Specific immunohistochemical localization of Type I collagen in porcine periodontal tissues using the peroxidase-labelled antibody technique

1979 ◽  
Vol 11 (1) ◽  
pp. 73-82 ◽  
Author(s):  
L. G. Rao ◽  
H. M. Wang ◽  
R. Kalliecharan ◽  
J. N. M. Heersche ◽  
J. Sodek
Keyword(s):  
Type I Collagen ◽  
Immunohistochemical Localization ◽  
Type I ◽  
Antibody Technique ◽  
Periodontal Tissues

scholarly journals Specific immunohistochemical localization of type III collagen in porcine periodontal tissues using the peroxidase-antiperoxidase method.

1980 ◽  
Vol 28 (11) ◽  
pp. 1215-1223 ◽  
Author(s):  
H M Wang ◽  
V Nanda ◽  
L G Rao ◽  
A H Melcher ◽  
J N Heersche ◽  
...  
Keyword(s):  
Bone Tissue ◽  
Type I Collagen ◽  
Alveolar Bone ◽  
Immunohistochemical Localization ◽  
Type Iii Collagen ◽  
Type I ◽  
Connective Tissues ◽  
Type Iii ◽  
Dental Tissues ◽  
Periodontal Tissues

Specific antibodies to porcine gingival type III collagen were raised in sheep. After purification on collagen affinity columns the antibodies were used for immunohistochemical localization of type III collagen in porcine periodontal and dental tissues employing the peroxidase-antiperoxidase (PAP) procedure. The extent of staining of the periodontal tissues was found to approximate the amount of type III collagen measured biochemically. A fairly uniform distribution of type III collagen was observed in the periodontal ligament and gingiva with more intense staining often being associated with blood vessels. A regular pattern of weakly staining fibers could be demonstrated throughout the cementum and in parts of the alveolar bone tissue. In addition, occasional sites in the cementum having a different morphological appearance from the rest of the cementum exhibited bundles of positively stained fibers. Although the bone tissue was essentially unstained, fibers in the endosteal spaces stained strongly. Sharpey's fibers passing from the soft connective tissues into alveolar bone and cementum also stained strongly. Three distinct arrangements of collagen fibers stained by the type III collagen antibodies could be identified: first, a reticular pattern, which was seen at the junction of the gingival epithelium and connective tissue, and in the endosteal spaces and dental pulp; second, a more diffuse pattern of fibers intermingled with type I collagen in the soft connective tissues; and third, a coating of some Sharpey's fibers, having a core believed to be type I collagen, and of fibers in the cementum inclusions.

scholarly journals Coronally Repositioned Flap with Bioresorbable Collagen Membrane for Miller’s Class I and II Recession Defects: A Case Series

2019 ◽  
Vol 28 (5) ◽  
pp. 477-480
Author(s):  
Mrinalini Agarwal ◽  
Deepa Dhruvakumar
Keyword(s):  
Type I Collagen ◽  
Case Series ◽  
Gingival Recession ◽  
Class I ◽  
Collagen Membrane ◽  
Type I ◽  
Root Coverage ◽  
Periodontal Tissues ◽  
Keratinized Tissue ◽  
Attached Gingiva

Objective: Gingival recession is one of the most common esthetic and functional concerns associated with periodontal tissues. Several techniques have been described to cover the exposed root surface. The aim of the present study was to evaluate the efficacy of recession coverage using a coronally repositioned flap in conjunction with a bioresorbable collagen membrane. Methods: Eight non-smoking healthy subjects with Miller’s Class I and II recession defects in the maxillary anterior region were selected. Recession was treated by a coronally repositioned flap along with a bioresorbable type I collagen guided tissue regeneration membrane (Periocol®). Clinical parameters recorded were recession depth, recession width, width of keratinized tissue, and width of the attached gingiva at baseline and 3 months postoperatively. Results: Three-month postoperative measurements demonstrated significant root coverage and a reduction in the recession depth and width. In addition, there was a significant increase in the width of keratinized tissue and of the attached gingiva. Conclusion: Recession coverage with a coronally repositioned and bioresorbable collagen membrane demonstrated good results in terms of root coverage as well as increase in the width of keratinized tissue.

Collagen fibrillogenesis in vitro: interaction of types I and V collagen

1986 ◽  
Vol 44 ◽  
pp. 210-211
Author(s):  
Arthur J. Wasserman ◽  
Kathy C. Kloos ◽  
David E. Birk
Keyword(s):  
Type I Collagen ◽  
Corneal Stroma ◽  
Minor Component ◽  
Homogeneous Distribution ◽  
Type I ◽  
Type V Collagen ◽  
Fibril Morphology ◽  
Type V ◽  
In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

948: Clinical Safety, Histologic Findings and Surgical Methods in Complex Phalloplasty Using Type I Collagen

2007 ◽  
Vol 177 (4S) ◽  
pp. 314-314 ◽  
Author(s):  
Joon-Yang Kim ◽  
Hoon Seog Jean ◽  
Beom Joon Kim ◽  
Kye Yong Song
Keyword(s):  
Type I Collagen ◽  
Type I ◽  
Clinical Safety ◽  
Surgical Methods
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