scholarly journals Clinical value of serum hyaluronan and propeptide of type III collagen in patients with pancreatic cancer

2020 ◽  
Vol 146 (10) ◽  
pp. 2913-2922 ◽  
Author(s):  
Inna M. Chen ◽  
Nicholas Willumsen ◽  
Christian Dehlendorff ◽  
Astrid Z. Johansen ◽  
Benny V. Jensen ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Type Iii Collagen ◽  
Clinical Value ◽  
Type Iii ◽  
Serum Hyaluronan

scholarly journals 22 The potential of serum autoantibodies against type III collagen in cancer

2021 ◽  
Vol 9 (Suppl 3) ◽  
pp. A24-A24
Author(s):  
Christina Jensen ◽  
Jeppe Thorlacius-Ussing ◽  
Patryk Drobinski ◽  
Morten Karsdal ◽  
Anne-Christine Bay-Jensen ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Prostate Cancer ◽  
Colorectal Cancer ◽  
Lung Cancer ◽  
Ovarian Cancer ◽  
Pancreatic Cancer ◽  
Type Iii Collagen ◽  
Healthy Controls ◽  
Type Iii ◽  
Tumor Types

BackgroundAutoantibodies are classically associated with autoimmune diseases but have recently emerged as attractive cancer biomarkers as they can be easily assessed in serum. Certain autoantibodies have been shown to promote cancer while others contribute to the body’s defense against it. Cancer progression is associated with excessive remodeling of the extracellular matrix (ECM) and collagen, but little is known about the role of autoantibodies against collagen in cancer. To investigate autoreactivity against collagen in cancer, we developed a novel biomarker assay to quantify autoantibodies against type III collagen products in serum from patients with various solid tumor types and compared levels with those find in healthy controls.MethodsThe presence and levels of autoantibodies against denatured type III collagen were measured in pretreatment serum from 223 patients with bladder cancer (n=20), breast cancer (n=20), colorectal cancer (n=20), head and neck cancer (n=20), kidney cancer (n=20), liver cancer (n=3), lung cancer (n=20), melanoma (n=20), ovarian cancer (n=20), pancreatic cancer (n=20), prostate cancer (n=20), and stomach cancer (n=20), and compared to age-matched healthy controls (n=33). Statistical differences were analyzed using the Kruskal-Wallis test adjusted for Dunn’s multiple comparisons test.ResultsSerum levels of autoantibodies against type III collagen were significantly lower in patients with bladder cancer (p=0.0007), breast cancer (p=0.0002), colorectal cancer (p<0.0001), head and neck cancer (p=0.0005), kidney cancer (p=0.005), liver cancer (p=0.030), lung cancer (p=0.0004), melanoma (p<0.0001), ovarian cancer (p<0.0001), pancreatic cancer (p<0.0001), prostate cancer (p<0.0001), and stomach cancer (p<0.0001) compared to healthy controls. This autoimmunity biomarker could discriminate between cancer and healthy controls with an AUROC value of 0.88 (p<0.0001).ConclusionsIn this study, we observed that cancer patients with different solid tumor types have downregulated levels of circulating autoantibodies directed against type III collagen compared to healthy controls suggesting that autoantibodies against type III collagen and tumor fibrosis may be important for tumor control and eradication. This autoimmunity biomarker may have the potential for studying and monitoring the close relationship between autoimmunity and cancer such as the risk of developing cancer on rheumatoid arthritis immunosuppressant or the risk of developing immune-related adverse events on cancer immunotherapy.Ethics ApprovalThe serum samples in this study were obtained from the commercial vendor Proteogenex and BioIVT, and according to the vendors, sample collection was approved by an Institutional Review Board or Independent Ethical Committee and patients gave their informed consent (Protocol numbers PG-ONC 2003/1 and WIRB® Protocol #20161665). All investigations were carried out according to the Helsinki Declaration.

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Structural Insights into the Glycine Pair Motifs in Type III Collagen

2017 ◽  
Vol 3 (3) ◽  
pp. 269-278
Author(s):  
Bo An ◽  
Shu-Wei Chang ◽  
Cody Hoop ◽  
Jean Baum ◽  
Markus J. Buehler ◽  
...  
Keyword(s):  
Type Iii Collagen ◽  
Type Iii ◽  
Structural Insights

scholarly journals Type III Collagen is Required for Adipogenesis and Actin Stress Fibre Formation in 3T3-L1 Preadipocytes

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 156
Author(s):  
Mohammad Al Hasan ◽  
Patricia E. Martin ◽  
Xinhua Shu ◽  
Steven Patterson ◽  
Chris Bartholomew
Keyword(s):  
Quantitative Polymerase Chain Reaction ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Actin Stress Fibre ◽  
Matrix Gene ◽  
Gene Transcripts ◽  
Polymerase Chain ◽  
Oil Red O Staining ◽  
Oil Red O

