scholarly journals The mRNAs for the three chains of human collagen type XI are widely distributed but not necessarily co-expressed: implications for homotrimeric, heterotrimeric and heterotypic collagen molecules

1995 ◽  
Vol 311 (2) ◽  
pp. 511-516 ◽  
Author(s):  
V C H Lui ◽  
R Y C Kong ◽  
J Nicholls ◽  
A N Y Cheung ◽  
K S E Cheah
Keyword(s):  
Collagen Type ◽  
Subunit Composition ◽  
Messenger Rnas ◽  
Collagen Types ◽  
Fetal Tissues ◽  
Chain Composition ◽  
Collagen Molecules ◽  
Human Collagen ◽  
Human Fetal Tissues ◽  
Cross Type

In cartilage collagen type XI exists as heterotrimeric molecules composed of alpha 1(XI), alpha 2(XI) and alpha 3(XI) subunits. Messenger RNAs for some of the alpha chains of collagen type XI have also been found in non-chondrogenic tissues but the chain composition of the molecule in these sites is not known. Some non-chondrogenic tissues also contain heterotrimers containing collagen alpha 2(V) and alpha 1(XI) chains. We have explored the possibility that collagen type XI could exist in differing trimeric forms in non-chondrogenic tissues and aimed to predict the subunit composition of this collagen in those tissues. The distribution and relative levels of expression of collagen alpha 1(XI), alpha 2(XI) and alpha 3(XI)/alpha 1(II) mRNAs in different human fetal tissues were studied. Expression of mRNAs for all three genes of collagen type XI is not restricted to cartilage but is widespread. However, in some non-chondrogenic tissues, the mRNAs for all three alpha chains of collagen type XI were not co-expressed, but collagen alpha 1(XI) and alpha 2(XI) mRNAs were found either singly or without collagen alpha 3(XI) transcripts. Collagen type XI may therefore exist as homotrimers and/or heterotrimers composed of two collagen alpha(XI) chains in some tissues. The distribution of mRNAs for collagen alpha 2(V) and alpha 1(I) were also studied. Co-expression of collagen type XI, alpha 2(V) and alpha 1(I) mRNAs was found for many tissues. These findings have implications for the possibility of additional chain associations for collagen types XI and V in cross-type heterotrimers within heterotypic fibrils.

Antibodies to Collagen Types I–VI in Dupuytren’s Contracture

1986 ◽  
Vol 11 (1) ◽  
pp. 58-60
Author(s):  
R. S. PEREIRA ◽  
C. M. BLACK ◽  
S. M. TURNER ◽  
J. D. SPENCER
Keyword(s):  
Patient Group ◽  
Blood Donor ◽  
Collagen Type ◽  
Type Ii Collagen ◽  
Dupuytren’S Contracture ◽  
Type Ii ◽  
Collagen Types ◽  
Igg Antibody ◽  
Dupuytren's Contracture ◽  
Human Collagen

Sera from 16 patients with Dupuytren’s contracture were tested for IgG and IgM antibodies to native and denatured human collagen types I, II, III, IV, V and VI. IgG antibody to at least one collagen type was found in 11/16 (69%) of these patients, compared with 27/96 (28%) normal adult blood donor controls. The prevalence of antibody to denatured type II collagen was raised, and although there was no overall increase in HLA-DR4 compared with a control population, this antibody was associated with HLA-DR4 in this patient group.

scholarly journals Human Basement Membrane Collagens do not Elicit Platelet Aggregation

1977 ◽  
Author(s):  
R. L. Trelstad ◽  
A. C. Carvalho
Keyword(s):  
Platelet Aggregation ◽  
Basement Membrane ◽  
Collagen Type ◽  
Serotonin Release ◽  
Basement Membranes ◽  
Collagen Type Iv ◽  
Collagen Types ◽  
Type Iv ◽  
Skin Collagen ◽  
Human Collagen

The immediate subendothelial connective tissue matrix consists of the basement membrane, a collagenous felt-like cell surface coat. The collagen from basement membranes has been isolated from human lung, skin, and kidney using a new fractionation method which separates native forms of collagen Types I, II, III, and IV. The Type IV collagens from the basement membranes have been characterized in respect to amino acid and carbohydrate composition, molecular size, charge and native structure. Antibodies prepared against the Type IV collagen reacted with both epithelial and vascular basement membranes as judged by immunofluorescence. Platelet-rich plasma (250,000/μl) from 5 normal subjects were tested for aggregation and 14C-serotonin release with human collagen Types I, II, III, and IV. Complete aggregation (100%) and 14C-serotonin release (80–100%) was obtained when Types I, II, and III were used. Human kidney, lung, and skin collagen Type IV (10–100μg/ml) did not aggregate platelets nor cause release of their contents. Pre-incubation of platelets and human collagen Type IV for periods of 30 minutes did not result in inhibition of platelet aggregation by Types I, II, or III.These data indicate that the collagenous component of the basement membrane, the first extra-vascular collagen to which a platelet is exposed, does not elicit aggregation as do the fibrillar collagens in the perivascular matrix.

