3651126 - Am Rev Respir Dis. 1987 Sep;136(3):698-703 15218074 - J Physiol. 2004 Sep 1;559(Pt 2):555-65 21896166 - Respir Res. 2011 Sep 06;12:118 22923574 - Science. 2012 Aug 24;337(6097):937-41 17463395 - Am J Respir Cell Mol Biol. 2007 Sep;37(3):273-90 20543006 - Am J Physiol Lung Cell Mol Physiol. 2010 Sep;299(3):L345-52 23125200 - Cold Spring Harb Perspect Med. 2012 Nov 01;2(11):null 23125206 - Cold Spring Harb Perspect Med. 2012 Nov 01;2(11):null 19783639 - Am J Physiol Lung Cell Mol Physiol. 2010 Jan;298(1):L15-22 17850213 - Annu Rev Physiol. 2008;70:459-86 23742042 - Am J Respir Cell Mol Biol. 2013 Oct;49(4):511-6 12649728 - Anat Embryol (Berl). 2003 Mar;206(4):301-9 20118925 - Nat Neurosci. 2010 Mar;13(3):338-43 16980555 - Am J Respir Cell Mol Biol. 2007 Feb;36(2):244-53 18096872 - Am J Respir Cell Mol Biol. 2008 Mar;38(3):256-62 16921125 - Proc Am Thorac Soc. 2006 Aug;3(6):493 16460283 - Annu Rev Physiol. 2006;68:543-61 17988208 - Annu Rev Physiol. 2008;70:487-512 12019299 - J Histochem Cytochem. 2002 Jun;50(6):829-38 22259143 - Methods Mol Biol. 2012;842:279-95 23467297 - Am J Physiol Cell Physiol. 2013 May 15;304(10):C976-84 17524805 - Trends Mol Med. 2007 Jun;13(6):231-40 20471239 - Curr Opin Cell Biol. 2010 Aug;22(4):488-95 20203291 - Am J Respir Cell Mol Biol. 2010 Aug;43(2):131-6 23187130 - J Clin Invest. 2012 Dec;122(12):4555-68 14517269 - J Gen Physiol. 2003 Oct;122(4):377-87 20926781 - Am J Physiol Cell Physiol. 2010 Dec;299(6):C1222-33 11753414 - Nat Neurosci. 2002 Jan;5(1):19-26 23442922 - Biophys J. 2013 Feb 5;104(3):716-26 21490149 - Mol Biol Cell. 2011 Jun 15;22(12):2094-105 1878744 - Br J Pharmacol. 1991 May;103(1):1053-6 22694344 - Biochem J. 2012 Sep 15;446(3):383-94 19285919 - Curr Opin Pharmacol. 2009 Jun;9(3):262-7 11533058 - J Biol Chem. 2001 Nov 2;276(44):40982-90 18003965 - N Engl J Med. 2007 Nov 15;357(20):2082-4 9252557 - Am J Physiol. 1997 Jul;273(1 Pt 1):L201-10 22451922 - Proc Natl Acad Sci U S A. 2012 Apr 10;109(15):5645-50 8670174 - Biochem J. 1996 Jun 15;316 ( Pt 3):943-51 22711878 - J Exp Med. 2012 Jul 2;209(7):1263-72 22358830 - Nature. 2012 Feb 22;482(7386):474-5 10861235 - Biochem J. 2000 Jul 1;349(Pt 1):247-53 23224297 - Histochem Cell Biol. 2013 May;139(5):717-26 23168839 - Mucosal Immunol. 2013 May;6(3):639-54 19359471 - Proc Natl Acad Sci U S A. 2009 Apr 28;106(17):6950-5 22144578 - J Physiol. 2012 Feb 1;590(3):545-62 22183981 - Glycobiology. 2012 Jun;22(6):736-56 10430018 - Eur J Cell Biol. 1999 Jun;78(6):375-81 16227318 - Am J Physiol Lung Cell Mol Physiol. 2006 Mar;290(3):L558-69 22923570 - Science. 2012 Aug 24;337(6097):924-5 11694445 - Am J Respir Cell Mol Biol. 2001 Oct;25(4):409-17 15191915 - Am J Respir Cell Mol Biol. 2004 Oct;31(4):382-94 1712847 - J Physiol. 1990 Dec;431:629-41 1590365 - Am J Physiol. 1992 May;262(5 Pt 1):C1313-23 15231488 - Am J Respir Cell Mol Biol. 2004 Oct;31(4):446-55 17850209 - Annu Rev Physiol. 2008;70:431-57 22945630 - J Clin Invest. 