scholarly journals Immunoelectron microscopic localization of laminin, type IV collagen, and type III pN-collagen in reticular fibers of human lymph nodes.

1989 ◽  
Vol 37 (3) ◽  
pp. 279-286 ◽  
Author(s):  
T Karttunen ◽  
R Sormunen ◽  
L Risteli ◽  
J Risteli ◽  
H Autio-Harmainen
Keyword(s):  
Basement Membrane ◽  
Lymph Nodes ◽  
Blood Vessels ◽  
Type Iv Collagen ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Amino Terminal ◽  
Type Iv ◽  
Reticular Fibers ◽  
Collagenous Fibers

We studied the ultrastructural distribution of laminin, type IV collagen, and the amino terminal pro-peptide of type III collagen (type III pN-collagen) in normal human lymph nodes. After fixation with freshly prepared 4% paraformaldehyde mixed with 0.1% glutaraldehyde, cryoultramicrotomy proved to preserve the antigenicity of these proteins better than embedding in Lowicryl K4M. Sections were treated with rabbit antibodies against the 7S domain of human type IV collagen, the fragment P1 of human laminin, and the amino terminal pro-peptide of human type III pro-collagen, followed by anti-rabbit IgG conjugated to 10-nm colloidal gold. Laminin and type IV collagen were seen in the basement membrane structures of the blood vessels and in the walls of sinuses. The amorphous material between the collagenous fibers in locations corresponding to reticular fibers also contained laminin and type IV collagen. The amino terminal pro-peptide of type III pro-collagen was present in the collagenous fibers in reticular fibers and in the walls of blood vessels and sinuses. Therefore, a significant number of the type III collagen molecules in these fibers must have retained their amino terminal pro-peptide. These results indicate that the basement membrane proteins laminin and type IV collagen are genuine components of reticular fibers, as suggested earlier by immunohistochemical studies at the light microscopic level.

scholarly journals An Ehrlich chromogen in collagen cross-links

1983 ◽  
Vol 209 (1) ◽  
pp. 263-264 ◽  
Author(s):  
J E Scott ◽  
R G Qian ◽  
W Henkel ◽  
R W Glanville
Keyword(s):  
Type Iv Collagen ◽  
Rich Source ◽  
Type Iii Collagen ◽  
Cross Link ◽  
Type Iii ◽  
Human Type ◽  
Type Iv ◽  
Cross Links

A well-characterized three-chain peptide [(Col1)2 X T9] from human type III collagen was a rich source of Ehrlich chromogen. The corresponding two-chain peptide [(Col1)2] was not, implying that the Ehrlich chromogen is a trifunctional cross-link. (Col1)2 X T9 also contained pyridinoline, which is not an Ehrlich chromogen. The 7S domain of type IV collagen also contained an Ehrlich chromogen.

scholarly journals RETRACTED: Production and Characterization of Recombinant Rat Non-collagen Domain of α3 Chain of Type IV Collagen α3 (IV) NC1 Antigen

2016 ◽  
Vol 12 (24) ◽  
pp. 98
Author(s):  
Afsana Munni
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Type Iv Collagen ◽  
Kidney Diseases ◽  
Cell Epitope ◽  
Affinity Column ◽  
Igg Antibody ◽  
Amino Terminal ◽  
Type Iv ◽  
Collagenous Domain

Glomerulonephritis disease is characterized by inflammation of glomeruli or small blood vessels in the kidney which causes kidney diseases. Glomerulonephritis disease deposits the anti-GBM auto antibody in the glomerular basement membrane. The type IV collagen is the main component of glomerular basement membrane that has α3 chain of type (IV) collagen of non-collagenous domain which contains N-terminal 7S domain, a triple helical collagenous domain, and a C- terminal non-collagenous glomerular domain (NC1). The amino terminal of α3 (IV) NC1 that induces the experimental autoimmuno glomerulonephritis (EAG) in rat model has been identified. The recombinant rat α3 (IV)NC1 antigen has nine amino acid span that is consistent with antibody or T cell epitope which is induced in EAG. The research is carried out on the recombinant rat α3 (IV) NC1 production, purification, quantification, and characterization. The circulation of Anti-GBM antibody in glomerular basement membrane can be measured by the ELISA assay. In addition, the recombinant rat antigen is secreted in HEK293 cell supernatant which is purified by Anti-FLAG M2 monoclonal IgG antibody affinity column. In addition, it is characterized and quantified by SDS-PAGE gel electrophoresis and Western blotting techniques.

