Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0268596 (EMA)
 2,520 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A recent report has demonstrated that the avidin-biotin-peroxidase (ABP) technique can successfully be used on previously stained histologic sections without the loss of sensitivity. In this study the tissues had been microwave fixed and only H & E stained sections were used. This procedure was tested on formalin-fixed tissues previously stained with H & E, PAS and van Gieson. Stained sections were prepared from selected blocks used as controls. One week after staining the sections were decolorized and together with the unstained control sections were restained with the ABP technique using IgA, IgD, IgE, IgM, kappa and lambda light chains, S100, EMA, LCA, amylase and PCK antisera. Demonstration of the tissue antigens was best with the previously stained H & E slides with little or no loss in sensitivity. Variable results were obtained with the PAS and van Gieson slides, the loss of sensitivity varying from none to complete.
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PMID:Use of the avidin-biotin-peroxidase immunostaining technique on previously stained histologic sections. 247 13

We previously reported that the small GTPase Rab27 and its effectors regulate isoproterenol (IPR)-stimulated amylase release from rat parotid acinar cells. Although activation of Rab27 by a specific guanine nucleotide exchange factor (GEF) is thought to be required for amylase release, its activation mechanism is poorly understood, because GEF for Rab27 has not been reported in parotid acinar cells. In the present study, we investigated the possible involvement of MADD/DENN/Rab3GEP, which was recently described as a Rab27-GEF in melanocytes, in amylase release from rat parotid acinar cells. Reverse transcription-PCR analyses indicated that mRNA of DENND family members, including MADD, was expressed in parotid acinar cells. MADD protein was also expressed in the cytosolic fraction of parotid acinar cells. Incubation of an antibody against the C-terminal 150 amino acids of MADD (anti-MADD-C antibody) with streptolysin O-permeabilized parotid acinar cells caused not only inhibition of IPR-induced amylase release but also reduction in the amount of GTP-Rab27. Our findings indicated that MADD functions as a GEF for Rab27 in parotid acinar cells and that its GEF activity for Rab27, i.e., GDP/GTP cycling, is required for IPR-induced amylase release.
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PMID:MADD/DENN/Rab3GEP functions as a guanine nucleotide exchange factor for Rab27 during granule exocytosis of rat parotid acinar cells. 2370 76