V kazuistice popisujeme neobvyklý případ rezistence na krku, jehož příčinou bylo zakrvácení do adenomu příštítného tělíska. 72letá pacientka byla vyšetřena pro rezistenci na krku, v diferenciální diagnostice bylo uvažováno o nádoru štítné žlázy. Zároveň byla u pacientky biochemicky diagnostikována primární hyperparatyreóza. Při operaci byl z krční incize odstraněn tuhý uzel odpovídající hemoragicky změněnému adenomu příštítného tělíska. Ačkoliv příčinou tuhé rezistence na krku je zřídka adenom příštítného tělíska, měl by na ni endokrinolog či chirurg pomýšlet.
The case report describes an unusual case of the resistance of the neck caused by bleeding into the parathyroid adenoma. A 72-year-old female patient was examined for resistance of the neck, differential diagnosis was a thyroid tumor. At the same time, primary hyperparathyroidism was confirmed by the patient. During surgery, a rigid node corresponding to the haemorrhagically altered parathyroid adenoma was removed from the cervical incision. Although the cause of the resistance of the neck is rarely the parathyroid adenoma, the endocrinologist or surgeon should think of it.
- MeSH
- adenom chirurgie diagnóza komplikace MeSH
- hyperkalcemie etiologie MeSH
- krvácení etiologie MeSH
- lidé MeSH
- nádory příštítného tělíska * chirurgie diagnóza komplikace MeSH
- primární hyperparatyreóza diagnóza komplikace MeSH
- senioři MeSH
- výsledek terapie MeSH
- Check Tag
- lidé MeSH
- senioři MeSH
- ženské pohlaví MeSH
- Publikační typ
- kazuistiky MeSH
The molecular mechanisms controlling microtubule formation in cells with non-centrosomal microtubular arrays are not yet fully understood. The key component of microtubule nucleation is gamma-tubulin. Although previous results suggested that tyrosine kinases might serve as regulators of gamma-tubulin function, their exact roles remain enigmatic. In the present study, we show that a pool of gamma-tubulin associates with detergent-resistant membranes in differentiating P19 embryonal carcinoma cells, which exhibit elevated expression of the Src family kinase Fyn (protein tyrosine kinase p59(Fyn)). Microtubule-assembly assays demonstrated that membrane-associated gamma-tubulin complexes are capable of initiating the formation of microtubules. Pretreatment of the cells with Src family kinase inhibitors or wortmannin blocked the nucleation activity of the gamma-tubulin complexes. Immunoprecipitation experiments revealed that membrane-associated gamma-tubulin forms complexes with Fyn and PI3K (phosphoinositide 3-kinase). Furthermore, in vitro kinase assays showed that p85alpha (regulatory p85alpha subunit of PI3K) serves as a Fyn substrate. Direct interaction of gamma-tubulin with the C-terminal Src homology 2 domain of p85alpha was determined by pull-down experiments and immunoprecipitation experiments with cells expressing truncated forms of p85alpha. The combined results suggest that Fyn and PI3K might take part in the modulation of membrane-associated gamma-tubulin activities.
- MeSH
- buněčná membrána metabolismus MeSH
- buněčné linie MeSH
- fosfatidylinositol-3-kinasy genetika metabolismus MeSH
- lidé MeSH
- mikrotubuly metabolismus MeSH
- myši MeSH
- podjednotky proteinů genetika metabolismus MeSH
- protoonkogenní proteiny c-fyn genetika metabolismus MeSH
- rekombinantní fúzní proteiny genetika metabolismus MeSH
- tubulin genetika metabolismus MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- práce podpořená grantem MeSH
Aggregation of the high-affinity IgE receptors (FcepsilonRIs) on the surface of granulated mast cells initiates a chain of signaling events culminating in the release of allergy mediators. Although microtubules are involved in mast cell degranulation, the molecular mechanism that controls microtubule rearrangement after FcepsilonRI triggering is poorly understood. In this study, we show that the activation of bone marrow-derived mast cells (BMMCs) induced by FcepsilonRI aggregation or treatment with pervanadate leads to a rapid polymerization of microtubules. This polymerization was not dependent on the presence of Lyn kinase as determined by experiments with BMMCs isolated from Lyn-negative mice. One of the key regulators of microtubule polymerization is gamma-tubulin. Immunoprecipitation experiments revealed that gamma-tubulin from activated cells formed complexes with Fyn and Syk protein tyrosine kinases and several tyrosine phosphorylated proteins from both wild-type and Lyn(-/-) BMMCs. Pretreatment of the cells with Src-family or Syk-family selective tyrosine kinase inhibitors, PP2 or piceatannol, respectively, inhibited the formation of microtubules and reduced the amount of tyrosine phosphorylated proteins in gamma-tubulin complexes, suggesting that Src and Syk family kinases are involved in the initial stages of microtubule formation. This notion was corroborated by pull-down experiments in which gamma-tubulin complex bounds to the recombinant Src homology 2 and Src homology 3 domains of Fyn kinase. We propose that Fyn and Syk kinases are involved in the regulation of binding properties of gamma-tubulin and/or its associated proteins, and thus modulate the microtubule nucleation in activated mast cells.
- MeSH
- buňky kostní dřeně enzymologie metabolismus MeSH
- dimerizace MeSH
- fosforylace MeSH
- intracelulární signální peptidy a proteiny fyziologie MeSH
- kultivované buňky MeSH
- mastocyty enzymologie metabolismus MeSH
- mikrotubuly enzymologie metabolismus MeSH
- myši MeSH
- nádorové buněčné linie MeSH
- protoonkogenní proteiny c-fyn fyziologie chemie metabolismus MeSH
- skupina kinas odvozených od src-genu genetika nedostatek MeSH
- substrátová specifita MeSH
- terciární struktura proteinů MeSH
- tubulin fyziologie chemie metabolismus MeSH
- tyrosin metabolismus MeSH
- tyrosinkinasy fyziologie metabolismus MeSH
- zvířata MeSH
- Check Tag
- myši MeSH
- zvířata MeSH