Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
8.1
4.9
Journals
IJMS
Special Issues
Molecular Investigations into the Structure Functional Roles of Coagulation Factors/Proteins
ijms-logo
Submit to IJMS Review for IJMS Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Molecular Investigations into the Structure Functional Roles of Coagulation Factors/Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (30 April 2022) | Viewed by 5939

Special Issue Editor

Dr. Arijit Biswas

E-Mail Website1 Website2
Guest Editor
Institute of Experimental Hematology and Coagulation Proteins Transfusion Medicine, University Clinic of Bonn, 53127 Bonn, Germany
Interests: coagulation protein; factor XIII; factor VIII; thrombosis; bleeding
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Coagulation proteins are expressed from a variety of cell and tissue types. While many coagulation proteins are secreted through classical mechanisms, some use non-classical pathways of secretion. Decades of intensive research have enabled researchers to study the discrete molecular mechanisms and pathways underlying the expression of coagulation proteins, helping them to recreate the same in heterologous in vitro conditions resulting in the production of highly efficient recombinant proteins which can be administered in specific coagulopathies. In spite of a great deal of scientific literature existing on this topic, a large degree of information is still missing. Owing to the pharmaceutical and translational relevance of many of these coagulation proteins, such as coagulation Factor VIII, VWF, and Factor XIII, among many others, understanding the molecular etiology, cell-tissue type and spatial/temporal modes of regulation of these proteins is very important. The current Special Issue solicits articles describing the current state of the art in this particular field, i.e., the mechanisms and implications of cellular expression and secretion of coagulation proteins. Submissions can be in the form of reviews providing insights into the current knowledge and technical know-how as well as original research that addresses the key questions being asked in this area.

Prof. Dr. Arijit Biswas
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • coagulation proteins
  • post-translational modifications
  • secretion pathways
  • tissue/cell-specific expression
  • interaction pathways
  • regulatory mechanisms

Published Papers (2 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

17 pages, 3946 KiB  
Article
Exploring Diverse Coagulation Factor XIII Subunit Expression Datasets: A Bioinformatic Analysis
by Muhammad Ahmer Jamil, Sneha Singh, Osman El-Maarri, Johannes Oldenburg and Arijit Biswas
Int. J. Mol. Sci. 2022, 23(9), 4725; https://doi.org/10.3390/ijms23094725 - 25 Apr 2022
Cited by 6 | Viewed by 2306
Abstract
Coagulation factor XIII (FXIII) circulates in plasma as a pro-transglutaminase heterotetrameric complex (FXIIIA2B2), which upon activation by thrombin and calcium covalently crosslinks preformed fibrin polymers. The heterotetrameric complex is composed of a catalytic FXIIIA2 subunit and a protective/regulatory [...] Read more.
Coagulation factor XIII (FXIII) circulates in plasma as a pro-transglutaminase heterotetrameric complex (FXIIIA2B2), which upon activation by thrombin and calcium covalently crosslinks preformed fibrin polymers. The heterotetrameric complex is composed of a catalytic FXIIIA2 subunit and a protective/regulatory FXIII-B2 subunit coded by F13A1 and F13B genes, respectively. The catalytic FXIIIA2 subunit is encoded by the F13A1 gene, expressed primarily in cells of mesenchymal origin, whereas the FXIIIB subunit encoded by the F13B gene is expressed and secreted from hepatocytes. The plasma FXIIIA2 subunit, which earlier was believed to be secreted from cells of megakaryocytic lineage, is now understood to result primarily from resident macrophages. The regulation of the FXIII subunits at the genetic level is still poorly understood. The current study adopts a purely bioinformatic approach to analyze the temporal, time-specific expression array-data corresponding to both the subunits in specific cell lineages, with respect to the gene promoters. We analyze the differentially expressed genes correlated with F13A1 and F13B expression levels in an array of cell types, utilizing publicly available microarray data. We attempt to understand the regulatory mechanism underlying the variable expression of FXIIIA2 subunit in macrophages (M0, M1, M2 and aortic resident macrophages). Similarly, the FXIIIB2 subunit expression data from adult, fetal hepatocytes and embryonic stem cells derived hepatoblasts (hESC-hepatoblast) was analyzed. The results suggest regulatory dependence between the two FXIII subunits at the transcript level. Our analysis also predicts the involvement of the FXIIIA2 subunit in macrophage polarization, plaque stability, and inflammation. Full article
(This article belongs to the Special Issue Molecular Investigations into the Structure Functional Roles of Coagulation Factors/Proteins)
►▼ Show Figures

Figure 1

15 pages, 2722 KiB  
Article
A Homozygous Deep Intronic Variant Causes Von Willebrand Factor Deficiency and Lack of Endothelial-Specific Secretory Organelles, Weibel–Palade Bodies
by Hamideh Yadegari, Muhammad Ahmer Jamil, Natascha Marquardt and Johannes Oldenburg
Int. J. Mol. Sci. 2022, 23(6), 3095; https://doi.org/10.3390/ijms23063095 - 13 Mar 2022
Cited by 1 | Viewed by 2520
Abstract
A type 3 von Willebrand disease (VWD) index patient (IP) remains mutation-negative after completion of the conventional diagnostic analysis, including multiplex ligation-dependent probe amplification and sequencing of the promoter, exons, and flanking intronic regions of the VWF gene (VWF). In this [...] Read more.
A type 3 von Willebrand disease (VWD) index patient (IP) remains mutation-negative after completion of the conventional diagnostic analysis, including multiplex ligation-dependent probe amplification and sequencing of the promoter, exons, and flanking intronic regions of the VWF gene (VWF). In this study, we intended to elucidate causative mutation through next-generation sequencing (NGS) of the whole VWF (including complete intronic region), mRNA analysis, and study of the patient-derived endothelial colony-forming cells (ECFCs). The NGS revealed a variant in the intronic region of VWF (997 + 118 T > G in intron 8), for the first time. The bioinformatics assessments (e.g., SpliceAl) predicted this variant creates a new donor splice site (ss), which could outcompete the consensus 5′ donor ss at exon/intron 8. This would lead to an aberrant mRNA that contains a premature stop codon, targeting it to nonsense-mediated mRNA decay. The subsequent quantitative real-time PCR confirmed the virtual absence of VWF mRNA in IP ECFCs. Additionally, the IP ECFCs demonstrated a considerable reduction in VWF secretion (~6% of healthy donors), and they were devoid of endothelial-specific secretory organelles, Weibel–Palade bodies. Our findings underline the potential of NGS in conjunction with RNA analysis and patient-derived cell studies for genetic diagnosis of mutation-negative type 3 VWD patients. Full article
(This article belongs to the Special Issue Molecular Investigations into the Structure Functional Roles of Coagulation Factors/Proteins)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-2
Back to TopTop