ArticleMaterials (Basel, Switzerland)2020
Proteomic Analysis of Porcine-Derived Collagen Membrane and Matrix.
Article in Materials (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- RNA-Seq of Gingival Fibroblasts Grown on Collagen Membranes and Hyaluronic Acid.Journal of functional biomaterials · 2026Article
- Tissue Sources Influence the Morphological and Morphometric Characteristics of Collagen Membranes for Guided Bone Regeneration.Polymers · 2024Article
- Proteomic Analysis of Human Serum Proteins Adsorbed onto Collagen Barrier Membranes.Journal of functional biomaterials · 2024Article
- White Isthmus Transcriptome Analysis Reveals the Mechanism of Translucent Eggshell Formation.Animals : an open access journal from MDPI · 2024Article
- Molecular insights into the proteomic composition of porcine treated dentin matrix.Materials today. Bio · 2024Article
- Physical, mechanical, and biological properties of collagen membranes for guided bone regeneration: a comparative in vitro study.BMC oral health · 2023Article
- A multifactorial analysis of FAP to regulate gastrointestinal cancers progression.Frontiers in immunology · 2023Article
- The use of periodontal membranes in the field of periodontology: spotlight on collagen membranes.Journal of applied biomedicine · 2022Review
- Adipose-derived stromal/stem cells are verified to be potential seed candidates for bio-root regeneration in three-dimensional culture.Stem cell research & therapy · 2022Article
- Osteoconductive Properties of a Volume-Stable Collagen Matrix in Rat Calvaria Defects: A Pilot Study.Biomedicines · 2021Article
- TGF-β Activity of a Demineralized Bone Matrix.International journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collagen membranes and matrices being widely used in guided bone regeneration and soft tissue augmentation have characteristic properties based on their composition. The respective proteomic signatures have not been identified. Here, we performed a high-resolution shotgun proteomic analysis on two porcine collagen-based biomaterials designed for guided bone regeneration and soft tissue augmentation. Three lots each of a porcine-derived collagen membrane and a matrix derived from peritoneum and/or skin were digested and separated by nano-reverse-phase high-performance liquid chromatography. The peptides were subjected to mass spectrometric detection and analysis. A total of 37 proteins identified by two peptides were present in all collagen membranes and matrices, with 11 and 16 proteins being exclusively present in the membrane and matrix, respectively. The common extracellular matrix proteins include fibrillar collagens (COL1A1, COL1A2, COL2A1, COL3A1, COL5A1, COL5A2, COL5A3, COL11A2), non-fibrillar collagens (COL4A2, COL6A1, COL6A2, COL6A3, COL7A1, COL16A1, COL22A1), and leucine-rich repeat proteoglycans (DCN, LUM, BGN, PRELP, OGN). The structural proteins vimentin, actin-based microfilaments (ACTB), annexins (ANXA1, ANXA5), tubulins (TUBA1B, TUBB), and histones (H2A, H2B, H4) were also identified. Examples of membrane-only proteins are COL12A1 and COL14A1, and, of matrix only proteins, elastin (ELN). The proteomic signature thus revealed the similarities between but also some individual proteins of collagen membrane and matrix.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.