Distribution of laminin and collagens during avian neural crest development

Development ◽  
1987 ◽  
Vol 101 (3) ◽  
pp. 461-478 ◽  
Author(s):  
J.L. Duband ◽  
J.P. Thiery
Keyword(s):  
Cell Migration ◽  
Neural Crest ◽  
Type Iv Collagen ◽  
Type I Collagen ◽  
Neural Crest Cell ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Type Iv ◽  
Crest Cell

The distribution of type I, III and IV collagens and laminin during neural crest development was studied by immunofluorescence labelling of early avian embryos. These components, except type III collagen, were present prior to both cephalic and trunk neural crest appearance. Type I collagen was widely distributed throughout the embryo in the basement membranes of epithelia as well as in the extracellular spaces associated with mesenchymes. Type IV collagen and laminin shared a common distribution primarily in the basal surfaces of epithelia and in close association with developing nerves and muscle. In striking contrast with the other collagens and laminin, type III collagen appeared secondarily during embryogenesis in a restricted pattern in connective tissues. The distribution and fate of laminin and type I and IV collagens could be correlated spatially and temporally with morphogenetic events during neural crest development. Type IV collagen and lamin disappeared from the basal surface of the neural tube at sites where neural crest cells were emerging. During the course of neural crest cell migration, type I collagen was particularly abundant along migratory pathways whereas type IV collagen and laminin were distributed in the basal surfaces of the epithelia lining these pathways but were rarely seen in large amounts among neural crest cells. In contrast, termination of neural crest cell migration and aggregation into ganglia were correlated in many cases with the loss of type I collagen and with the appearance of type IV collagen and laminin among the neural crest population. Type III collagen was not observed associated with neural crest cells during their development. These observations suggest that laminin and both type I and IV collagens may be involved with different functional specificities during neural crest ontogeny. (i) Type I collagen associated with fibronectins is a major component of the extracellular spaces of the young embryo. Together with other components, it may contribute to the three-dimensional organization and functions of the matrix during neural crest cell migration. (ii) Type III collagen is apparently not required for tissue remodelling and cell migration during early embryogenesis. (iii) Type IV collagen and laminin are important components of the basal surface of epithelia and their distribution is consistent with tissue remodelling that occurs during neural crest cell emigration and aggregation into ganglia.

Immunohistochemical Analysis of Type III and IV Collagens in Tubulointerstitial Damage in Human Benign Nephrosclerosis

1995 ◽  
Vol 23 (6) ◽  
pp. 480-486 ◽  
Author(s):  
M S Razzaque ◽  
M Cheng ◽  
Y Horita ◽  
M Nishihara ◽  
T Harada ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Structural Changes ◽  
Immunohistochemical Analysis ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Type Iv ◽  
Tubulointerstitial Damage ◽  
Basement Membrane Collagen ◽  
Immunohistochemical Techniques

Prolonged hypertension causes structural changes including glomerulosclerosis and tubulointerstitial damage of the kidney, termed benign nephrosclerosis. It is generally accepted that, in benign nephrosclerosis, increased accumulation of extracellular matrix in the glomeruli results in glomerulosclerosis. Little is known, however, about the possible role of the extracellular matrix in the tubulointerstitial damage in benign nephrosclerosis. In this study, the possible roles of type IV basement-membrane collagen and type III interstitial collagen in tubulointerstitial damage caused by hypertension were explored. Immunohistochemical techniques were used to investigate the distribution of type III and type IV collagens in the kidney sections of 15 patients with benign nephrosclerosis with tubulointerstitial damage and in 10 controls. In the control renal sections strong immunostaining for type III collagen was found in the interstitium and immunostaining for type IV collagen was present in the tubular basement membrane and weakly in the interstitium. In the patients with tubulointerstitial damage there was increased immunostaining for both type III and type IV collagens in the expanded interstitium and damaged tubules than was found in the control kidney sections. These findings indicate that increased accumulation of both type III and type IV collagens might play a significant role in the tubulointerstitial damage in benign nephrosclerosis.

scholarly journals Blood-based extracellular matrix biomarkers are correlated with clinical outcome after PD-1 inhibition in patients with metastatic melanoma

