A tailored extracellular matrix (ECM) - Mimetic coating for cardiovascular stents by stepwise assembly of hyaluronic acid and recombinant human type III collagen

Biomaterials ◽  
2021 ◽  
pp. 121055
Author(s):  
Li Yang ◽  
Haoshuang Wu ◽  
Lu Lu ◽  
Qing He ◽  
Boting Xi ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hyaluronic Acid ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Cardiovascular Stents ◽  
Human Type ◽  
Stepwise Assembly

scholarly journals Abnormal type III collagen produced by an exon-17-skipping mutation of the COL3A1 gene in Ehlers-Danlos syndrome type IV is not incorporated into the extracellular matrix

1995 ◽  
Vol 311 (3) ◽  
pp. 939-943 ◽  
Author(s):  
A A Chiodo ◽  
D O Sillence ◽  
W G Cole ◽  
J F Bateman
Keyword(s):  
Extracellular Matrix ◽  
Triple Helix ◽  
Type Iii Collagen ◽  
Syndrome Type ◽  
Ehlers Danlos Syndrome ◽  
Type Iii ◽  
Type Iv ◽  
Col3a1 Gene ◽  
Collagen Molecules ◽  
Danlos Syndrome

A novel heterozygous mutation of the COL3A1 gene that encodes the alpha 1(III) chains of type III collagen was identified in a family with the acrogeric form of Ehlers-Danlos syndrome type IV (EDS-IV). Cultured dermal fibroblasts produced normal and shortened alpha 1(III) chains. The triple helix of the latter chain was shortened owing to a 33 amino acid deletion of Gly-184 to Pro-216. The corresponding region of cDNA lacked 99 base pairs from nucleotides 1051 to 1149. The deletions corresponded exactly to the normal sequence encoded by exon 17 of the COL3A1 gene. The proband was heterozygous for a T to G transversion at position +2 of intron 17, which resulted in skipping of exon 17. The splicing defect was not corrected by growing the fibroblasts at 33 degrees C and no other splicing variants were identified at 33 or 37 degrees C. The affected brother had the same mutation but his unaffected mother did not. Heterotrimeric type III collagen molecules containing normal and mutant chains were retained within the cell. The mutant homotrimeric molecules were modified and secreted normally and were thermally stable. These normal characteristics of the mutant homotrimers suggested that the loss of ten Gly-Xaa-Yaa triplets (where Gly-Xaa-Yaa is a repetitive amino acid triplet structure in which Xaa and Yaa are other amino acids, proline and hydroxyproline being more common in the Yaa position) did not adversely affect the formation and stability of the triple helix or the structural requirements for secretion. However, the mutant homotrimers were not incorporated into the extracellular matrix of an in vitro model of EDS-IV dermis. The EDS-IV phenotype in this family was probably due to a deficiency in the amount of normal type III collagen available for formation of the heterotypic collagen fibrils of the extracellular matrix. Intracellular and extracellular quality-control mechanisms prevented the incorporation of heterotrimeric and homotrimeric mutant type III collagen molecules into the cross-linked extracellular matrix.

scholarly journals Characterization of Human Type III Collagen Expressed in a Baculovirus System

1996 ◽  
Vol 271 (20) ◽  
pp. 11988-11995 ◽  
Author(s):  
Arja Lamberg ◽  
Tarja Helaakoski ◽  
Johanna Myllyharju ◽  
Sirkku Peltonen ◽  
Holger Notbohm ◽  
...  
Keyword(s):  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type ◽  
Baculovirus System

scholarly journals Production and characterization of a monoclonal antibody to human type III collagen.

1986 ◽  
Vol 34 (8) ◽  
pp. 1003-1011 ◽  
Author(s):  
E J Macarak ◽  
P S Howard ◽  
E T Lally
Keyword(s):  
Monoclonal Antibody ◽  
Lymph Node ◽  
Staining Pattern ◽  
Immunohistochemical Localization ◽  
White Pulp ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Human Type ◽  
New Information

Human type III collagen from placenta was isolated and purified for use as an immunogen. A monoclonal antibody was produced which specifically recognizes epitopes unique to type III collagen. The specificity of the antibody was determined by inhibition ELISA, an immunoblot assay, and by immunoprecipitation. Results indicated that the monoclonal antibody recognized only the alpha 1(III) polypeptide chains and did not crossreact with type I, IV, or V collagen. The monoclonal antibody was also used for immunohistochemical localization of type III collagen in tissue sections of human placenta, bovine spleen, and lymph node. In placenta, both large and small blood vessels showed pronounced staining of the tunica media, which contains largely smooth muscle cells, known to synthesize type III collagen. In contrast, the intimal areas and endothelial cells showed no staining with the antibody. In the placental villi, staining was limited to the villous core, where fine fibrillar structures showed strong staining. In lymph nodes, the capsule and pericapsular adipose cells were surrounded by a covering of type III collagen. Within the parenchyma of the node, staining was localized to a branching, reticular array of fine fibers. In the spleen, staining was pronounced in the capsule, splenic trabeculae, and white pulp, where blood vessel staining was especially prominent. The red pulp and splenic sinuses contain little or no type III collagen. The fine network-like or reticular staining pattern found in the lymph node parenchyma is consistent with the staining pattern of the protein reticulin, and suggests that type III collagen may be closely associated with reticulin in certain tissues. Since the role of type III in tissues is unclear, this reagent will be useful in providing new information in this regard.

