ArticleWorld journal of surgery2011
Helix pomatia agglutinin binding glycoproteins in thyroid tumors.
Article in World journal of surgery, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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.
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
3 citing papers in PubMed, 5 citations in OpenAlex.
- Targeting Tn Antigen Suppresses Aberrant O-Glycosylation-Elicited Metastasis in Breast Cancer.Journal of cellular and molecular medicine · 2024Article
- Role of TruncatedCancers · 2023Review
- Binding of aberrant glycoproteins recognizable by Helix pomatia agglutinin in adrenal cancers.BJS open · 2018Article
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBinding of the lectin Helix pomatia agglutinin (HPA) has been shown to be associated with poor prognosis in many human cancers, but not in thyroid cancer. The aims of the present study were to assess alteration in cellular glycosylation, detected by HPA binding, in thyroid tumors; to determine if such altered glycosylation carries any prognostic significance; and to analyze qualitative and quantitative differences of HPA-binding glycoproteins in various thyroid tumors.
methodsLectin histochemistry was performed on 110 archival paraffin wax embedded specimens of various thyroid tumors excised between the years 1983-1993. Demographic data, histological data, and time to death were recorded, and multivariate Cox regression analysis was performed to determine a prognostic model for patient survival based on the data. Helix pomatia agglutinin binding glycoproteins were isolated from 128 fresh specimens of various thyroid tissues by affinity chromatography, analyzed by SDS-PAGE and western blotting.
resultsThere was a marked qualitative difference in the profile of HPA-binding glycoproteins, with the malignant thyroid tumors showing a heterogeneous profile of numerous HPA binding glycoprotein bands. Lectin histochemistry showed significant positive HPA binding in malignant thyroid tumors (p = 0.0009). Kaplan-Meir survival analysis revealed that among patients who died of their disease those with HPA-positive tumors had a significantly shorter survival (p = 0.009).
conclusionsThis is the first study showing that HPA binding glycoproteins are synthesized by thyroid tumors. Thyroid cancers show a broader profile of HPA binding glycoproteins compared to benign thyroid tumors, and positive HPA binding is significantly associated with shorter survival and poorer prognosis in thyroid cancers.
Indexed as
Identifiers
What OpenQuestion holds
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.