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Alpha-1-antitrypsin: a novel human high temperature requirement protease A1 (HTRA1) substrate in human placental tissue

Frochaux, Violette ; Hildebrand, Diana ; Talke, Anja ; Linscheid, Michael W ; Schlüter, Hartmut Isalan, Mark

PloS one, 2014-10, Vol.9 (10), p.e109483-e109483 [Periódico revisado por pares]

United States: Public Library of Science

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Título:
Alpha-1-antitrypsin: a novel human high temperature requirement protease A1 (HTRA1) substrate in human placental tissue
Autor: Frochaux, Violette ; Hildebrand, Diana ; Talke, Anja ; Linscheid, Michael W ; Schlüter, Hartmut
Isalan, Mark
Assuntos: Actin ; alpha 1-Antitrypsin - chemistry ; alpha 1-Antitrypsin - metabolism ; Amino Acid Sequence ; Amino acids ; Animals ; Apoptosis ; Arthritis ; Biochemistry ; Biology and Life Sciences ; Blood plasma ; E coli ; Female ; Gestation ; High temperature ; High-Temperature Requirement A Serine Peptidase 1 ; Humans ; Mass Spectrometry ; Mass spectroscopy ; Molecular Sequence Data ; Muscle proteins ; Ovarian cancer ; Peptides ; Placenta ; Placenta - cytology ; Placenta - metabolism ; Pregnancy ; Protease ; Protease inhibitors ; Proteases ; Protein Binding ; Proteinase inhibitors ; Proteins ; Proteolysis ; Serine ; Serine Endopeptidases - metabolism ; Serine proteinase ; Serine Proteinase Inhibitors - pharmacology ; Spectroscopy ; Substrates ; Synthetic peptides ; Temperature requirements ; Tropomyosin
É parte de: PloS one, 2014-10, Vol.9 (10), p.e109483-e109483
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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Competing Interests: The affiliation to the company ProteaImmun does not alter the authors’ adherence to all the PLOS ONE policies on sharing data and materials. There were no competing interests (no employment, no consultancy, no patents, no products in development and no marketed products).
Conceived and designed the experiments: HS MWL VF. Performed the experiments: VF AT DH. Analyzed the data: VF. Contributed reagents/materials/analysis tools: HS MWL AT. Wrote the paper: VF HS.
Descrição: The human serine protease high temperature requirement A1 (HTRA1) is highly expressed in the placental tissue, especially in the last trimester of gestation. This suggests that HTRA1 is involved in placental formation and function. With the aim of a better understanding of the role of HTRA1 in the placenta, candidate substrates were screened in a placenta protein extract using a gel-based mass spectrometric approach. Protease inhibitor alpha-1-antitrypsin, actin cytoplasmic 1, tropomyosin beta chain and ten further proteins were identified as candidate substrates of HTRA1. Among the identified candidate substrates, alpha-1-antitrypsin (A1AT) was considered to be of particular interest because of its important role as protease inhibitor. For investigation of alpha-1-antitrypsin as substrate of HTRA1 synthetic peptides covering parts of the sequence of alpha-1-antitrypsin were incubated with HTRA1. By mass spectrometry a specific cleavage site was identified after met-382 (AIPM382↓383SIPP) within the reactive centre loop of alpha-1-antitrypsin, resulting in a C-terminal peptide comprising 36 amino acids. Proteolytic removal of this peptide from alpha-1-antitrypsin results in a loss of its inhibitor function. Beside placental alpha-1-antitrypsin the circulating form in human plasma was also significantly degraded by HTRA1. Taken together, our data suggest a link between the candidate substrates alpha-1-antitrypsin and the function of HTRA1 in the placenta in the syncytiotrophoblast, the cell layer attending to maternal blood in the villous tree of the human placenta. Data deposition: Mass spectrometry (MS) data have been deposited to the ProteomeXchange with identifier PXD000473.
Editor: United States: Public Library of Science
Idioma: Inglês

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Alpha-1-antitrypsin: a novel human high temperature requirement protease A1 (HTRA1) substrate in human placental tissue

Frochaux, Violette ; Hildebrand, Diana ; Talke, Anja ; Linscheid, Michael W ; Schlüter, Hartmut Isalan, Mark

United States: Public Library of Science

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