scholarly journals Crystal Structure of Human Type III Collagen Gly991–Gly1032Cystine Knot-containing Peptide Shows Both 7/2 and 10/3 Triple Helical Symmetries

2008 ◽  
Vol 283 (47) ◽  
pp. 32580-32589 ◽  
Author(s):  
Sergei P. Boudko ◽  
Jürgen Engel ◽  
Kenji Okuyama ◽  
Kazunori Mizuno ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type

scholarly journals Identification of the epitope for a monoclonal antibody that blocks platelet aggregation induced by type III collagen

1997 ◽  
Vol 323 (1) ◽  
pp. 45-49 ◽  
Author(s):  
Veronica GLATTAUER ◽  
Jerome A. WERKMEISTER ◽  
Alan KIRKPATRICK ◽  
John A. M. RAMSHAW
Keyword(s):  
Monoclonal Antibody ◽  
Platelet Aggregation ◽  
Type Iii Collagen ◽  
Inhibit Platelet Aggregation ◽  
Inhibitory Antibody ◽  
Type Iii ◽  
Human Type ◽  
Letter Code ◽  
The One ◽  
Α2β1 Integrin

A library of eight conformation-dependent monoclonal antibodies that react with distinct epitopes on native human type III collagen has been examined for the ability of these antibodies to inhibit platelet aggregation induced by this collagen. Six of these antibodies had no effects; one, 1E7-D7/Col3, delayed the onset and slowed the rate of platelet aggregation, while another, 2G8-B1/Col3, completely inhibited aggregation. In order to identify the epitope recognized by this inhibitory antibody, a series of peptides that could fold to form triple-helical fragments was examined. Each peptide included six Gly-Xaa-Yaa triplets from the human type III collagen sequence, where Xaa and Yaa represent the particular amino acids in the sequence, and a C-terminal (Gly-Pro-Hyp)4 sequence to enhance triple-helical stability. Using these peptides we have identified the epitope as a nine-amino-acid sequence, GLAGAOGLR (where O is the one-letter code for 4-hydroxyproline), starting at position 520 in the human type III collagen helical domain. This sequence is proximal to the site proposed for the interaction of type III collagen with α2β1-integrin of platelets.

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 Evaluation of the Biological Behavior of Mucograft® in Human Gingival Fibroblasts: An In Vitro Study

2015 ◽  
Vol 26 (6) ◽  
pp. 602-606 ◽  
Author(s):  
Rafaela S. R. e Lima ◽  
Daiane C. Peruzzo ◽  
Marcelo H. Napimoga ◽  
Eduardo Saba-Chujfi ◽  
Silvio Antonio dos Santos-Pereira ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
In Vitro Study ◽  
Vitro Study ◽  
Human Gingival Fibroblasts ◽  
Soft Tissue Augmentation ◽  
Biological Behavior ◽  
Type Iii Collagen ◽  
Gingival Fibroblasts ◽  
Type Iii

Mucograft(r) is a resorbing porcine matrix composed of type I and type III collagen, used for soft tissue augmentation in guided tissue bony regeneration procedures. This in vitro study aimed to evaluate the biological behavior of Mucograft(r) in human gingival fibroblasts, as well as the ability of the matrix to induce production of extracellular matrix. Six resorbing Mucograft(r) matrices (MCG) were cut into 3 x 2 mm rectangles and 5 x 5 mm squares and were placed in 96- and 24-well plates, respectively. The control group (CTRL) consisted of cells plated on polystyrene without the MCG. After one, two, three and seven days, cell proliferation and viability were assessed using the Trypan exclusion method and MTT test, respectively. Type III collagen (COL 3A1) and vimentin (VIM) expression were also evaluated at 10 and 14 days, using Western blotting. Statistical analysis, using ANOVA with post hoc Bonferroni test, revealed that human gingival fibroblasts from MCG showed similar results (p>0.05) for proliferation and viability as the cells cultured on CTRL. After 14 days, a significant decrease in COL 3A1 expression (p<0.05) was observed when cultured with the MCG. VIM expression showed no significant difference at any time period (p>0.05). Although no increase in extracellular matrix secretion was observed in this in vitro study, Mucograft(r) presented cellular compatibility, being an option for a scaffold whenever it is required.

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