Abstract
The serine protease inhibitor, clade A, member 1 (SERPINA1) is the gene for a protein called alpha-1-antitrypsin (AAT), which is a member of the serine protease inhibitor (serpin) superfamily of proteins. By conformational change, serpins control several chemical reactions inhibiting the activity of proteases. AAT is the most abundant endogenous serpin in blood circulation and it is present in relatively high concentration in human milk as well as in bovine and porcine colostrum. Here we report for the first time the molecular characterization and sequence variability of the ovine SERPINA1 cDNA and gene. cDNAs from mammary gland and from milk were PCR amplified, and three different transcripts (1437, 1166 and 521bp) of the SERPINA1 gene were identified. We amplified and sequenced different regions of the gene (5’ UTR, from exon 2 to exon 5 and 3’ UTR), and we found that the exon-intron structure of the gene is similar to that of human and bovine. We detected a total of 97 SNPs in cDNAs and gene sequences from 10 sheep of three different breeds. In adult sheep tissues a SERPINA1 gene expression analysis indicated a differential expression of the three different transcripts. The finding reported in this paper will aid further studies on possible involvement of the SERPINA1 gene in different physiological states and its possible association with production traits.
Highlights
Serine protease inhibitor superfamily constitutes the largest class of serine/cysteine peptidase inhibitors, currently having >3000 members within Eukarya, Bacteria, Archea and certain viruses [1,2]
The regions important for protease inhibition are centered on β sheet A and a stretch of amino acids termed Reactive Center Loop (RCL)
Using the primer pair for full length ovine SERPINA1 cDNA (Table 1, cDNA FWD and cDNA REV) three different transcripts were obtained by PCR using RNA extracted from milk and mammary gland samples (Figure 1)
Summary
Serine protease inhibitor (serpin) superfamily constitutes the largest class of serine/cysteine peptidase inhibitors, currently having >3000 members within Eukarya, Bacteria, Archea and certain viruses [1,2]. These protease inhibitors are involved in many critical biological processes like blood coagulation, fibrinolysis, programmed cell death, development and inflammation [3]. The serpin fold is comprised of 3 β sheets (A, B,C) and 7-9 α helices. The regions important for protease inhibition are centered on β sheet A and a stretch of amino acids termed Reactive Center Loop (RCL). The RCL participates in the initial interaction with the target protease, which recognizes it as a substrate and cleaves between two residues termed P1 (N-terminal of the cleavage event) and P1’
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