2012 Oct;122(10):3629-34 17192432 - J Neurosci. 2006 Dec 27;26(52):13493-504 21479242 - PLoS One. 2011 Mar 29;6(3):e18444 15923355 - J Histochem Cytochem. 2005 Oct;53(10):1305-9 17728398 - Am J Physiol Cell Physiol. 2007 Nov;293(5):C1445-54 14716307 - Nat Med. 2004 Feb;10(2):193-6 23532850 - J Biol Chem. 2013 May 3;288(18):13046-56 16763221 - Am J Respir Cell Mol Biol. 2006 Nov;35(5):549-58 16946028 - J Appl Physiol (1985). 2007 Jan;102(1):399-405 23377348 - Am J Physiol Lung Cell Mol Physiol. 2013 Apr 15;304(8):L511-8 19164740 - Science. 2009 Jan 23;323(5913):474-7 21121836 - N Engl J Med. 2010 Dec 2;363(23 ):2233-47 |
References_xml | |
SSID | ssj0000401998 |
Score | 2.3468966 |
SecondaryResourceType | review_article |
Snippet | Secretory epithelial cells of the proximal airways synthesize and secrete gel-forming polymeric mucins. The secreted mucins adsorb water to form mucus that is... |
SourceID | doaj pubmedcentral proquest crossref pubmed |
SourceType | Open Website Open Access Repository Aggregation Database Index Database |
StartPage | 129 |
SubjectTerms | Endocrinology Exocytosis MARCKS mucin Mucus secretion synaptotagmin |
SummonAdditionalLinks | – databaseName: Directory of Open Access Journals dbid: DOA link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrZ3NS8MwGMaD7CBexG_rFxW8eCiuTZq3Oc6xMYR5UAe7heajOBjd2Afif--btJubCF68doWmzxuW30Oa5yXkLhEsQQrWWAEQEdMpj1RTQ8SzgiN-o0Pw8cX9Z94bsKdhOtxo9eW-CavigSvhXMgtpMrGGZiUuWQUlUNmNW0WOdM6q9AoTjfMlP8PRtuARqLal0QXJh4KWxp32C92iaaxJ8rvdcjH9f_GmD8_ldxYe7oHZL-GxrBVDfaQ7NjyiOz2623xY8Jfqo7y1oT9JV4KXx0MOslDd3wkbI1mH_ln2Jm6AxhjnHFh247H8xMy6Hbe2r2obogQaYbgEBnOoaBIJFlMgQorEEdM02YmoYyrWCPM6EwnyiQ21aCsUKg2LThAaoDlgp6SRjkp7TkJgWuD1ghyZlwXMiWY1bwQMRpilptEBeR-JY-cVrkXEv2Ck1J6KaWTUnopA_Lo9Fvf5xKr_QWso6zrKP-qY0BuV-pLnOFu2yIv7WQ5lwh5PuiOQ0DOqmqsH-V4JMX3CAhs1WlrLNu_lKN3n6JNAdcBSC7-Y_CXZC_xbTJEFGdXpLGYLe01wspC3fh5-QXizOZx priority: 102 providerName: Directory of Open Access Journals – databaseName: Scholars Portal Journals: Open Access dbid: M48 link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Nb9QwEB2VVkJcEFA-AgWlUi8cAhvH8cSHqmqrVlWl5QCs1Jvlr0ClVbbsdgX998w4aWGrvfTqRHH8Zpx5I2feAOwJLQWxYE8WQF1IX6vCjTwWqmkV0W_KEJJ88fiLOpvI84v64l959ADgYm1qx_2kJvPppz-_bg5ow-9zxknx9nMbu8B1fCWLlVL8egRbQlaS_X08kP30XaZUQqfmuKVSshDEDPpzy7UPWYlTSc5_HQe9_yvlf7Hp9Bk8HUhlfth7wXPYiN0LeDwejs23QX3tO87HkI-XNJR_Y7LIJsm5vCQ_vJz_tjf5yRUXaEzJI_PjOJ0uXsLk9OT78VkxNEwovCRiUQSlsK2IsTRlhZWOmuhKGMUmCELDlZ7Ijm-8cEHE2qOL2pE1qlYh1gGl1dUr2OxmXXwDOSofKHVCKwN3KXNaRq9aXVLCLG0QLoOPt_CYq14Xw1A-wVCaBKVhKE2CMoMjxu_uPla0TgOz-Q8zbBBjg8TaxbJBmpAVcJzFJvpq1FrpfWMz2L1F39AO4GMN28XZcmGIBCYhPIUZvO6tcTcV85Wa1pEBrthp5V1Wr3SXP5PKdoUUJ1C8fcBC38ETkbpl6KJsdmDzer6M74mzXLsPyRX_AnyH5oQ priority: 102 providerName: Scholars Portal |
Title | Regulated mucin secretion from airway epithelial cells |
URI | https://www.ncbi.nlm.nih.gov/pubmed/24065956 https://search.proquest.com/docview/1540106767 https://pubmed.ncbi.nlm.nih.gov/PMC3776272 https://doaj.org/article/ad475be187d541958ba78ec30fa4cc8a |
