ArticleJournal of cellular biology & molecular sciences2016
Expression of Syntaxin 2 in Bovine Sperm.
Article in Journal of cellular biology & molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed, 0 citations in OpenAlex.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Syntaxins are membrane integrated Q-SNARE proteins known to participate in exocytosis. Vesicle docking involves the binding of two plasma membrane proteins, syntaxin and SNAP-25, to the vesicle membrane protein VAMP to form a stable trimeric core complex; synaptophysin is thought to regulate the formation of this complex. Although the members of Q-SNARE proteins are characterized in somatic cells, it is not known whether related proteins function in the sperm acrosome reaction. The objective of the present study is to identify and localize syntaxin in bovine epididymal spermatozoa and to determine the fate of syntaxin 2 during the acrosome reaction. Western blots of caput and cauda sperm lysates and plasma membrane fractions, stained with anti-syntaxin 2, revealed the presence of a 31kDa band in both sperm lysates and plasma membrane fractions, respectively. Indirect immunofluorescence localized syntaxin 2 to the anterior but not the equatorial regions of the acrosomal segment. Several biochemical analyses demonstrated that syntaxin 2 is an integral component of bovine cauda sperm plasma membranes. Our immunoblot data reveals that syntaxin 2 of bovine cauda sperm is released after lysophosphatidylcholine (LPC)-induced acrosomal exocytosis. It is assumed that syntaxin 2 may be involved in triggering the acrosome reaction through a ligand-receptor mediated signal transduction pathway.
Indexed as
Identifiers
28435937PMC5400102W2520866062What 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.