2020 ◽  
Vol 8 (2) ◽  
pp. e001193
Author(s):  
Daan P Hurkmans ◽  
Christina Jensen ◽  
Stijn L W Koolen ◽  
Joachim Aerts ◽  
Morten Asser Karsdal ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Clinical Outcome ◽  
Metastatic Melanoma ◽  
Type Iv Collagen ◽  
Type Iii Collagen ◽  
Cox Regression Analysis ◽  
High Baseline ◽  
Type Iii ◽  
Type Iv ◽  
M1 Macrophage

BackgroundImmune checkpoint inhibitors that target the programmed cell death protein 1 (PD-1) receptor induce a response in only a subgroup of patients with metastatic melanoma. Previous research suggests that transforming growth factor beta signaling and a collagen-rich peritumoral stroma (tumor fibrosis), may negatively interfere with the interaction between T cells and tumor cells and thereby contribute to resistance mechanisms by immune-exclusion, while increased tumor infiltration of M1-like macrophages enhances T cell activity. Hence, the current study aimed to assess the relationship between blood-based markers of collagen or vimentin turnover (reflecting M1 macrophage activity) and clinical outcome in patients with metastatic melanoma after PD-1 inhibition.MethodsPatients with metastatic melanoma who were treated with anti-PD-1 monotherapy between May 2016 and March 2019 were included in a prospective observational study. N-terminal pro-peptide of type III collagen (PRO-C3) cross-linked N-terminal pro-peptides of type III collagen (PC3X), matrix metalloprotease (MMP)-degraded type III (C3M) and type IV collagen (C4M), granzyme B-degraded type IV collagen and citrullinated and MMP-degraded vimentin (VICM) were measured with immunoassays in serum before (n=107), and 6 weeks after the first administration of immunotherapy (n=94). The association between biomarker levels and overall survival (OS) or progression-free survival (PFS) was assessed.ResultsMultivariate Cox regression analysis identified high baseline PRO-C3 (Q4) and PC3X (Q4) as independent variables of worse PFS (PRO-C3: HR=1.81, 95% CI=1.06 to 3.10, p=0.030 and PC3X: HR=1.86, 95% CI=1.09 to 3.18, p=0.023). High baseline PRO-C3 was also independently related to worse OS (HR=2.08, 95% CI=1.06 to 4.09, p=0.035), whereas a high C3M/PRO-C3 ratio was related to improved OS (HR=0.42, 95% CI=0.20 to 0.90, p=0.025). An increase in VICM (p<0.0001; in 56% of the patients) was observed after 6 weeks of treatment, and an increase in VICM was independently associated with improved OS (HR=0.28, 95% CI=0.10 to 0.77, p=0.014).ConclusionsBlood-based biomarkers reflecting excessive type III collagen turnover were associated with worse OS and PFS after PD-1 inhibition in metastatic melanoma. Moreover, an increase in VICM levels after 6 weeks of treatment was associated with improved OS. These findings suggest that type III collagen and vimentin turnover contribute to resistance/response mechanisms of PD-1 inhibitors and hold promise of assessing extracellular matrix-derived and stroma-derived components to predict immunotherapy response.

Synthesis of type III Collagen and type IV collagen by tubular epithelial cells in diabetic nephropathy

1995 ◽  
Vol 191 (11) ◽  
pp. 1099-1104 ◽  
Author(s):  
M.S. Razzaque ◽  
T. Koji ◽  
Y. Horita ◽  
M. Nishihara ◽  
T. Harada ◽  
...  
Keyword(s):  
Diabetic Nephropathy ◽  
Epithelial Cells ◽  
Type Iv Collagen ◽  
Type Iii Collagen ◽  
Tubular Epithelial Cells ◽  
Type Iii ◽  
Type Iv

Use of a Biodegradable Neuroprosthesis Containing Laminin for Avulsive Peripheral Nerve Injury Results in Early Endoneurial and Perineurial Collagen Type III Formation

1990 ◽  
Vol 48 (3) ◽  
pp. 158-159
Author(s):  
B. Giammara ◽  
E. Anderson ◽  
P. Yates ◽  
J. Zuniga ◽  
J. Hanker
Keyword(s):  
Basement Membrane ◽  
Peripheral Nerve ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Type Iii Collagen ◽  
Distal Stump ◽  
Type Iii ◽  
Type Iv ◽  
Direct Anastomosis ◽  
Leg Movement