Volume | 4 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Nb9QwEB21PSAuiG9CoQoSFw7pbmLHYx_LqqVCCkJApb1Z_gqstM2utl0h_n3HTlLtIk5cfHASOXozid_IM28A3leKV8SCHVkAVcFdLQo7dVgI2Qqi3xQhJPni5ou4vOKf5_X8AOqxFiYl7Tu7OO2W16fd4lfKrVxfu8mYJzb52swY0ieM1eQQDpGxnRA9_X4pYqAYoj-SpABMTdrQ-VjnV0YxU9rfogAwj-eJsWv1zm6URPv_xTT_Tpjc2YEuHsOjgTrmZ_0rPoGD0D2FB81wOP4MxLe-r3zwebOlqfx7pIQR-DwWkeRni81v8yc_X8cyjCX5XT4Ly-XNc7i6OP8xuyyGtgiF40QfCi8Etox4iSwZMhUUkRI_DdJXjAtbOqI0TrrK-irUDm1QljBnrUCsPXKj2As46lZdeAU5CucJBTTcx15kVvHgRKtKCou58ZXN4MMIj1736heaooaIqk6o6oiqTqhm8DHid39f1K1OE6vNTz1YTxvPsbahlEgLRp0ba1AGx6at4c5Jk8G7EX1Nfh4PL0wXVtsbTVQvyd0JzOBlb437pUZrZoB7dtp7l_0r5FpJS3twpdf__eQxPKxShwxVlPINHN1utuEt8ZRbe5Liexo_zUsaGy5PkqfeAd1o6M8 |
link.rule.ids | 230,315,733,786,790,870,891,2115,24346,27955,27956,53825,53827 |
linkProvider | National Library of Medicine |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1LT9wwEB5RKrVc6BtCX6nUSw_Z3TiOHR_pCrS0BFUtVNwsv1JWLNnVsquq_PqOnQTtol7o1U5kx58df6OZ-QbgIxGUIAs2iAAXCTU5S_TA8IQVFUP6jRZCkC8uT9jojH45z883IO9yYULQvtHjXj256tXjixBbObsy_S5OrP-tHGYcjzAn_QfwEM8ryVeM9PADRpsBrYjGKYkmmOhXrrY-0y_1cqZ4w3kJYOo9ir5u9cp9FGT7_8U174ZMrtxBh0_gZzf7JvTksrdc6J65uSPseO_PewrbLSuN95vuZ7Dh6ufwqGz97i-AfW9K1jsbl0tsin94tukxjX1-Srw_nv9Wf-KDmc_wmOCWjoduMrl-CWeHB6fDUdJWXEgMRWaSWMZ4lSHlKdKMZ8IJ5Dt24ApLMsp0apAtmcIQbYnLDddOaIQzqxjnueVUiewVbNbT2u1CzJmxuLxcUevLnGlBnWGVSNHipsoSHcGnbt3lrBHWkGiQeLhkgEt6uGSAK4LPHpjb57wkdmiYzn_JduWkspTn2qUFxwG9hI5WvHAmG1SKGlOoCD50sEo8Qt4vomo3XV5LZJFBSY_xCHYamG-H6rZJBHxtA6zNZb0HYQ0y3S2Me__95nt4PDotj-Xx0cnX17BFQiEOkaTFG9hczJfuLdKhhX4XNv9fx4UIFg |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB5BkSoulGcJzyBx4ZDNJnE88bEsXZXHVhVQqeJi-RVYsc2utruq4NczdpJqt-LUq-PIsb9x_I1m_A3A21ywnFiwIQRQJMyUPNFDgwmvak70mzyEIF88OeZHp-zTWXm2UeorJO0bPR00s_NBM_0VcisX5ybt88TSk8moQNrCmKcLW6e34Q7t2Rw3HPXwEya_gTyJNjBJbphIa9dYf9sv85KmdMp5GWDmo4q-dvXGmRSk-__HN6-nTW6cQ-M9-NHPoE0_-T1Yr_TA_L0m7nijKd6Hex07jQ_aLg_glmsewu6ki78_Av61LV3vbDxZU1P8zbNOj23s76nEB9PlpfoTHy78TY8ZmXY8crPZxWM4HR9-Hx0lXeWFxDBiKInlHOuCqE-VFVgIJ4j32KGrbF4wrjNDrMlUJtc2d6VB7YQmWIuaI5YWmRLFE9hp5o17CjFyY2mJUTHry51pwZzhtcjI82bK5jqCd_3ay0UrsCHJMfGQyQCZ9JDJAFkE7z04V_28NHZomC9_ym71pLIMS-2yCmlAL6WjFVbOFMNaMWMqFcGbHlpJW8nHR1Tj5usLSWwyKOpxjGC_hfpqqN5UIsAtI9j6lu0nBG2Q6-6gfHbjN1_D7smHsfzy8fjzc7ibh3ocIsmqF7CzWq7dS2JFK_0q2P8_HMIKlg |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Regulated+Mucin+Secretion+from+Airway+Epithelial+Cells&rft.jtitle=Frontiers+in+endocrinology+%28Lausanne%29&rft.au=Adler%2C+Kenneth+B.&rft.au=Tuvim%2C+Michael+J.&rft.au=Dickey%2C+Burton+F.&rft.date=2013-09-18&rft.issn=1664-2392&rft.eissn=1664-2392&rft.volume=4&rft_id=info:doi/10.3389%2Ffendo.2013.00129&rft.externalDBID=n%2Fa&rft.externalDocID=10_3389_fendo_2013_00129 |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1664-2392&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1664-2392&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1664-2392&client=summon |