scholarly journals Collagen VI as a driver and disease biomarker in human fibrosis

FEBS Journal ◽  
2021 ◽  
Author(s):  
Lynn. Williams ◽  
Thomas Layton ◽  
Nan Yang ◽  
Marc Feldmann ◽  
Jagdeep Nanchahal
Keyword(s):  
Collagen Vi ◽  
Disease Biomarker

Determination of Cardiac Disease Biomarker by Plasmonic Sandwich‐ELISA

2020 ◽  
Author(s):  
Weirong Wei ◽  
Yinyan Tang ◽  
Huimin He ◽  
Subash C.B. Gopinath ◽  
Lingling Wang
Keyword(s):  
Cardiac Disease ◽  
Sandwich Elisa ◽  
Disease Biomarker

scholarly journals Ligand Binding to the Collagen VI Receptor Triggers a Talin-to-RhoA Switch that Regulates Receptor Endocytosis

2020 ◽  
Vol 53 (4) ◽  
pp. 418-430.e4
Author(s):  
Jérôme Bürgi ◽  
Laurence Abrami ◽  
Irinka Castanon ◽  
Luciano Andres Abriata ◽  
Beatrice Kunz ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Collagen Vi ◽  
Receptor Endocytosis

scholarly journals Collagen type VI in the human bone marrow microenvironment: a strong cytoadhesive component

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1740-1748 ◽  
Author(s):  
G Klein ◽  
CA Muller ◽  
E Tillet ◽  
ML Chu ◽  
R Timpl
Keyword(s):  
Bone Marrow ◽  
Cell Lines ◽  
Triple Helix ◽  
Collagen Type ◽  
Hematopoietic Cell ◽  
Human Bone ◽  
Human Bone Marrow ◽  
Collagen Vi ◽  
Collagen Type Vi ◽  
Hematopoietic Cell Lines

Collagen type VI, which forms characteristic microfibrillar structures, is assembled from three individual alpha(VI) chains that form a short triple helix and two adjacent globular domains. Expression of all three alpha (VI) collagen chains in the human bone marrow (BM) microenvironment could be detected by chain-specific antibodies in tissue sections and in the adherent stromal layer of long-term BM cultures. In functional studies, collagen type VI was shown to be a strong adhesive substrate for various hematopoietic cell lines and light-density BM mononuclear cells. The adhesive site within the molecule seems to be restricted to the triple helical domain of all three alpha (VI) chains, because individual alpha (VI) chains were not active in the attachment assays. Adhesion of the hematopoietic cell lines to collagen VI was dose-dependent and could be inhibited by heparin. Although the triple helix contains several RGD sequences, adhesion of the hematopoietic cell types to collagen VI could be blocked neither by RGD-containing peptides nor by a neutralizing antibody to the beta 1 integrin subunit. In combination with an antiadhesive substrate, the binding properties of collagen VI could be downregulated. These data suggest that this collagen type may play an important role in the adhesion of hematopoietic cells within the BM microenvironment.

scholarly journals Collagen VI (COL6)

2009 ◽  
Vol 2 (3) ◽  
pp. 103-103
Keyword(s):  
Collagen Vi

scholarly journals Effects of Risperidone and Galantamine Treatment on Alzheimer’s Disease Biomarker Levels in Cerebrospinal Fluid

2017 ◽  
Vol 57 (2) ◽  
pp. 387-393 ◽  
Author(s):  
Victor Bloniecki ◽  
Dag Aarsland ◽  
Kaj Blennow ◽  
Jeffrey Cummings ◽  
Farshad Falahati ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Cerebrospinal Fluid ◽  
Disease Biomarker

scholarly journals CMG2/ANTXR2 regulates extracellular collagen VI which accumulates in hyaline fibromatosis syndrome

2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Jérôme Bürgi ◽  
Béatrice Kunz ◽  
Laurence Abrami ◽  
Julie Deuquet ◽  
Alessandra Piersigilli ◽  
...  
Keyword(s):  
Collagen Vi ◽  
Hyaline Fibromatosis Syndrome

Effect of Mechanical Strain on the Collagen VI Pericellular Matrix in Anterior Cruciate Ligament Fibroblasts

2014 ◽  
Vol 229 (7) ◽  
pp. 878-886 ◽  
Author(s):  
Francesca Sardone ◽  
Francesco Traina ◽  
Francesca Tagliavini ◽  
Camilla Pellegrini ◽  
Luciano Merlini ◽  
...  
Keyword(s):  
Anterior Cruciate Ligament ◽  
Cruciate Ligament ◽  
Mechanical Strain ◽  
Pericellular Matrix ◽  
Collagen Vi ◽  
Anterior Cruciate

scholarly journals Cloning and sequence analysis of cDNAs encoding the α1, α2 and α3 chains of mouse collagen VI

1993 ◽  
Vol 291 (3) ◽  
pp. 787-792 ◽  
Author(s):  
R Z Zhang ◽  
T C Pan ◽  
R Timpl ◽  
M L Chu
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Untranslated Regions ◽  
Cdna Libraries ◽  
Cdna Clones ◽  
Collagen Vi ◽  
Central Segment ◽  
Glycosylation Sites ◽  
Key Features ◽  
Triple Helical Domain

cDNA clones encoding the alpha 1, alpha 2 and alpha 3 chains of mouse collagen VI have been isolated by screening cDNA libraries with the corresponding human probes. The composite cDNAs for the alpha 1, alpha 2, and alpha 3 chains are 2.5, 1.6 and 2.9 kb in size respectively. The alpha 1 and alpha 2 cDNAs encode the C-terminal portions of the chains as well as the entire 3′-untranslated regions, while the alpha 3 cDNAs encode a central segment of 959 amino acids flanking the triple-helical domain. The deduced amino acid sequences share 86-88% identity with the human counterparts and 67-73% identity with the chicken equivalents. Alignment of the deduced amino acid sequences of mouse, human and chicken collagens reveal that the key features of the protein, including the cysteine residues, imperfections in the Gly-Xaa-Xaa regions, Arg-Gly-Asp sequences and potential N-glycosylation sites, are mostly conserved.

Sign in / Sign up

Export Citation Format

Share Document