scholarly journals The human carbonic anhydrase I gene has two promoters with different tissue specificities

1991 ◽  
Vol 277 (3) ◽  
pp. 903-905 ◽  
Author(s):  
H J M Brady ◽  
N Lowe ◽  
J C Sowden ◽  
M Edwards ◽  
P H W Butterworth
Keyword(s):  
Carbonic Anhydrase ◽  
Sequence Similarity ◽  
Transcription Start ◽  
S1 Nuclease ◽  
Transcription Start Sites ◽  
Similar Region ◽  
Carbonic Anhydrase I ◽  
Mrna Transcripts ◽  
Human Carbonic Anhydrase ◽  
Strong Sequence Similarity

Primer extension and S1 nuclease analysis of human carbonic anhydrase I (HCA1) mRNA transcripts in erythroid and non-erythroid tissues show that the HCA1 gene has two promoters with different tissue specificities, separated by 36 kb of DNA. The promoter of the HCA1 gene which is active in non-erythroid tissue shows strong sequence similarity with a similar region in the mouse CA1 gene, but has two equally used transcription start sites.

scholarly journals Synthesis and Human Carbonic Anhydrase I, II, IX, and XII Inhibition Studies of Sulphonamides Incorporating Mono-, Bi- and Tricyclic Imide Moieties

2021 ◽  
Vol 14 (7) ◽  
pp. 693
Author(s):  
Kalyan K. Sethi ◽  
KM Abha Mishra ◽  
Saurabh M. Verma ◽  
Daniela Vullo ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Carbonic Anhydrase ◽  
Docking Studies ◽  
Carbonic Anhydrases ◽  
Molecular Docking Studies ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Inhibition Studies

New derivatives were synthesised by reaction of amino-containing aromatic sulphonamides with mono-, bi-, and tricyclic anhydrides. These sulphonamides were investigated as human carbonic anhydrases (hCAs, EC 4.2.1.1) I, II, IX, and XII inhibitors. hCA I was inhibited with inhibition constants (Kis) ranging from 49 to >10,000 nM. The physiologically dominant hCA II was significantly inhibited by most of the sulphonamide with the Kis ranging between 2.4 and 4515 nM. hCA IX and hCA XII were inhibited by these sulphonamides in the range of 9.7 to 7766 nM and 14 to 316 nM, respectively. The structure–activity relationships (SAR) are rationalised with the help of molecular docking studies.

Crystal analysis of aromatic sulfonamide binding to native and (Zn)2 adduct of human carbonic anhydrase I Michigan 1

2002 ◽  
Vol 339 ◽  
pp. 135-144 ◽  
Author(s):  
Marta Ferraroni ◽  
Fabrizio Briganti ◽  
W.Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
Andrea Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
Aromatic Sulfonamide

A simple enzyme-linked immunoassay of human carbonic anhydrase I for the study of developing erythroid cells

1990 ◽  
Vol 191 (3) ◽  
pp. 169-174 ◽  
Author(s):  
Takahito Kondo ◽  
Kazuhiro Murakami ◽  
Hiroshi Isobe ◽  
Naoyuki Taniguchi ◽  
Yoshikazu Kawakami
Keyword(s):  
Carbonic Anhydrase ◽  
Erythroid Cells ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

scholarly journals New Histamine-Related Five-Membered N-Heterocycle Derivatives as Carbonic Anhydrase I Activators

Molecules ◽  
2022 ◽  
Vol 27 (2) ◽  
pp. 545
Author(s):  
Niccolò Chiaramonte ◽  
Alessio Gabellini ◽  
Andrea Angeli ◽  
Gianluca Bartolucci ◽  
Laura Braconi ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Imidazole Ring ◽  
Aliphatic Chain ◽  
Amino Group ◽  
Carbonic Anhydrase I ◽  
Terminal Amino ◽  
Human Carbonic Anhydrase ◽  
New Compounds ◽  
Related Compounds ◽  
Micromolar Range

A series of histamine (HST)-related compounds were synthesized and tested for their activating properties on five physiologically relevant human Carbonic Anhydrase (hCA) isoforms (I, II, Va, VII and XIII). The imidazole ring of HST was replaced with different 5-membered heterocycles and the length of the aliphatic chain was varied. For the most interesting compounds some modifications on the terminal amino group were also performed. The most sensitive isoform to activation was hCA I (KA values in the low micromolar range), but surprisingly none of the new compounds displayed activity on hCA II. Some derivatives (1, 3a and 22) displayed an interesting selectivity for activating hCA I over hCA II, Va, VII and XIII.

Structural organization of upstream exons and distribution of transcription start sites in the chicken c-myb gene

1989 ◽  
Vol 9 (2) ◽  
pp. 837-843
Author(s):  
S L Hahn ◽  
M Hahn ◽  
W S Hayward
Keyword(s):  
Binding Sites ◽  
Noncoding Region ◽  
Open Reading Frames ◽  
Transcription Start ◽  
S1 Nuclease ◽  
Transcription Start Sites ◽  
Conserved Sequence ◽  
Myb Gene ◽  
Putative Transcription Factor ◽  
Myb Genes

We mapped and sequenced three upstream exons of the chicken c-myb gene and the regions flanking the first coding exon. We found multiple potential binding sites for transcription factors in the 5'-noncoding region, a T-rich stretch of 78 base pairs (bp) (68% T) in the first intron, and four fairly long open reading frames in the antisense direction of the first coding exon and its flanking regions. Three major transcription start sites, contained within a single 11-bp region, were identified by S1 nuclease analysis and primer extension. A sequence comparison of the avian and murine c-myb genes revealed a highly conserved sequence of 124 bp in the 5'-noncoding region. Its location between the putative transcription factor binding sites and the major transcription start sites suggests that it may play an important regulatory role in c-myb expression.

scholarly journals (Hetero)aryl substituted thiazol-2,4-yl scaffold as human carbonic anhydrase I, II, VII and XIV activators

2019 ◽  
Vol 34 (1) ◽  
pp. 224-229 ◽  
Author(s):  
Marouan Rami ◽  
Jean-Yves Winum ◽  
Claudiu T. Supuran ◽  
Patricia Melnyk ◽  
Saïd Yous
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

scholarly journals Synthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid–sulphonamide conjugates

2020 ◽  
Vol 35 (1) ◽  
pp. 489-497 ◽  
Author(s):  
Hasan Küçükbay ◽  
Nesrin Buğday ◽  
F. Zehra Küçükbay ◽  
Andrea Ageli ◽  
Gianluca Bartolucci ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase
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