Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.25.1 (
deoxyribonuclease
)
1,471
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Intracellular localization of
thyroglobulin
(TG) using a pre-embedding diffusion technique and an indirect localization sequence has been made in human thyroid obtained from 20 patients with treated Grave's disease. Both antibodies, anti-human TG-rabbit IgG F(ab')2 and anti-rabbit IgG F(ab')2-goat IgG F(ab')2 fragments easily penetrated the cytoplasm of follicular cells which were dissociated by RPMI-1640 solution containing collagenase, dispase, and
deoxyribonuclease
. With light microscopic observation of semithin sections positive immuno-reaction for TG was demonstrated as fine granular deposits in the cytoplasm of the dissociated cells. In electron microscopic studies, intracellular antigen was well circumscribed within certain cell organelles in all cases with the positive immuno-reaction for TG being observed in perinuclear space, rough endoplasmic reticulum, Golgi complexes, secretory granules, and reabsorbed colloid droplets. Content of positive immuno-reaction product differed somewhat from one case to another and from one follicle to another even in the same case. There was no immunoreaction product in nuclei, mitochondria, lysosomes, and lipofuscin-like granules.
...
PMID:An immuno-electron microscopic study on intracellular localization of thyroglobulin (TG) in the thyroid gland in Grave's disease. 389 13
A thyroid transcription factor-1 (TTF-1)-binding element in the rat TSH receptor (TSHR) promoter, between -189 and -175 basepairs (bp), is important for both thyroid-specific expression and thyroid-specific TSH/cAMP autoregulation of the TSHR. The identification of an up-stream TTF-1-binding site and its relationship to the function of the down-stream TTF-1 element are the subjects of this report. Sequence analysis identifies a potential TTF-1 site at -878 bp;
deoxyribonuclease
-I footprinting shows that the -881 to -866 bp region is protected by recombinant TTF-1 protein and by nuclear extracts from FRTL-5 thyroid cells that contain TTF-1, but not by extracts from nonfunctioning FRT thyroid or Buffalo rat liver (BRL) cells, which have no TTF-1, or by Pax-8. FRTL-5, but not FRT or BRL cell nuclear extracts, form a specific protein-DNA complex with this region in gel mobility shift analyses; its formation is prevented by TTF-1-binding elements from the
thyroglobulin
promoter. The upstream TTF-1 site acts as an enhancer when coupled to a heterologous simian virus-40 promoter-chloramphenicol acetyltransferase (CAT) chimera and transfected into FRTL-5 thyroid cells. There is a greater increase, 3-vs. 2-fold (P < 0.05), when TSHR promoter-CAT chimeras, which contain the up-stream TTF-1 element, pTRCAT5'-907 or pTRCAT5'-886, as opposed to those in which it is deleted, pTRCAT5'-907 delta USTTF-1, are transfected into FRTL-5 cells or cotransfected with a TTF-1 expression vector into BRL cells, which have no endogenous TTF-1. The TTF-1-dependent activity of pTRCAT5'-907 delta USTTF-1 is the same as that of the minimal promoter, -220 to -39 bp, containing only the down-stream TTF-1 site in both cells. Transfection of chimeric TSHR-CAT plasmids with the down- and/or up-stream TTF-1 site deleted reveals that the down-stream TTF-1 element functions in the absence of the up-stream element, but function of the up-stream site requires the down-stream TTF-1 element. Like the down-stream TSHR TTF-1-binding site, the up-stream TTF-1 site is different from TTF-1 sites in the
thyroglobulin
and thyroid peroxidase promoter, in that it does not interact with Pax-8.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Characterization of an up-stream thyroid transcription factor-1-binding site in the thyrotropin receptor promoter. 782 40