GPR56 is required for the adipogenesis of preadipocytes, and the role of one of its ligands, type III collagen (ColIII), was investigated here. ColIII expression was examined by reverse transcription quantitative polymerase chain reaction, immunoblotting and immunostaining, and its function investigated by knockdown and genome editing in 3T3-L1 cells. Adipogenesis was assessed by oil red O staining of neutral cell lipids and production of established marker and regulator proteins. siRNA-mediated knockdown significantly reduced Col3a1 transcripts, ColIII protein and lipid accumulation in 3T3-L1 differentiating cells. Col3a1−/− 3T3-L1 genome-edited cell lines abolished adipogenesis, demonstrated by a dramatic reduction in adipogenic moderators: Pparγ2 (88%) and C/ebpα (96%) as well as markers aP2 (93%) and oil red O staining (80%). Col3a1−/− 3T3-L1 cells displayed reduced cell adhesion, sustained active β-catenin and deregulation of fibronectin (Fn) and collagen (Col4a1, Col6a1) extracellular matrix gene transcripts. Col3a1−/− 3T3-L1 cells also had dramatically reduced actin stress fibres. We conclude that ColIII is required for 3T3-L1 preadipocyte adipogenesis as well as the formation of actin stress fibres. The phenotype of Col3a1−/− 3T3-L1 cells is very similar to that of Gpr56−/− 3T3-L1 cells, suggesting a functional relationship between ColIII and Gpr56 in preadipocytes.

scholarly journals Subpopulations of rat lung fibroblasts with different amounts of type I and type III collagen mRNAs.

1990 ◽  
Vol 265 (11) ◽  
pp. 6286-6290
Author(s):  
E Breen ◽  
V M Falco ◽  
M Absher ◽  
K R Cutroneo
Keyword(s):  
Lung Fibroblasts ◽  
Type Iii Collagen ◽  
Type I ◽  
Rat Lung ◽  
Type Iii

scholarly journals Cleavage of bovine skin type III collagen by proteolytic enzymes. Relative resistance of the fibrillar form.

1985 ◽  
Vol 260 (30) ◽  
pp. 16411-16417
Author(s):  
H Birkedal-Hansen ◽  
R E Taylor ◽  
A S Bhown ◽  
J Katz ◽  
H Y Lin ◽  
...  
Keyword(s):  
Proteolytic Enzymes ◽  
Skin Type ◽  
Type Iii Collagen ◽  
Relative Resistance ◽  
Type Iii

scholarly journals Solubilized eggshell membrane supplies a type III collagen-rich elastic dermal papilla

2018 ◽  
Vol 376 (1) ◽  
pp. 123-135 ◽  
Author(s):  
Eri Ohto-Fujita ◽  
Miho Shimizu ◽  
Shoei Sano ◽  
Masashi Kurimoto ◽  
Kai Yamazawa ◽  
...  
Keyword(s):  
Dermal Papilla ◽  
Eggshell Membrane ◽  
Type Iii Collagen ◽  
Type Iii

POLYMERIC TYPE-III COLLAGEN IN INFLAMED HUMAN SYNOVIA

The Lancet ◽  
1975 ◽  
Vol 306 (7941) ◽  
pp. 917 ◽  
Author(s):  
JacquelineB. Weiss ◽  
C.Adrian Shuttleworth ◽  
R. Brown ◽  
JohnA.A. Hunter
Keyword(s):  
Type Iii Collagen ◽  
Type Iii

scholarly journals Immunolocalization of type III collagen in human articular cartilage prepared by high-pressure cryofixation, freeze-substitution, and low-temperature embedding.

1995 ◽  
Vol 43 (4) ◽  
pp. 421-427 ◽  
Author(s):  
R D Young ◽  
P A Lawrence ◽  
V C Duance ◽  
T Aigner ◽  
P Monaghan
Keyword(s):  
High Pressure ◽  
Articular Cartilage ◽  
Polyclonal Antibodies ◽  
Freeze Substitution ◽  
Immunogold Electron Microscopy ◽  
Type Iii Collagen ◽  
Human Articular Cartilage ◽  
Chemical Fixation ◽  
Osteoarthritic Cartilage ◽  
Type Iii

We localized Type III collagen by immunogold electron microscopy in resin sections of intact normal and osteoarthritic human articular cartilage. Comparisons of antibody staining between tissue prepared by high-pressure cryofixation and freeze-substitution without fixatives and that exposed to conventional mild chemical fixation with paraformaldehyde showed that dedicated cryotechniques yielded superior preservation of epitopes that are modified by chemical fixation, and simultaneously provided good ultrastructural preservation. Type III collagen was detected with two polyclonal antibodies, one against the triple-helical domain of the molecule and a second against the more antigenic, globular amino pro-peptide domain, which in this collagen is retained in the extracellular matrix after secretion. Positive labeling was seen in association with the major interstitial fibrils, suggesting co-polymerization of Types III and II collagen in cartilage. Type III collagen could not be detected in aldehyde-fixed normal cartilage. In fixed osteoarthritic cartilage, Type III was detectable only when the antibody to the amino pro-peptide was employed. In contrast, high-pressure cryofixation and freeze-substitution preserved epitopes for both antibodies, permitting immunodetection of Type III collagen in normal and osteoarthritic cartilage. Cryotechniques offer exciting possibilities for significantly improving the immunolocalization of collagens and other fixative-sensitive antigens in situ.

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