ArticleJournal of molecular and cellular cardiology plus2025
Glyoxal is a superior fixative to formaldehyde in promoting antigenicity and structural integrity in murine cardiac tissues.
Article in Journal of molecular and cellular cardiology plus, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Background: Immunofluorescence (IF) is an essential technique for evaluating histological and biochemical changes in tissue specimens. A critical step in IF is sample fixation, typically achieved using formaldehyde-based fixatives, such as 4 % paraformaldehyde (PFA) or 10 % formalin. However, these fixatives are prone to over-fixation, which can alter antigenicity and promote artifacts. This study investigated glyoxal, a two‑carbon dialdehyde, as a potential alternative fixative for murine cardiac tissues for IF and crosslinking immunoprecipitation-mass spectrometry (xIP-MS) applications. Methods: Various concentrations and fixation durations of glyoxal were compared with 4 % PFA. Tissue structural integrity was assessed using Hematoxylin and Eosin (H&E) staining, while antigen preservation in cardiomyocytes was evaluated through fluorescent microscopy. Immunofluorescence of cardiac resident cells, including cardiac fibroblasts, smooth muscle cells, and endothelial cells were also investigated. xIP-MS assays were carried by phospholamban (PLN) immunoprecipitation in glyoxal-fixed mouse hearts, followed by mass spectrometry analysis. Results: Glyoxal showed comparable preservation of cardiac tissue architecture and myofiber integrity to PFA, but with superior antigen retention and protein detection. Fluorescent imaging was performed for sarcoplasmic reticulum markers (SERCA2 and PLN), intercalated disc proteins (N-Cadherin and Cx43), and contractile proteins (F-Actin and MyHC). Quantitative image analysis confirmed that glyoxal enhanced antibody penetration in thicker tissues (30 μm) and maintained the antigenicity of various cardiac resident cell markers. Glyoxal fixation allowed for xIP-MS by lightly crosslinking PLN with its associated protein complexes, enabling the identification of novel PLN-interacting proteins in mouse hearts. Conclusion: Our findings underscore the utility of glyoxal as a superior alternative to PFA in cardiac biochemistry research, offering improvements in the preservation of tissue morphology, antigen detection, and protein complex conservation in murine cardiac tissues.
Indexed as
Identifiers
What Socratic 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 Socratic graph.