scholarly journals Collagen type VI is the antigen recognized by the ER‐TR7 antibody

2021 ◽  
Author(s):  
Alvise Schiavinato ◽  
Matthias Przyklenk ◽  
Birgit Kobbe ◽  
Mats Paulsson ◽  
Raimund Wagener
Keyword(s):  
Collagen Type ◽  
Collagen Type Vi

scholarly journals POS-777 ELEVATED PLASMA PRO-COLLAGEN TYPE VI PREDICTS ACUTE KIDNEY INJURY AFTER RENAL TRANSPLANTATION

2021 ◽  
Vol 6 (4) ◽  
pp. S338-S339
Author(s):  
M. Tepel ◽  
S. J. L. Bakker ◽  
O. Thaunat ◽  
S. Nagarajah ◽  
F. Genovese ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Renal Transplantation ◽  
Collagen Type ◽  
Kidney Injury ◽  
Elevated Plasma ◽  
Collagen Type Vi

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 Abnormal human chondrocyte morphology is related to increased levels of cell-associated IL-1β and disruption to pericellular collagen type VI

2010 ◽  
Vol 28 (11) ◽  
pp. 1507-1514 ◽  
Author(s):  
Dianne H. Murray ◽  
Peter G. Bush ◽  
Ivan J. Brenkel ◽  
Andrew C. Hall
Keyword(s):  
Collagen Type ◽  
Human Chondrocyte ◽  
Collagen Type Vi

scholarly journals Study of The Collagen Type VI Alpha 3 (COL6A3) Gene in Parkinson’s Disease

2021 ◽  
Author(s):  
Chong-Yao Jin ◽  
Ran Zheng ◽  
Zhi-Hao Lin ◽  
Nai-Jia Xue ◽  
Ying Chen ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Collagen Type ◽  
Gene Mutations ◽  
Compound Heterozygous ◽  
Genetic Characteristics ◽  
Increased Risk ◽  
Collagen Type Vi ◽  
Chinese Cohort ◽  
Aggregate Burden

Abstract Background To date, the genetic contribution to Parkinson’s disease (PD) remains unclear. Mutations in the collagen type VI alpha 3 (COL6A3) gene were recently identified as a cause of isolated dystonia. Since PD and dystonia are closely related disorders with shared clinical and genetic characteristics, we explored the association between COL6A3 and PD in a Chinese cohort. Methods We performed genetic screening of COL6A3 in a Chinese cohort of 173 patients with sporadic PD and 200 healthy controls. We identified variants that are likely to have pathogenic effects based on: 1) a minor allele frequency of < 0.01; and 2) the variant being recognized as deleterious by at least 15 different in silico predicting tools. Finally, we tested the aggregate burden of COL6A3 on PD via SKAT-O analysis. Results First, we found compound heterozygous COL6A3 gene mutations in one early-onset PD patients. Then, we explored whether COL6A3 variants contributed to increased risk of developing PD in a Chinese population. We detected 21 rare non-synonymous variants. Pathogenicity predictions identified seven novel non-synonymous variants as likely to be pathogenic. SKAT-O analysis further revealed that an aggregate burden of variants in COL6A3 contributes to PD (p = 0.03). Conclusion An increased aggregate burden of the COL6A3 gene was detected in patients with PD.

scholarly journals Compromised cardiac performance and remodeling in collagen type VI deficient mice after myocardial infarction

2009 ◽  
Vol 23 (S1) ◽  
Author(s):  
Daniel John Luther ◽  
Patricia E. Shamhart ◽  
Vaghan Ohanyan ◽  
Cheryl M. Hodnichak ◽  
James T. Miller ◽  
...  
Keyword(s):  
Myocardial Infarction ◽  
Collagen Type ◽  
Cardiac Performance ◽  
Collagen Type Vi ◽  
Deficient Mice

Collagen type VI

1998 ◽  
pp. 69-76 ◽  
Author(s):  
Shirley Ayad ◽  
Ray Boot-Handford ◽  
Martin J. Humphries ◽  
Karl E. Kadler ◽  
Adrian Shuttleworth
Keyword(s):  
Collagen Type ◽  
Collagen Type Vi

Collagen type VI expression during cardiac development and in human fetuses with trisomy 21

2003 ◽  
Vol 275A (2) ◽  
pp. 1109-1116 ◽  
Author(s):  
Adriana C. Gittenberger-De Groot ◽  
Ulrike Bartram ◽  
Petra W. Oosthoek ◽  
Margot M. Bartelings ◽  
Bianca Hogers ◽  
...  
Keyword(s):  
Trisomy 21 ◽  
Collagen Type ◽  
Cardiac Development ◽  
Human Fetuses ◽  
Collagen Type Vi
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