2 edition of Type IV collagen in development and disease found in the catalog.
Type IV collagen in development and disease
Scott Jon Harvey
Written in English
X-linked Alport syndrome (XLAS) is a disorder characterized by nephropathy and deafness that is caused by mutations in the COL4A5 gene, which encodes the alpha5(IV) collagen chain. A canine model of XLAS was studied to elucidate the pathogenesis of this disease in humans and to establish the feasibility of gene therapy for its treatment. The temporal and spatial expression of the alpha1(IV)--alpha6(IV) chains in basement membranes (BMs) of the kidney, inner ear and testis was documented and correlated to normal and pathologic changes in BM ultrastructure and function. The loss of the alpha3(IV), alpha4(IV) and alpha6(IV) chains from all BMs in affected dogs stems from a failure at the level of protein assembly, and is permissive to normal development in all tissues studied. In affected kidney, the alpha1(IV) and alpha2(IV) chains are sufficient for normal glomerular structure and function on a short-term basis, but not for their long-term maintenance. In normal inner ear, changes in the distribution of the alpha3(IV)--alpha5(IV) chains occurred co-incident with, but were not required for the acquisition of mature auditory function, and their localization led to a new theory on the etiology of deafness in XLAS. In affected testis, the absence of the alpha3(IV)--alpha6(IV) chains leads to structural changes of the seminiferous tubule BM that impairs, but does not prevent normal function. A cDNA encoding canine alpha5(IV) collagen was cloned and expressed in vitro in 293 cells. By Northern blotting, an alpha5(IV) mRNA transcript of ∼5.2 kb was expressed and the recombinant protein was detected by immunocytochemistry. The alpha5(IV) chain was secreted as a ∼190 kDa monomer that did not form homotrimers, nor heterotrimers with the endogenous alpha1(IV) or alpha2(IV) chains, a finding consistent with its requirement for the alpha3(IV) and alpha4(IV), or alpha6(IV) chains for triple helical assembly. An adenoviral vector for the alpha5(IV) chain was used to express the transgene in smooth muscle of affected dogs, which lacks the alpha5(IV) and alpha6(IV) chains. Expression of the alpha5(IV) transgene rescued expression of the alpha6(IV) chain and both assumed a BM distribution. This finding provides "proof of principle" that gene therapy for XLAS may be feasible.
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OA is quite common in companion animals, especially in large breed dogs and horses. Collagen, the most abundant protein of mammals, has specific connective tissue types for skin, bones, reticulate, basal lamina, bones, cell surfaces, while type II collagen (UC-II) forms the main structure of cartilage tissue. Even at the smaller dosages, UC-II has also been reported to be more effective than. Type III collagen is found in the walls of arteries and other hollow organs and usually occurs in the same fibril with type I collagen. Type IV forms the bases of cell basement membrane.
Collagen type VI-related disorders encompass two genetic muscle disorders formerly thought to be separate entities: Bethlem myopathy and Ullrich congenital muscular dystrophy. Researchers have determined that these disorders represent a disease spectrum associated with disruptions or changes (mutations) in genes that contain instructions to. To generate clumps appropriate for passaging, both enzymatic and mechanical (by dissection or scraping) methods can be used. Collagenase Type IV is an enzyme that is routinely used at 1 mg/mL for the generation of human ES cell and iPS cell clumps for passaging.
The immunoassay for quantitation of type IV collagen used type IV collagen purified from human placenta (Collaborative Biomedical Products, Bedford, MA) and rabbit anti-human type IV collagen antibody (Biodesign, Kennebunk, ME), according to previously described methodology. The antigen was coated onto plastic microtiter wells ( ng/well) in. Type III collagen is a fibrillar forming collagen comprising three α1(III) chains and is expressed in early embryos and throughout embryogenesis. In the adult, type III collagen is a major component of the extracellular matrix in a variety of internal organs and skin. Mutations in the COL3A1 gene have been implicated as a cause of type IV Ehlers–Danlos syndrome, a disease leading to aortic.
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Type IV collagen is the target of two autoimmune diseases affecting the kidney: Goodpasture syndrome and Alport posttransplantation disease. Both diseases are characterized by autoantibodies attacking the glomerular basement membrane and causing rapidly progressive glomerulonephritis Cited by: 3.
Type IV collagen is the main collagen component of the basement membrane. It is a network-forming collagen that underlies epithelial and endothelial cells and functions as a barrier between tissue compartments.
Type IV collagen has many binding partners and forms the backbone of the basement membrane. A new genome-wide association study of patients with type 1 diabetes mellitus reveals novel loci that are associated with the development of diabetic kidney disease.
The most significant of Author: Jeffrey H. Miner. Collagen IV (ColIV or Col4) is a type of collagen found primarily in the basal lamina. The collagen IV C4 domain at the C-terminus is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel.
