A new multigene HCIQ subfamily from the sea anemone Heteractis crispa encodes Kunitz-peptides exhibiting neuroprotective activity against 6-hydroxydopamine

The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multi...

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Published inScientific reports Vol. 10; no. 1; p. 4205
Main Authors Kvetkina, Aleksandra, Leychenko, Elena, Chausova, Victoria, Zelepuga, Elena, Chernysheva, Nadezhda, Guzev, Konstantin, Pislyagin, Evgeny, Yurchenko, Ekaterina, Menchinskaya, Ekaterina, Aminin, Dmitry, Kaluzhskiy, Leonid, Ivanov, Alexis, Peigneur, Steve, Tytgat, Jan, Kozlovskaya, Emma, Isaeva, Marina
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 06.03.2020
Nature Publishing Group
Subjects
6-Hydroxydopamine
631/45
631/45/611
Amino Acid Sequence
Animals
Cell Survival - genetics
Cell Survival - physiology
Cell viability
Endopeptidases
Exons - genetics
Female
Heteractis crispa
Humanities and Social Sciences
Inflammation
Introns
Isoforms
multidisciplinary
Neuroblastoma
Neuroprotection
Neurotoxicity
Peptides
Peptides - chemistry
Peptides - genetics
Peptides - metabolism
Phylogeny
Protein Binding - genetics
Protein Binding - physiology
Protein Isoforms - genetics
Protein Isoforms - metabolism
Science
Science (multidisciplinary)
Sea Anemones - genetics
Sea Anemones - metabolism
Serine
Serine Proteases - genetics
Serine Proteases - metabolism
Thermodynamics
Trypsin
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Abstract The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with K i 5.2 × 10 −8  M and K i 1.9 × 10 −7  M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.
AbstractList The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with K i 5.2 × 10 −8  M and K i 1.9 × 10 −7  M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.
The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with Ki 5.2 × 10−8 M and Ki 1.9 × 10−7 M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.
The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with Ki 5.2 × 10-8 M and Ki 1.9 × 10-7 M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with Ki 5.2 × 10-8 M and Ki 1.9 × 10-7 M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.
The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities and therefore they are the subject of a number of investigations. We have discovered a new HCIQ subfamily belonging to recently described multigene HCGS family of Heteractis crispa Kunitz-peptides. The uniqueness of this subfamily is that the HCIQ precursors contain a propeptide terminating in Lys-Arg (endopeptidase cleavage site) the same as in the neuro- and cytotoxin ones. Moreover, the HCIQ genes contain two introns in contrast to HCGS genes with one intron. As a result of Sanger and amplicon deep sequencings, 24 HCIQ isoforms were revealed. The recombinant peptides for the most prevalent isoform (HCIQ2c1) and for the isoform with the rare substitution Gly17Glu (HCIQ4c7) were obtained. They can inhibit trypsin with K 5.2 × 10  M and K 1.9 × 10  M, respectively, and interact with some serine proteinases including inflammatory ones according to the SPR method. For the first time, Kunitz-peptides have shown to significantly increase neuroblastoma cell viability in an in vitro 6-OHDA-induced neurotoxicity model being a consequence of an effective decrease of ROS level in the cells.
ArticleNumber 4205
Author Guzev, Konstantin
Yurchenko, Ekaterina
Chausova, Victoria
Chernysheva, Nadezhda
Leychenko, Elena
Peigneur, Steve
Isaeva, Marina
Kozlovskaya, Emma
Menchinskaya, Ekaterina
Zelepuga, Elena
Pislyagin, Evgeny
Kvetkina, Aleksandra
Aminin, Dmitry
Kaluzhskiy, Leonid
Tytgat, Jan
Ivanov, Alexis
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/32144281$$D View this record in MEDLINE/PubMed
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PublicationTitle Scientific reports
PublicationTitleAbbrev Sci Rep
PublicationTitleAlternate Sci Rep
PublicationYear 2020
Publisher Nature Publishing Group UK
Nature Publishing Group
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
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Snippet The Kunitz/BPTI-type peptides are ubiquitous in numerous organisms including marine venomous animals. The peptides demonstrate various biological activities...
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StartPage 4205
SubjectTerms 6-Hydroxydopamine
631/45
631/45/611
Amino Acid Sequence
Animals
Cell Survival - genetics
Cell Survival - physiology
Cell viability
Endopeptidases
Exons - genetics
Female
Heteractis crispa
Humanities and Social Sciences
Inflammation
Introns
Isoforms
multidisciplinary
Neuroblastoma
Neuroprotection
Neurotoxicity
Peptides
Peptides - chemistry
Peptides - genetics
Peptides - metabolism
Phylogeny
Protein Binding - genetics
Protein Binding - physiology
Protein Isoforms - genetics
Protein Isoforms - metabolism
Science
Science (multidisciplinary)
Sea Anemones - genetics
Sea Anemones - metabolism
Serine
Serine Proteases - genetics
Serine Proteases - metabolism
Thermodynamics
Trypsin
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Title A new multigene HCIQ subfamily from the sea anemone Heteractis crispa encodes Kunitz-peptides exhibiting neuroprotective activity against 6-hydroxydopamine
URI https://link.springer.com/article/10.1038/s41598-020-61034-x
https://www.ncbi.nlm.nih.gov/pubmed/32144281
https://www.proquest.com/docview/2372861362
https://www.proquest.com/docview/2374352158
https://pubmed.ncbi.nlm.nih.gov/PMC7060258
Volume 10
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