A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species
PADs are a group of calcium-dependent enzymes that play key roles in inflammatory pathologies and have diverse roles in cancers. PADs cause irreversible post-translational modification of arginine to citrulline, leading to changes in protein function in different cellular compartments. PAD isozyme d...
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI
2022
|
| Subjects: | |
| Online Access: | https://repository.londonmet.ac.uk/7848/1/ijms-23-08697-v2.pdf |
| _version_ | 1804072829071654912 |
|---|---|
| author | Inal, Jameel Hristova, Mariya Lange, Sigrun |
| author_facet | Inal, Jameel Hristova, Mariya Lange, Sigrun |
| author_sort | Inal, Jameel |
| collection | LMU |
| description | PADs are a group of calcium-dependent enzymes that play key roles in inflammatory pathologies and have diverse roles in cancers. PADs cause irreversible post-translational modification of arginine to citrulline, leading to changes in protein function in different cellular compartments. PAD isozyme diversity differs throughout phylogeny in chordates, with five PAD isozymes in mammals, three in birds, and one in fish. While the roles for PADs in various human cancers are mounting (both in regards to cancer progression and epigenetic regulation), investigations into animal cancers are scarce. The current pilot-study therefore aimed at assessing PAD isozymes in a range of animal cancers across the phylogeny tree. In addition, the tissue samples were assessed for total protein deimination and histone H3 deimination (CitH3), which is strongly associated with human cancers and also indicative of gene regulatory changes and neutrophil extracellular trap formation (NETosis). Cancers were selected from a range of vertebrate species: horse, cow, reindeer, sheep, pig, dog, cat, rabbit, mink, hamster, parrot, and duck. The cancers chosen included lymphoma, kidney, lung, testicular, neuroendocrine, anaplastic, papilloma, and granulosa cell tumour. Immunohistochemical analysis revealed that CitH3 was strongly detected in all of the cancers assessed, while pan-deimination detection was overall low. Both PAD2 and PAD3 were the most predominantly expressed PADs across all of the cancers assessed, while PAD1, PAD4, and PAD6 were overall expressed at lower, albeit varying, levels. The findings from this pilot study provide novel insights into PAD-mediated roles in different cancers across a range of vertebrate species and may aid in the understanding of cancer heterogeneity and cancer evolution. |
| first_indexed | 2024-07-09T04:05:21Z |
| format | Article |
| id | oai:repository.londonmet.ac.uk:7848 |
| institution | London Metropolitan University |
| language | English |
| last_indexed | 2024-07-09T04:05:21Z |
| publishDate | 2022 |
| publisher | MDPI |
| record_format | eprints |
| spelling | oai:repository.londonmet.ac.uk:78482022-08-12T14:19:16Z http://repository.londonmet.ac.uk/7848/ A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species Inal, Jameel Hristova, Mariya Lange, Sigrun 570 Life sciences; biology 590 Animals (Zoology) PADs are a group of calcium-dependent enzymes that play key roles in inflammatory pathologies and have diverse roles in cancers. PADs cause irreversible post-translational modification of arginine to citrulline, leading to changes in protein function in different cellular compartments. PAD isozyme diversity differs throughout phylogeny in chordates, with five PAD isozymes in mammals, three in birds, and one in fish. While the roles for PADs in various human cancers are mounting (both in regards to cancer progression and epigenetic regulation), investigations into animal cancers are scarce. The current pilot-study therefore aimed at assessing PAD isozymes in a range of animal cancers across the phylogeny tree. In addition, the tissue samples were assessed for total protein deimination and histone H3 deimination (CitH3), which is strongly associated with human cancers and also indicative of gene regulatory changes and neutrophil extracellular trap formation (NETosis). Cancers were selected from a range of vertebrate species: horse, cow, reindeer, sheep, pig, dog, cat, rabbit, mink, hamster, parrot, and duck. The cancers chosen included lymphoma, kidney, lung, testicular, neuroendocrine, anaplastic, papilloma, and granulosa cell tumour. Immunohistochemical analysis revealed that CitH3 was strongly detected in all of the cancers assessed, while pan-deimination detection was overall low. Both PAD2 and PAD3 were the most predominantly expressed PADs across all of the cancers assessed, while PAD1, PAD4, and PAD6 were overall expressed at lower, albeit varying, levels. The findings from this pilot study provide novel insights into PAD-mediated roles in different cancers across a range of vertebrate species and may aid in the understanding of cancer heterogeneity and cancer evolution. MDPI 2022-08-04 Article PeerReviewed text en cc_by_4 https://repository.londonmet.ac.uk/7848/1/ijms-23-08697-v2.pdf Inal, Jameel, Hristova, Mariya and Lange, Sigrun (2022) A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species. International Journal of Molecular Sciences, 23 (15). pp. 1-27. ISSN 1422-0067 https://doi.org/10.3390/ijms23158697 10.3390/ijms23158697 |
| spellingShingle | 570 Life sciences; biology 590 Animals (Zoology) Inal, Jameel Hristova, Mariya Lange, Sigrun A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title | A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title_full | A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title_fullStr | A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title_full_unstemmed | A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title_short | A pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| title_sort | pilot study on peptidylarginine deiminases and protein deimination in animal cancers across vertebrate species |
| topic | 570 Life sciences; biology 590 Animals (Zoology) |
| url | https://repository.londonmet.ac.uk/7848/1/ijms-23-08697-v2.pdf |
| work_keys_str_mv | AT inaljameel apilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies AT hristovamariya apilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies AT langesigrun apilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies AT inaljameel pilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies AT hristovamariya pilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies AT langesigrun pilotstudyonpeptidylargininedeiminasesandproteindeiminationinanimalcancersacrossvertebratespecies |