ArticleInternational journal of biochemistry & physiology2023
Fibrinogen-Related Protein, Fgl2, of Hamster Cauda Epididymal Fluid: Enzymatic Characterization, and Identification of Fgl2-Binding Proteins and Ligand of Defective Hamster Sperm Organelles.
Article in International journal of biochemistry & physiology, 2023. 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.
- Metabolomic Analysis of Cauda Epididymal Fluid in Yaks and Cattle.Animals : an open access journal from MDPI · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The luminal environment of the mammalian epididymidis performs a dual function; sperm maturation and maintaining sperm viability. We previously identified a secretory protein (260/280KDa oligomers) of hamster cauda epididymal principal cells that binds to nonviable sperm. The 260/280KDa oligomers are composed of 64kDa FGL2 (fibrinogen-like protein-2) and 33kDa FGL1) (fibrinogen-like protein-1). The potential mechanism by which FGL2 binds to degenerative sperm is not clearly demonstrated. In this study, we report the downstream sequence of prothrombinase activity of FGL2, the identification of organelles, and characterize candidate proteins that bind FGL2. The following reaction sequence confirms that FGL2 is a phospholipid-activated serine protease; the conversion of prothrombin to thrombin by FGL2, followed by the conversion of soluble fibrinogen to insoluble fibrin polymers by thrombin. FGL2 binds intensely to tails than heads of de-membranated sperm. A spectrum of polypeptides of cauda sperm tails binds to FGL2. Proteomic analyses of 65KDa, 16kDa, and 13kDa polypeptides of tails correspond to a-Kinase anchor protein 4, glutathione peroxidase 4, and cytochrome c oxidase subunit 4, respectively. Annexin V, a calcium-dependent phosphatidylserine-binding protein localized to the flagellum and co-precipitated with FGL2. We have demonstrated a novel protective mechanism for recognizing and eliminating defective spermatozoa from viable sperm population.
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.