Human Cystatin A Is Inactivated by Engineered Truncation. The NH2-Terminal Region of the Cysteine Proteinase Inhibitor Is Essential for Expression of Its Inhibitory Activity

Biochemistry ◽  
1995 ◽  
Vol 34 (38) ◽  
pp. 12185-12192 ◽  
Author(s):  
Kazunori Shibuya ◽  
Hiroyuki Kaji ◽  
Takehito Itoh ◽  
Yukihito Ohyama ◽  
Akiyoshi Tsujikami ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Terminal Region ◽  
Cysteine Proteinase Inhibitor ◽  
Cystatin A ◽  
Human Cystatin

scholarly journals Structure and expression of the human cystatin C gene

1990 ◽  
Vol 268 (2) ◽  
pp. 287-294 ◽  
Author(s):  
M Abrahamson ◽  
I Olafsson ◽  
A Palsdottir ◽  
M Ulvsbäck ◽  
Å Lundwall ◽  
...  
Keyword(s):  
Cystatin C ◽  
Proteinase Inhibitor ◽  
Genomic Dna ◽  
Cysteine Proteinase ◽  
Housekeeping Genes ◽  
Genomic Region ◽  
Cysteine Proteinase Inhibitor ◽  
Specific Expression ◽  
Human Cystatin C ◽  
Human Cystatin

The structural organization of the gene for the human cysteine-proteinase inhibitor cystatin C was studied. Restriction-endonuclease digests of human genomic DNA hybridized with human cystatin C cDNA and genomic probes produced patterns consistent with a single cystatin C gene and, also, the presence of six closely related sequences in the human genome. A 30 kb restriction map covering the genomic region of the cystatin C gene was constructed. The positions of three polymorphic restriction sites, found at examination of digests of genomic DNA from 79 subjects, were localized in the flanking regions of the gene. The gene was cloned and the nucleotide sequence of a 7.3 kb genomic segment was determined, containing the three exons of the cystatin C structural gene as well as 1.0 kb of 5′-flanking and 2.0 kb of 3′-flanking sequences. Northern-blot experiments revealed that the cystatin C gene is expressed in every human tissue examined, including kidney, liver, pancreas, intestine, stomach, antrum, lung and placenta. The highest cystatin C expression was seen in seminal vesicles. The apparently non-tissue-specific expression of this cysteine-proteinase inhibitor gene is discussed with respect to the structure of its 5′-flanking region, which shares several features with those of housekeeping genes.

Identification of acid cysteine proteinase inhibitor (cystatin A) in the human thymus

1994 ◽  
Vol 240 (1) ◽  
pp. 115-119 ◽  
Author(s):  
Karl-Ove Söderström ◽  
Ritta Rinne ◽  
Väinö K. Hopsu-Havu ◽  
Mikko Järvinen ◽  
Ari Rinne
Keyword(s):  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor ◽  
Human Thymus ◽  
Cystatin A
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