Type I and Type III Collagen mRNA Levels in Kidney Regions of Old and Young Rats

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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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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Coordinate regulation of the levels of type III and type I collagen mRNA in most but not all mouse fibroblasts.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89765-4 ◽

1985 ◽

Vol 260 (1) ◽

pp. 531-536

Author(s):

G Liau ◽

Y Yamada ◽

B de Crombrugghe

Keyword(s):

Type I Collagen ◽

Type I ◽

Coordinate Regulation ◽

Mouse Fibroblasts ◽

Type Iii ◽

Collagen Mrna

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Infliximab Increases the Tissue Contents of Type-I and Type-III Collagen in Colorectal Segments Without Fecal Stream After Hartmann’s Procedure

Journal of Gastrointestinal Surgery ◽

10.1007/s11605-021-05138-3 ◽

2021 ◽

Author(s):

Bruna Zini de Paula Freitas ◽

Fábio Guilherme Campos ◽

Danilo Toshio Kanno ◽

Andress Godoy Delben ◽

José Aires Pereira ◽

...

Keyword(s):

Hartmann’S Procedure ◽

Type Iii Collagen ◽

Type I ◽

Fecal Stream ◽

Type Iii ◽

Hartmann's Procedure ◽

Tissue Contents

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Change in phenotype in long-term cultures of a clonal rat bone cell line: switch to the synthesis of α1 (I)-trimer collagen

Canadian Journal of Biochemistry and Cell Biology ◽

10.1139/o84-063 ◽

1984 ◽

Vol 62 (6) ◽

pp. 462-469 ◽

Cited By ~ 2

Author(s):

Hardy Limeback ◽

Kichibee Otsuka ◽

Kam-Ling Yao ◽

Jane E. Aubin ◽

Jaro Sodek

Keyword(s):

Collagen Synthesis ◽

Type I Collagen ◽

Bone Cell ◽

Detectable Effect ◽

Prostaglandin E ◽

Intracellular Camp ◽

Type Iii Collagen ◽

Type I ◽

Type Iii ◽

Type V

A number of bone cell clones isolated from rat calvaria have been maintained in culture for more than 3 years. Several of these clones have undergone dramatic changes in phenotype. One of these clones, RGB 2.2, was observed originally to have a fibroblastic morphology in culture and to respond to parathyroid hormone (PTH), but not prostaglandin E2 (PGE2), with an increase in intracellular cAMP. Throughout several passages in early subcultures, these cells synthesized mostly type I collagen, with small amounts of type III and type V collagens. Whereas PTH had no detectable effect on collagen synthesis, PGE2 decreased the amount of total cell layer collagen, with the greatest effect on type III collagen, while increasing the proportion of type V collagen. Subsequent studies on these cells during 3 years in culture have indicated changes in their phenotype including a progressive change in morphology to a more cuboidal shape and a change in collagen synthesis, the cells producing large amounts of the "embryonic" collagen, α1(I) trimer. The reason(s) for the change in collagen expression is unknown, but may be the result of a change in which gene(s) is being expressed.

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PERITONEAL ADHESIONS TYPE I, III AND TOTAL COLLAGEN ON POLYPROPYLENE AND COATED POLYPROPYLENE MESHES: EXPERIMENTAL STUDY IN RATS

ABCD Arquivos Brasileiros de Cirurgia Digestiva (São Paulo) ◽

10.1590/0102-6720201700020001 ◽

2017 ◽

Vol 30 (2) ◽

pp. 77-82 ◽

Cited By ~ 2

Author(s):

Lucas Félix ROSSI ◽

Manoel Roberto Maciel TRINDADE ◽

Armando José D`ACAMPORA ◽

Luise MEURER

Keyword(s):