Sequence Alignment between vWF and Peptides Inhibiting the vWF-collagen Interaction Does not Result in the Identification of a Collagen-binding Site in vWF

2000 ◽  
Vol 84 (10) ◽  
pp. 621-625 ◽  
Author(s):  
R. M. van der Plas ◽  
G. Vandecasteele ◽  
S. Vauterin ◽  
E. G. Huizinga ◽  
J. J. Sixma ◽  
...  
Keyword(s):  
Binding Site ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Binding Studies ◽  
Collagen Types ◽  
Collagen Binding ◽  
Human Collagen ◽  
Rat Tail ◽  
Calf Skin

SummaryWe previously found that two peptides (N- and Q-peptide) selected by phage display for binding to an anti-vWF antibody, were able to inhibit vWF-binding to collagen (1). The sequence of those peptides could be aligned with the sequence in vWF at position 1129-1136 just outside the A3-domain. As the peptides represent an epitope or mimotope of vWF for binding to collagen we next wanted to study whether the alignment resulted in the identification of a new collagen binding site in vWF. We mutated the 1129-1136 VWTLPDQC sequence in vWF to VATAPAAC. Expressing this mutant vWF (7.8-vWF) in a fur-BHK cell line resulted in well processed 7.8-vWF containing a normal distribution of molecular weight multimers. However, binding studies of this mutant vWF to rat tail, human and calf skin collagens type I, to human collagen types III and VI, revealed no decrease in vWF-binding to any of these collagens. Thus, although the N-and Q-peptides did inhibit the vWF-collagen interaction, the resulting alignment with the vWF sequence did not identify a collagen binding site, pointing out that alignments (although with a high percentage of identity) do not always result in identification of binding epitopes. However, suprisingly removal of the A3-domain or changing the vWF sequence at position 1129-1136 resulted in an increase of vWF-binding to human collagen type VI and to rat tail collagen type I, implying that these changes result in a different conformation of vWF with an increased binding to these collagens as a consequence.

scholarly journals Expression of mRNAs coding for the alpha 1 chain of type XIII collagen in human fetal tissues: comparison with expression of mRNAs for collagen types I, II, and III.

1989 ◽  
Vol 109 (3) ◽  
pp. 1371-1379 ◽  
Author(s):  
M Sandberg ◽  
M Tamminen ◽  
H Hirvonen ◽  
E Vuorio ◽  
T Pihlajaniemi
Keyword(s):  
Striated Muscle ◽  
Hybridization Signal ◽  
Northern Hybridization ◽  
Fibrillar Collagen ◽  
Collagen Types ◽  
Root Cells ◽  
Fetal Tissues ◽  
Type Xiii Collagen ◽  
Human Fetal Tissues

This paper describes the topographic distribution of the multiple mRNAs coding for a novel human short-chain collagen, the alpha 1 chain of type XIII collagen. To identify the tissues and cells expressing these mRNAs, human fetal tissues of 15-19 gestational wk were studied by Northern and in situ hybridizations. The distribution pattern of the type XIII collagen mRNAs was compared with that of fibrillar collagen types I, II, and III using specific human cDNA probes for each collagen type. Northern hybridization showed the bone, cartilage, intestine, skin, and striated muscle to contain mRNAs for type XIII collagen. An intense in situ hybridization signal was obtained with the type XIII collagen cDNAs in the epidermis, hair follicles, and nail root cells of the skin, whereas the fibrillar collagen mRNAs were detected in the dermis. Cells in the intestinal mucosal layer also appeared to contain high levels of alpha 1(XIII) collagen mRNAs, but contained none of the fibrillar collagen mRNAs. In the bone and striated muscle, alpha 1(XIII) collagen mRNAs were detected in the mesenchymal cells forming the reticulin fibers of the bone marrow and endomycium. The hybridization signal obtained with the alpha 1(XIII) collagen cDNA probe in cartilaginous areas of the growth plates was similar, but less intense, to that obtained with the type II collagen probe. A clear hybridization signal was also detected at the (pre)articular surfaces and at the margins of the epiphyses, whereas it was weaker in the resting chondrocytes in the middle of the epiphyses. The brain, heart, kidney, liver, lung, placenta, spleen, testis, tendon, and thymus did not appear to contain alpha 1(XIII) collagen mRNAs.