Also, collagen IV lacks the regular glycine in every third residue necessary for the tight, collagen helix. This makes the overall arrangement more sloppy with kinks. This Collagen Type IV product is generated by human fibroblasts and epithelial cells in a co-culture system, which produces an ECM in vitro.
The Collagen Type IV is then purified biochemically. It is sterilized by dialysis in an acetic acid and % chloroform solution, Type IV collagen in development and disease book is supplied sterile at a concentration of ∼ mg/ml in 25% acetic acid.
The most abundant molecule of type IV collagen is the heterotrimer [α1(IV)]2 β2(IV), which is found in all basement membranes. There are 6 genes, COL 4A1 through COL4A6, located on 3 different chromosomes (13q34, 2q, Xq22) responsible for producing type IV collagen. Collagen type I comprises approximately 70% of collagen in the skin, with type III being 10%, and trace amounts of collagen type IV, V, VI and VII (Uitto et al, ; Hay, ).
8 Protein. Type-IV collagen related diseases. Pescucci C(1), Longo I, Bruttini M, Mari F, Renieri A. Author information: (1)Medical Genetics, Department of Molecular Biology, Policlinico Le Scotte, University of Siena, Viale Bracci 2, Siena, Italy.
Type IV collagen is a type of collagen found primarily in the skin within the basement membrane zone.
The type IV collagen C4 domain at the C-terminus is not removed in post-translational. A final outlook indicates the importance of different collagen types not only for the understanding of collagen-related diseases, but also as a basis for the therapeutical use of members of this protein family discussed in other chapters of this Collagen type IV—the collagen of basement membranes 4.
Biosynthesis of collagens. Basement membranes are composed of highly complex arrays of ∼50 glycoproteins. 1 Type IV collagen, along with laminin, plays an important role in cell adhesion, migration, differentiation, and growth.
12 In this regard, degradation of type IV collagen can occur under both physiological and pathological conditions. 1 Type IV collagen degradation products also play an important role during.
• Collagen I: skin, tendon, vascular ligature, organs, bone (main component of the organic part of bone) • Collagen II: cartilage (main component of cartilage) • Collagen III: reticulate (main component of reticular fibers), commonly found alongside type I. • Collagen IV: forms basal lamina, the epithelium-secreted layer of the basement membrane.
• Collagen V: cell surfaces, hair and placentaFile Size: 90KB. We investigated the collagen turnover profile of 81 non-dialysis CKD stage 2–5 patients by measuring peptides reflecting formation and degradation of collagen type (COL) I, III, IV, and VI.
Collagen alpha-4(IV) chain is a protein that in humans is encoded by the COL4A4 gene. This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. This particular collagen IV subunit, however, is.
The ultrafiltration function of the glomerular basement membrane (GBM) of the kidney is impaired in genetic and acquired diseases that affect type IV collagen. The GBM is composed of five (α1 to α5) of the six chains of type IV collagen, organized into an α1α2(IV) and an α3α4α5(IV) network.
Predominant collagen present in cementum is type I collagen (forms 90% of the organic matrix). Other collagens associated with cementum include type III, a less cross-linked collagen found in high concentrations during development, repair, and regeneration of mineralized tissues and type XII that binds to type I collagen and to non-collagenous.
Type IV Collagen Disorders: Alport syndrome and Goodpasture’s syndrome is caused by a mutation in collagen type IV. Type IV collagen is found in the eye lens and also as part of the filtration system in capillaries.
Mutations occur in the genes COL4A1, COL4A2, COL4A3, COL4A4, COL4A5, and COL4A6. COL4A1 (collagen type IV α 1 chain) related disorder is associated with pulmonary complication.
This gene is a major constituent required in basal membrane stability. Mutations in COL4A1 result in familial porencephaly, infantile hemiplegia, cerebral small vessel disease (CSVD) and hemorrhagic stroke.
This IV was formulated to provide the key ingredients in the formation of skin’s most important components: collagen and elastin.
It includes amino acids like l-proline, l-lysine, and l-glycine; minerals such as manganese, magnesium and zinc; and even powerful antioxidants like vitamin C and glutathione. CHARACTERIZATION OF TYPE I AND TYPE III COLLAGENS IN HUMAN TISSUES MICHAELA BODE Academic Dissertation to be presented with the assent of the Facu lty of Med icine, University of Oulu, for public discussion in Auditorium 9 of the Univ ersity Hospital of Oulu, on April 7th,at 12 noon.
Basement membranes are assembled through an interweaving of type IV collagen with laminins, nidogen and sulphated proteoglycans.
COL4A1 to COL4A6 are the genes encoding the six existing α (IV) chains which are expressed in different membranes at different stages of embryonic development.Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation.The COL4A1 gene provides instructions for making one component of type IV collagen, which is a flexible protein important in the structure of many tissues throughout the body.
Specifically, this gene makes the alpha1(IV) chain of type IV collagen. This chain combines with another alpha1 chain and a different type of alpha (IV) chain called alpha2 to make a complete type IV collagen alpha