Type I Collagen ◽

Cell Types ◽

Type Iii Collagen ◽

Type I ◽

Abdominal Adhesions ◽

Peritoneal Adhesions ◽

Type Iii ◽

Total Collagen

ABSTRACT Background: Hernia correction is a routinely performed treatment in surgical practice. The improvement of the operative technique and available materials certainly has been a great benefit to the quality of surgical results. The insertion of prostheses for hernia correction is well-founded in the literature, and has become the standard of treatment when this type of disease is discussed. Aim: To evaluate two available prostheses: the polypropylene and polypropylene coated ones in an experimental model. Methods: Seven prostheses of each kind were inserted into Wistar rats (Ratus norvegicus albinus) in the anterior abdominal wall of the animal in direct contact with the viscera. After 90 days follow-up were analyzed the intra-abdominal adhesions, and also performed immunohistochemical evaluation and videomorphometry of the total, type I and type III collagen. Histological analysis was also performed with hematoxylin-eosin to evaluate cell types present in each mesh. Results: At 90 days the adhesions were not different among the groups (p=0.335). Total collagen likewise was not statistically different (p=0.810). Statistically there was more type III collagen in the coated polypropylene group (p=0.039) while type I was not different among the prostheses (p=0.050). The lymphocytes were statistically more present in the polypropylene group (p=0.041). Conclusion: The coated prosthesis was not different from the polypropylene one regarding the adhesion. Total and type I collagen were not different among the groups, while type III collagen was more present on the coated mesh. There was a greater number of lymphocytes on the polypropylene mesh.

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A matrix metalloproteinase-generated neoepitope of CRP can identify knee and multi-joint inflammation in osteoarthritis

Arthritis Research & Therapy ◽

10.1186/s13075-021-02610-y ◽

2021 ◽

Vol 23 (1) ◽

Author(s):

Louie C. Alexander ◽

Grant McHorse ◽

Janet L. Huebner ◽

Anne-Christine Bay-Jensen ◽

Morten A. Karsdal ◽

...

Keyword(s):

Synovial Fluid ◽

Matrix Metalloproteinase ◽

Type I Collagen ◽

Joint Inflammation ◽

Cartilage Degradation ◽

Womac Pain ◽

Type Iii Collagen ◽

Type I ◽

Radiographic Imaging ◽

Type Iii

Abstract Objective To compare C-reactive protein (CRP) and matrix metalloproteinase-generated neoepitope of CRP (CRPM) as biomarkers of inflammation and radiographic severity in patients with knee osteoarthritis. Methods Participants with symptomatic osteoarthritis (n=25) of at least one knee underwent knee radiographic imaging and radionuclide etarfolatide imaging to quantify inflammation of the knees and other appendicular joints. For purposes of statistical analysis, semi-quantitative etarfolatide and radiographic imaging scores were summed across the knees; etarfolatide scores were also summed across all joints to provide a multi-joint synovitis measure. Multiple inflammation and collagen-related biomarkers were measured by ELISA including CRP, CRPM, MMP-generated neoepitopes of type I collagen and type III collagen in serum (n=25), and CD163 in serum (n=25) and synovial fluid (n=18). Results BMI was associated with CRP (p=0.001), but not CRPM (p=0.753). Adjusting for BMI, CRP was associated with radiographic knee osteophyte score (p=0.002), while CRPM was associated with synovitis of the knee (p=0.017), synovitis of multiple joints (p=0.008), and macrophage marker CD163 in serum (p=0.009) and synovial fluid (p=0.03). CRP correlated with MMP-generated neoepitope of type I collagen in serum (p=0.045), and CRPM correlated with MMP-generated neoepitope of type III collagen in serum (p<0.0001). No biomarkers correlated with age, knee pain, or WOMAC pain. Conclusions To our knowledge, this is the first time that CRPM has been shown to be associated with knee and multi-joint inflammation based on objective imaging (etarfolatide) and biomarker (CD163) measures. These results demonstrate the capability of biomarker measurements to reflect complex biological processes and for neoepitope markers to more distinctly reflect acute processes than their precursor proteins. CRPM is a promising biomarker of local and systemic inflammation in knee OA that is associated with cartilage degradation and is independent of BMI. CRPM is a potential molecular biomarker alternative to etarfolatide imaging for quantitative assessment of joint inflammation.

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