Disease relevance of Serpina3k

• On the other hand, the plasma levels of the F isoform, contrapsin, and alpha-macroglobulin showed moderate (1.5 to 2.3-fold) elevation during the acute-phase reaction [1].
• In mice bearing ascites tumors, such as Ehrlich, L1210, Meth-A, and P-815, the plasma levels of contrapsin and alpha-1-antiproteinase remained virtually unchanged [2].

High impact information on Serpina3k

• In contrast, the mRNAs for contrapsin (a plasma protease inhibitor) and the major urinary proteins (MUPs) are not detected in the visceral yolk sac at any stage of embryonic development [3].
• We also found that the contrapsin and the alpha 1-PI multigene families have acquired very different regulatory responses since the time of the gene duplication event [4].
• The two major protease inhibitors in mouse plasma are alpha 1-protease inhibitor (alpha 1-PI), putative inhibitor of neutrophil elastase, and contrapsin, an inhibitor in vitro of trypsinlike proteases [4].
• The nucleotide and deduced amino acid sequences of lambda Spi-1 and lambda Spi-2 which align with the reactive centers of known members of this family differ substantially from each other and from other members of the family [5].
• In order to study the molecular actions of growth hormone on gene expression, we have cloned and characterized two unique, but related, cDNA sequences from rat liver, lambda Spi-1 and lambda Spi-2 [5].

Chemical compound and disease context of Serpina3k

• On the other hand, induction of acute phase reaction by injection of bacterial lipopolysaccharide caused differential effects on the two proteinase inhibitors: hepatic translatable mRNA for contrapsin was doubled while that for alpha-1-antiproteinase remained unchanged [2].

Biological context of Serpina3k

• Here, we show that the contrapsin and alpha 1-PI genes are members of two different multigene families, each containing at least three genes in mice and rats [4].
• A cDNA clone (lambda MC-2) for contrapsin, a serine-proteinase inhibitor, was isolated from a lambda ZAP mouse liver cDNA library [6].
• The N-terminal amino acid sequence of the isolated contrapsin matched residues 30 to 48 of the sequence deduced on nucleotide analysis [7].
• M13 vector sequence analysis revealed that contrapsin cDNA contained an open reading frame of 1,254 bases encoding 418 amino acids [7].
• We have studied the effects of murine alpha-1-antitrypsin and contrapsin, a new trypsin inhibitor (Takahara, H. and Sinohara, H. (1982) J. Biol. Chem. 257, in press), on several serine proteases participating in blood clotting, fibrinolysis, kinin generation, and complement activation [8].

Anatomical context of Serpina3k

• Thus, epitopes characterizing native trypsin were presumably either masked following complex formation with contrapsin, or their processing and presentation to antigen presenting cells was suppressed, so that an antibody response was not mounted against them [9].
• Northern blot analysis of RNA extracted from primary cultures of mouse hepatocytes did not detect IL-1ra mRNA, although constitutive and stimulated contrapsin mRNA expression were easily demonstrated [10].

Associations of Serpina3k with chemical compounds

• Inhibitory spectrum of mouse contrapsin and alpha-1-antitrypsin against mouse serine proteases [11].
• A glycoprotein with Mr 63,000 purified from rat serum was found to inhibit trypsin activity but not chymotrypsin or elastase activity, resembling contrapsin purified from mouse serum [12].
• Treatment of adult worms with deoxycholate resulted in a change in the electrophoretic behaviour of worm-derived contrapsin [9].
• After extraction of these parasites with Triton X-114, contrapsin was found in the aqueous phase of the detergent, suggesting it is unlikely to be an integral membrane protein [9].
• Estradiol administration to intact females caused a marked elevation in contrapsin level but a decrease in alpha 1-antiprotease level [13].

Regulatory relationships of Serpina3k

• The latter two were up-regulated, whereas contrapsin was down-regulated in neonatal MT-null mice [14].

Other interactions of Serpina3k

• The primary structure of each of the three proteins has about 70% homology with that of mouse contrapsin, in contrast to 43-46% homology with that of rat alpha 1-protease inhibitor [12].
• Contrapsin inactivated trypsin, but did not significantly affect chymotrypsin, pancreatic elastase, or pancreatic kallikrein [1].
• Seventy-seven spots/spot chains from the reducing gels were identified by HPLC MS/MS, representing 28 distinct proteins, including a species-specific protease inhibitor, contrapsin, and high levels of carboxylesterase [15].
• Five secreted proteins including three protease inhibitors (fetuin-A, alpha-1 antitrypsin 1-6, and contrapsin) were identified from tumor masses at the regressive stage [16].

Analytical, diagnostic and therapeutic context of Serpina3k

• Molecular cloning and sequence analysis of cDNAs coding for guinea pig alpha 1-antiproteinases S and F and contrapsin [17].
• Contrapsin, a serine protease inhibitor (serpin) present in mouse serum, was compared with that found in adult Schistosoma mansoni worm homogenates, which although immunologically identical to contrapsin in mouse serum, had a higher molecular weight in Western blotting [9].
• The S isoform of alpha-1-antiproteinase was present in barely detectable amounts in healthy animals, but increased markedly when the acute-phase reaction was induced by subcutaneous injection of turpentine [1].
• Conformational differences between mouse contrapsin and alpha-1-antitrypsin as studied by ultraviolet absorption and circular dichroism spectroscopy [18].

References