Members of the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway are present and active in human sperm.

@article{Dcruz2001MembersOT,
  title={Members of the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway are present and active in human sperm.},
  author={Osmond J. D’cruz and Alexei O. Vassilev and Faith M Uckun},
  journal={Fertility and sterility},
  year={2001},
  volume={76 2},
  pages={
          258-66
        }
}
Mediators of the JAK/STAT Signaling Pathway in Human Spermatozoa1
TLDR
The presence of STAT proteins in sperm structural components suggests that their role is different from their well-known transcription factor activity in somatic cells, but further investigations are required to determine their role in sperm function.
Progesterone activates Janus Kinase 1/2 and activators of transcription 1 (JAK1‐2/STAT1) pathway in human spermatozoa
TLDR
It is concluded that in human spermatozoa, the JAK1/2 pathway is activated upon capacitation and is further modulated by progesterone; the biological processes controlled by this pathway in sperm need to be elucidated.
Stattic V, a STAT3 inhibitor, affects human spermatozoa through regulation of mitochondrial activity
TLDR
The results suggest that STAT3 is involved in sperm functions, at least through regulation of mitochondrial activity, and further emphasizes thatSTAT3 mediates cellular activities in a manner different than strictly the activation of gene transcription.
In spermatozoa, Stat1 is activated during capacitation and the acrosomal reaction.
TLDR
The results show tight spatio-temporal rearrangements of Stat1, suggesting that after fertilization Stat1 participates in the first rounds of transcription within the male pronucleus.
Les intermédiaires de la voie JAK/STAT dans les spermatozoïdes humains
TLDR
This last study suggests that a common signaling pathway activate the cAMP-dependent protein kinase and leads to the identification of a new potential substrate of the enzyme in spermatozoa, the triosephosphate isomerase.
Sperm lipid peroxidation and pro‐inflammatory cytokines
TLDR
Several pro-inflammatory cytokines at physiological concentrations increase the level of lipid peroxidation of sperm membranes, which could be important for the sperm fecundation process, However, infection-inflammation concentrations of some cytokines, such as IL-8 and TNF-α, either alone or in the presence of leukocytes, could drive the lipid per oxidation of the spermatozoa plasma membrane to levels that can affect the sperm fertility capacity.
Induction of human sperm capacitation and protein tyrosine phosphorylation by endometrial cells and interleukin-6.
TLDR
It is shown that, as for endometrial cell-conditioned media, IL- 6 induces human sperm capacitation and the IL-6 intracellular signalling machinery is present in human spermatozoa and might be involved in the acquisition of sperm fertilizing ability.
IFN-gamma alters the human sperm membrane permeability to Ca2+
TLDR
In vitro, IFN-γ modifies Ca2+ sperm membrane permeability, probably via lipid peroxidation, and can affect [Ca2+]cyto regulation and alter sperm fertilizing capacity.
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TLDR
The importance of STAT activation to growth control in experiments using anti-sense molecules or dominant negative STAT protein encoding constructs performed in cell lines or studies in animals lacking specific STATs strongly indicate that STATs play an important role in controlling cell cycle progression and apoptosis.
Interleukin 12 induces tyrosine phosphorylation and activation of STAT4 in human lymphocytes.
TLDR
It is shown that IL-12 stimulates formation of a DNA-binding complex that recognizes a DNA sequence previously shown to bind STAT proteins and that this complex contains STAT4, and that STAT4 expression is regulated by T-cell activation.
IL-10 induces the tyrosine phosphorylation of tyk2 and Jak1 and the differential assembly of STAT1 alpha and STAT3 complexes in human T cells and monocytes.
TLDR
It is shown that in monocytes and T cells IL-10 stimulates tyrosine phosphorylation of the signal transducers and activators of transcription, STAT1 alpha and STAT3, in a differential manner such that the relative formation of homo- and heterodimers varies between the two cell types.
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TLDR
It is shown that IL- 12 and IL-2 induce tyrosine phosphorylation of distinct members of the Janus (JAK) family of protein tyrosin kinases in human T lymphocytes.
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TLDR
Comparison with the deduced protein sequence of the two previously described genes (Stat91 and Stat113), discovered because of their activation as transcription factors after interferon-induced tyrosine phosphorylation, shows several highly conserved regions, including the putative SH3 and SH2 domains.
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TLDR
The abundant expression ofIL-1alpha, IL-1beta, the IL-2RtI, and its antagonist IL- 1RA by human cumulus cells provides further evidence that the IL/1 system plays a role in human ovarian physiology.
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TLDR
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Direct binding to and tyrosine phosphorylation of the alpha subunit of the type I interferon receptor by p135tyk2 tyrosine kinase
TLDR
The hypothesis that the Tyk2 protein functions as part of a receptor complex to initiate intracellular signaling in response to type I IFNs is supported.
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