Isolation of Nuclear Fractions from Human Fetal Tissues

Pharmacology ◽  
1985 ◽  
Vol 30 (4) ◽  
pp. 188-196 ◽  
Author(s):  
G.M. Pacifici ◽  
H. Glaumann ◽  
A. Rane°
Keyword(s):  
Fetal Tissues ◽  
Human Fetal Tissues

scholarly journals Plant Recombinant Human Collagen Type I Hydrogels for Corneal Regeneration

2021 ◽  
Author(s):  
Michel Haagdorens ◽  
Elle Edin ◽  
Per Fagerholm ◽  
Marc Groleau ◽  
Zvi Shtein ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Fibrils ◽  
Type I ◽  
Safe Alternative ◽  
Human Donor ◽  
Human Collagen ◽  
Donor Corneas

Abstract Purpose To determine feasibility of plant-derived recombinant human collagen type I (RHCI) for use in corneal regenerative implants Methods RHCI was crosslinked with 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) to form hydrogels. Application of shear force to liquid crystalline RHCI aligned the collagen fibrils. Both aligned and random hydrogels were evaluated for mechanical and optical properties, as well as in vitro biocompatibility. Further evaluation was performed in vivo by subcutaneous implantation in rats and corneal implantation in Göttingen minipigs. Results Spontaneous crosslinking of randomly aligned RHCI (rRHCI) formed robust, transparent hydrogels that were sufficient for implantation. Aligning the RHCI (aRHCI) resulted in thicker collagen fibrils forming an opaque hydrogel with insufficient transverse mechanical strength for surgical manipulation. rRHCI showed minimal inflammation when implanted subcutaneously in rats. The corneal implants in minipigs showed that rRHCI hydrogels promoted regeneration of corneal epithelium, stroma, and nerves; some myofibroblasts were seen in the regenerated neo-corneas. Conclusion Plant-derived RHCI was used to fabricate a hydrogel that is transparent, mechanically stable, and biocompatible when grafted as corneal implants in minipigs. Plant-derived collagen is determined to be a safe alternative to allografts, animal collagens, or yeast-derived recombinant human collagen for tissue engineering applications. The main advantage is that unlike donor corneas or yeast-produced collagen, the RHCI supply is potentially unlimited due to the high yields of this production method. Lay Summary A severe shortage of human-donor corneas for transplantation has led scientists to develop synthetic alternatives. Here, recombinant human collagen type I made of tobacco plants through genetic engineering was tested for use in making corneal implants. We made strong, transparent hydrogels that were tested by implanting subcutaneously in rats and in the corneas of minipigs. We showed that the plant collagen was biocompatible and was able to stably regenerate the corneas of minipigs comparable to yeast-produced recombinant collagen that we previously tested in clinical trials. The advantage of the plant collagen is that the supply is potentially limitless.

Maternal microchimerism in human fetal tissues

2008 ◽  
Vol 198 (3) ◽  
pp. 325.e1-325.e6 ◽  
Author(s):  
Anna Maria Jonsson ◽  
Mehmet Uzunel ◽  
Cecilia Götherström ◽  
Nikos Papadogiannakis ◽  
Magnus Westgren
Keyword(s):  
Fetal Tissues ◽  
Human Fetal Tissues

Immunohistochemical localization of dehydroepiandrosterone sulfotransferase in human fetal tissues.

1994 ◽  
Vol 78 (1) ◽  
pp. 234-236
Author(s):  
C R Parker ◽  
C N Falany ◽  
C R Stockard ◽  
A K Stankovic ◽  
W E Grizzle
Keyword(s):  
Immunohistochemical Localization ◽  
Fetal Tissues ◽  
Human Fetal Tissues

Specificity and T cell receptor β chain usage of a human collagen type II-reactive T cell clone derived from a healthy individual

1992 ◽  
Vol 22 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Tan Yan ◽  
Harald Burkhardt ◽  
Thomas Ritter ◽  
Barbara Bröker ◽  
Karl Heinz Mann ◽  
...  
Keyword(s):  
T Cell ◽  
T Cell Receptor ◽  
Collagen Type ◽  
Cell Clone ◽  
Cell Receptor ◽  
Type Ii ◽  
Collagen Type Ii ◽  
T Cell Clone ◽  
Human Collagen ◽  
Β Chain
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