Glucocorticoids inhibit the synthesis rate of type III collagen, but do not affect the hepatic clearance of its aminoterminal propeptide (PIIINP)

Aim. To study the morpho-molecular mechanisms underlying the formation of microscopic colitis (MC), as well as to identify features of its two forms – collagenous and lymphocytic.Material and methods. We studied biopsy samples from 23 patients exhibiting a clinical picture of irritable bowel syndrome; the material was obtained at the Endoscopic Department of the Region Clinic Hospital No. 2. The material was sampled from the five zones of the large intestine specified in the guidelines (Clinical Guidelines — Diagnosis and treatment of patients with digestive diseases, Appendix No. 3). The material was fixed in 10 % formalin, processed and embedded in paraffin. Sections were stained with hematoxylin and eosin (according to Mallory and Masson), as well as with picrosirius red, followed by the examination of these sections in polarised light. The immunohistochemical study was performed in line with the guidelines using monoclonal antibodies. Abcam antibodies (England) were used to detect type I and type III collagen; Cell Marque antibodies to CD4+ T and CD8+ T-lymphocytes (USA) were used to characterise lymphocytes.Results. It has been established that fi broblasts in the lamina propria play a key role in the pathogenesis of collagenous MC. This cell population synthesises extracellular matrix and forms layers of collagen fibres in the area under the surface epithelium. Pericryptal fibroblasts are also activated. Their differentiation occurs simultaneously with the migration of epithelial cells to the surface of the crypts with a possible change in their cellular composition. Intercryptal fi broblasts provide an increase in the synthesis rate of type III collagen. In the case of lymphocytic colitis, the pathogenetic mechanism is based on the relationship between lymphocytes and the cells in the lamina propria. The outcome is determined by the type of activated lymphocytes. CD8+ lymphocytes infiltrate the epithelial lining, causing a reaction to the luminal component, whereas CD4+ lymphocytes act as helpers and populate the lamina propria in the area under the epithelium.Conclusion. The pathogenesis of collagenous MC is based on the mechanism exhibited by the fibroblasts in the colon lamina propria, whereas the pathogenesis of lymphocytic colitis is determined by the dynamics of CD4+ T and CD8+ T-lymphocyte subpopulations.

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Methionine-Specific Staining of Collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010005408x ◽

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).

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Structural Insights into the Glycine Pair Motifs in Type III Collagen

ACS Biomaterials Science & Engineering ◽

10.1021/acsbiomaterials.6b00512 ◽

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

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

Biomolecules ◽

10.3390/biom11020156 ◽

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.

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

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)39323-8 ◽

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

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

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)36252-x ◽

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

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

Cell and Tissue Research ◽

10.1007/s00441-018-2954-3 ◽

2018 ◽

Vol 376 (1) ◽

pp. 123-135 ◽

Cited By ~ 3

Author(s):

Eri Ohto-Fujita ◽

Miho Shimizu ◽

Shoei Sano ◽

Masashi Kurimoto ◽

Kai Yamazawa ◽

...

Keyword(s):

Dermal Papilla ◽

Eggshell Membrane ◽

Type Iii Collagen ◽

Type Iii

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POLYMERIC TYPE-III COLLAGEN IN INFLAMED HUMAN SYNOVIA

The Lancet ◽

10.1016/s0140-6736(75)92145-5 ◽

1975 ◽

Vol 306 (7941) ◽

pp. 917 ◽

Cited By ~ 1

Author(s):

JacquelineB. Weiss ◽

C.Adrian Shuttleworth ◽

R. Brown ◽

JohnA.A. Hunter

Keyword(s):

Type Iii Collagen ◽

Type Iii

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

Journal of Histochemistry & Cytochemistry ◽

10.1177/43.4.7897183 ◽

1995 ◽

Vol 43 (4) ◽

pp. 421-427 ◽

Cited By ~ 17

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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