Evidence map›Paper›PMID 9480884›Full record

ArticleThe Biochemical journal1998

Sialomucin complex in the rat respiratory tract: a model for its role in epithelial protection.

R R McNeer, D Huang, N L Fregien, K L Carraway

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Muc4/MUC4 functions and regulation in cancer.Future oncology (London, England) · 2009
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Muc4/sialomucin complex in the mammary gland and breast cancer.Journal of mammary gland biology and neoplasia · 2001
    Review
  12. Article
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

R R McNeerDepartment of Cell Biology and Anatomy, University of Miami School of Medicine, Miami, FL 33101, USA.
D Huang
N L Fregien
K L Carraway
University of Miami · US

Funding

STRUCTURE/BIOSYNTHESIS OF TUMOR SIALOMUCIN COMPLEXR01CA052498 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI CARRAWAY, KERMIT L. · 1991 to 2009
$2.7M
CORE--WORD PROCESSING CENTERP30CA014395 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · 1985 to 1995
–
NCI NIH HHS CA 14395NCI NIH HHS CA 52498
6 · The paper itself

Abstract

The pulmonary epithelium has a multitude of specialized functions, which depend on regulated growth and differentiation of several cell types. One such function is the synthesis and secretion of mucins, which offer the epithelium protection from and a means for removal of noxious environmental factors. Sialomucin complex (SMC) is a heterodimeric glycoprotein consisting of a mucin subunit (ASGP-1, ascites sialoglycoprotein-1) and a transmembrane protein (ASGP-2) with two epidermal-growth-factor-like domains. SMC was originally discovered in a highly metastatic rat mammary adenocarcinoma and has been implicated in metastasis and in the protection of the tumour cells from natural killer cells. It can also act as a ligand for the receptor tyrosine kinase 185(neu), suggesting that it is bifunctional as well as heterodimeric. SMC is expressed on the epithelium of rat conducting airways, with the highest levels occurring in the proximal trachea and progressively decreasing into the bronchioles. Airway SMC consists of two forms: a soluble form that lacks the C-terminal cytoplasmic and transmembrane domains and accounts for about 70% of the total, and a membrane-associated form that has the C-terminal domains. Immunocytochemical analyses show that SMC is predominantly present on the apical surfaces of the airway epithelium, but not in goblet cells. Soluble form can be removed from the trachea by rinsing, suggesting that a fraction of the protein is adsorbed to the apical surface. Based on these results, we propose a protective mechanism in which membrane and soluble forms of SMC are produced by airway luminal epithelial cells to provide a cell-associated epithelial glycoprotein barrier that also serves as an interface with flowing mucus. In support of this mechanism, we demonstrated secretion of soluble SMC by primary cultures of tracheal epithelial cells. This model suggests that SMC is a critical element in the protective barrier of the airway epithelium.

Indexed as

Respiratory Physiological PhenomenaAnimalsCells, CulturedEpithelial CellsFemaleModels, BiologicalMucin-4MucinsRatsRats, Inbred F344Respiratory SystemSialoglycoproteinsSialomucinsMucin-4MucinsSialoglycoproteinsSialomucins

Identifiers

PMID9480884
PMCPMC1219199
OpenAlexW1892540398

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.