The direct anastomosis of nerve stumps is most desirable after peripheral nerve transection. There are many avulsive nerve injuries, however, where a nerve segment is destroyed or must be removed -- and the proximal and distal stumps are separated by a gap requiring bridging. Earlier studies showed that a biodegradable polyester mesh (polyglactin 910, Vicryl™) sleeve can act as a conduit and guide regenerating axons into the distal stump across an 11 mm gap created in rat sciatic nerve. This is facilitated by filling the sleeve with Matrigel™, an extracellular basement membrane gel containing 80% laminin, smaller amounts of collagen type IV, heparan sulfate proteoglycan and entaction. The avulsed sciatic was reconnected in animals examined after 30 and 45 days and sensation and leg movement were much improved.The PATS variation of the PAS reaction can be used to demonstrate all glycomacromolecules containing alpha-diglycol groups. Although it also stains basement membrane or type IV collagen brown, it stains type III collagen or reticulin intensely black.

scholarly journals P047 Differences in extra cellular matrix remodelling in highly active Crohn’s disease and ulcerative colitis

2020 ◽  
Vol 14 (Supplement_1) ◽  
pp. S156-S157
Author(s):  
V Domislović ◽  
J H Mortensen ◽  
M A Karsdal ◽  
M Brinar ◽  
T Manon-Jensen ◽  
...  
Keyword(s):  
Ulcerative Colitis ◽  
Disease Activity ◽  
Type Iv Collagen ◽  
Collagen Degradation ◽  
Type Iii Collagen ◽  
Collagen Turnover ◽  
Collagen Formation ◽  
Type Iii ◽  
Highly Active ◽  
Type Iv

Abstract Background Ulcerative colitis (UC) and Crohn’s disease (CD) require continuous evaluation of disease activity and response to therapy. Current gold standard is endoscopy; therefore it is important to investigate biomarkers associated with endoscopic disease activity. Extra cellular matrix (ECM) consists of basement membrane (BM) and interstitial matrix (IM). BM consists mainly of type IV collagen, while IM of types I, III and V collagen. Pathological environment leads to impaired remodelling, structure, quality and function of the ECM. We investigated biomarkers of collagen degradation and formation and their association with endoscopic disease activity and in patients with CD and UC. Methods In this cross-sectional study, we measured six biomarkers of ECM remodelling in 94 IBD patients (60 with CD and 34 UC). Biomarkers of type III collagen degradation (C3M) and formation (PRO-C3), type IV collagen degradation (C4M), formation (PRO-C4), type V collagen formation (PRO-C5) and PROC23 were measured in serum by ELISA. Inflammatory activity was measured using endoscopic scores; SES-CD for CD, MES and modified MES (mMES) for UC. Patients were divided in remission and mild activity group vs. moderate-to-severe activity (SES-CD &lt; 3 vs. ≥3 and MES &lt; 2 vs. ≥2) Student t-test and correlation analysis were applied in statistical analysis. Results CD patients with moderate and severe disease had lower levels of PRO-C3 (14.7 ± 10.5 vs. 9.9 ± 4.6, p = 0.04), and higher levels of C4M (26.54 ± 10.5 vs. 37.8 ± 20, p = 0.009) compared with patients in remission and mild disease. Biomarker of type III collagen turnover (C3M/PROC3) showed higher levels in moderate and severe active disease in CD (1 ± 0.5 vs. 1.8 ± 1.1, p = 0.006). UC patients with moderate to severe activity showed higher levels of type III collagen turnover biomarker (C3M/PROC3) (1.1 ± 0.4 vs. 1.97 ± 1, p = 0.049). C4M correlated positively (r = 0.28, p = 0.03) and PRO-C3 correlated negatively (r = −0.29, p = 0.03) to SES-CD and combined in a multivariate regression model (r = 0.39, p = 0.009). C3M (r = 0.60, p = 0.004) and C4M (r = 0.36, p = 0.039) correlated positively with mMES. Conclusion In highly active CD, there is increased type IV collagen degradation and reduced type III collagen formation. Both biomarkers significantly correlate with SES-CD, with increased correlation when combined together. Type III collagen turnover is increased in highly active CD and UC. Biomarkers of types III and IV collagen degradation correlate significantly with mMES. Biomarkers of types III and IV collagen could be used to differentiate highly active CD from UC. Our findings suggest that biomarkers of basement membrane and interstitial matrix remodelling may be used as surrogate markers for monitoring of disease activity for UC and CD.

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