Isolation, characterization, and cDNA sequencing of α-1-antiproteinase-like protein from rainbow trout seminal plasma

Mak, Monika; Mak, Paweł; Olczak, Mariusz; Szalewicz, Agata; Dubin, Adam; Watorek, W; Ciereszko, Andrzej

doi:10.1016/j.bbagen.2004.02.001

Cited by 26 publications

(29 citation statements)

References 43 publications

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“…The sequence of the rainbow trout a 1 -PI reactive loop was estimated along the whole 38-amino-acid chain. It is identical to the sequence of trout seminal plasma serpin described by other authors (Mak et al 2004). The whole primary structure of the reactive loop has approximate 70% homology with a 1 -PIs found in other species.…”

Section: Serpinmentioning

confidence: 65%

“…Presumably, the major physiological role of fish serpins is to prevent self-destructive activity of proteinases. Mak et al 2004 …”

Section: Serpinmentioning

confidence: 97%

“…Bovine α 1 -PI [e] AIPM SLPPDVEFNRPFLCILYDRNTKSPLFVGKVVNPT a Mak et al 2004 b Huang et al 1995b c Bollen et al 1983;Carrell et al 1982d Brown et al 1989 e Sinha et al 1992 Proteinase inhibitors of the serpin group interact with proteinases as suicide substrates with a very high affinity, and proteinase usually cleaves at least one peptide bond in the inhibitor protein-the bait amino acid bond between P1 and P1 0 residues in the reactive loop. Stable covalent enzyme-inhibitor complexes are formed during that reaction and these complexes do not disintegrate even in the presence of SDS and high temperature.…”

Section: Aipm Slppdvefnrpflcilydrntksplfvgkvvnptmentioning

confidence: 99%

“…The occurrence of trypsin inhibitor in carp muscle was reported (Toyohara and Makinodan 1986). Glycoprotein forming stable complexes with proteinases was isolated also form rainbow trout seminal plasma (Mak et al 2004).…”

Section: Introductionmentioning

confidence: 97%

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Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Mickowska

2008

Fish Physiol Biochem

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The main serine proteinase inhibitors of rainbow trout (Oncorhynchuss mykiss) and common carp (Cyprinus carpio) blood plasma were isolated and purified. The investigated inhibitors, alpha(1)-proteinase inhibitor (alpha(1)-PI) and antithrombin III (AT III), act by forming stable complexes with target proteinases. The association rate constants k (on) for the interaction of fish plasma inhibitors with several serine proteinases have been determined: k (on) for both carp and rainbow trout alpha(1)-PI were >10(7) M(-1) s(-1) for human neutrophil elastase, and in the case of bovine trypsin and chymotrypsin k (on) values were 2.0-5.2 x 10(6) M(-1) s(-1). Association rate constants k (on) for the interaction of carp and rainbow trout AT III with bovine trypsin and thrombin were about 1.3 x 10(4)-7.9 x 10(5) M(-1) s(-1) without and >10(7) M(-1) s(-1) in presence of heparin; so antithrombins require the presence of heparin to become effective proteinase inhibitors. The high degree of homology of the estimated amino acid sequences of fish inhibitors reactive site loops confirms their similarity with other proteinase inhibitors from the serpin family.

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Section: Serpinmentioning

confidence: 65%

“…Presumably, the major physiological role of fish serpins is to prevent self-destructive activity of proteinases. Mak et al 2004 …”

Section: Serpinmentioning

confidence: 97%

Section: Aipm Slppdvefnrpflcilydrntksplfvgkvvnptmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

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Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Mickowska

2008

Fish Physiol Biochem

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“…Serine proteinase inhibitors have been found in some teleost fish such as carp and rainbow trout [19][20][21][22]. Serpins involved in G1 need to study for understanding the regulation of its proteolytic activity.…”

Section: Resultsmentioning

confidence: 99%

A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

et al. 2009

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Collagen degradation is known to be involved in post mortem tenderization of fish muscle. A serine proteinase which is assumed to be related to collagen degradation after fish death was purified from sarcoplasmic fraction of red sea bream Pagrus major by ammonium sulfate fractionation and column chromatographies on Sephacryl S-300, Q Sepharose and Phenyl Sepharose CL-4B. The enzyme hydrolyzed gelatin and was obtained as a protein band of approximately 38 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing condition. N-terminal amino acid sequence of the enzyme was determined for 32 residues. The protein having the same N-terminal amino acid sequence of the enzyme for 10 residues was purified from the serum of red sea bream and showed the same characteristics as the enzyme. Therefore, the serine proteinase was suggested to migrate from blood to muscle and to degrade muscle proteins after fish death.

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Proteomic identification of rainbow trout seminal plasma proteins

et al. 2013

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In the study, the combination of protein fractionation by 1DE and HPLC-ESI-MS/MS was used to characterize the rainbow trout seminal plasma proteome. Our results led to the creation of a catalogue of rainbow trout seminal plasma proteins (152 proteins) and significantly contributed to the current knowledge regarding the protein composition of fish seminal plasma. The major proteins of rainbow trout seminal plasma, such as transferrin, apolipoproteins, complement C3, serum albumin, and hemopexin-, alpha-1-antiproteinase-, and precerebellin-like protein, were recognized as acute-phase proteins (proteins that plasma concentration changes in response to inflammation). This study provides the basis for further functional studies of fish seminal plasma proteins, as well as for the identification of novel biomarkers for sperm quality. The MS data have been deposited in the ProteomeXchange with identifier PXD000306 (http://proteomecentral.proteomexchange.org/dataset/PXD000306).

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Isolation, characterization, and cDNA sequencing of α-1-antiproteinase-like protein from rainbow trout seminal plasma

Cited by 26 publications

References 43 publications

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

A serine proteinase from the sarcoplasmic fraction of red sea bream Pagrus major is possibly derived from blood

Proteomic identification of rainbow trout seminal plasma proteins

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