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Collagen types and fibronectin in the uterine muscle of normal and hypertensive Pulkkinen MO, Lehto M, Jalkanen M, Näntö-Salonen K.Specimens from the uterine wall were obtained from 16 patients at 31 to 40 weeks of pregnancy: 10 underwent surgical procedures for a hypertensive disorder and six for abnormality of the birth canal or faulty presentation. Collagen types I, III, and V and fibronectin antibodies were used for immunohistologic studies. Collagen types I and V were located mainly around single cells, but type III and fibronectin were found mainly around cell bundles. Collagenous structures in the uterine muscle of patients with hypertensive disorder in pregnancy were torn. Abundant fibronectin fluorescence was detected in the lobuli within the disrupted tissue.
Disruption of the uterine structure correlated with the amount Factors influencing the properties of reconstituted collagen fibers prior to self-assembly: animal species and collagen extraction method.This research work allows a direct comparison between collagen solutions of equal concentration derived from the two widely used collagen sources: bovine Achilles tendon (BAT) and rat tail tendon (RTT), and extraction methods: acid (AS) and pepsin (PS) solubilization on the properties of extruded collagen fibers. Scanning electron microscopy revealed that the substructure of the collagen fibers was the same independent of the treatment. Transmission electron microscopy revealed that the AS collagen-derived fibers were comprised of thick quarter-staggered fibrils, while the coexistence of thin nonbanded and thick banded fibrils was apparent for the PS collagen-derived fibers. The BAT-derived fibers demonstrated higher denaturation temperature than the RTT-derived ones (p < 05). The extraction method had no influence on the thermal characteristics of the fibers produced (p > 05). ASBAT collagen was of higher viscosity than both ASRTT and PSBAT (p < 002), and therefore larger diameter fibers were obtained (p < 001).
An inversely proportional relationship between dry-fiber diameter and stress at break was observed within the treatments. The PS yielded 10 times more soluble collagen from BAT and the derived fibers were of similar tensile strength, stiffness, and elongation (p > 05) as those derived from the AS collagen. No significant difference was observed for the stress at break for the ASBAT and the ASRTT, while significant difference was observed for the elongation and modulus values (p < 005). Seebio supplements collagen , reconstituted collagen fibers were produced with properties similar to native or synthetic fibers to suit a wide range of tissue engineering applications.Imaging Collagen in Scar Tissue: Developments in Second Harmonic Generation Microscopy for Biomedical Applications.British Columbia, Vancouver, BC V6Z 1Y6, Canada. The ability to respond to injury with tissue repair is a fundamental property of all multicellular organisms.
The extracellular matrix (ECM), composed of fibrillar collagens as well as a number of other components is dis-regulated during repair in many organs. In many tissues, scaring results when the balance is lost between ECM synthesis and degradation. Investigating what disrupts this balance and what effect this can have on tissue function remains an active area of research. Recent advances in the imaging of fibrillar collagen using second harmonic generation (SHG) imaging have proven useful in enhancing our understanding of the supramolecular changes that occur during scar formation and disease progression. Here, we review the physical properties of SHG, and the current nonlinear optical microscopy imaging (NLOM) systems that are used for SHG imaging. We provide an extensive review of studies that have used SHG in skin, lung, cardiovascular, tendon and ligaments, and eye tissue to understand alterations in fibrillar collagens in scar tissue. Lastly, we review the current methods of image analysis that are used to extract important information about the role of fibrillar collagens in scar formation.
Conflict of interest statement: The authors have no conflicts of interest.Type VI collagen and glycoprotein MFPI are distinct components of the Ayad S, Chambers CA, Berry L, Shuttleworth CA, Grant ME.Two collagenous glycoproteins, Mr 140,000 and Mr 150,000, are synthesized and secreted into the medium of cultured fibroblasts. The glycoprotein of Mr 140,000 is identical with the 140K(VI) component of type VI collagen by both immunological and physicochemical criteria. benefits of collagen of Mr 150,000 is immunologically distinct and exhibits the physicochemical characteristics of the putative elastic microfibrillar glycoprotein MFPI.Study of the noncollagenous components of the periodontium.Periodontal ligament and gingivae of bovine and porcine periodontium were analyzed for relative amounts of carbohydrates, collagen, and acid mucopolysaccharides.
The sugar content was 3% and 3% of dry weight in bovine and porcine periodontal ligament, respectively. The values were lower in the gingivae being 24% and 20%, respectively. Approximately 50% of hexosamine in gingivae was present in acid mucopolysacchrides as compared to 36% in periodontal ligament.
