Molecular Packing in Network-Forming Collagens

Knupp, Carlo; Squire, John M.

doi:10.1100/tsw.2003.40

Cited by 20 publications

(17 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Collagen VIII and X are separately involved in the constitution of hexagonal lattice layers in Descemet's membrane, a specialized layer between endothelial cells and the stroma, and in cartilage growth plate, respectively (Sawada et al ., ; Kwan et al ., ; Khoshnoodi et al ., ). Type VI collagen forms tetramers resulting in a more complex association to create ‘beaded filaments’ that are associated with various connective tissues including type II fibrils in cartilage and type I fibrils in tendons (Baldock et al ., ; Knupp & Squire, ; Guilak et al ., ; Izu et al ., ). Among the variety of structures collagens form, four members of the collagen family are found at the surface of cells as transmembrane proteins.…”

Section: Structure Function and Distribution Of Collagenmentioning

confidence: 99%

“…Uro‐epithelial cells express Ln isoforms composed of α1, α3, α5, β1, β2, β3, γ1 and γ2 chains, while stromal cells express α1, α2, α4, α5, β1, β2 and γ1 chains (Table S1) (Hattori et al ., ). Collagen type IV is also present in the BM underlying the urogenital epithelium and the bladder epithelium (Knupp & Squire, ). The collagen protein family is largely present in adult skin in quantity and in variety.…”

Section: Urogenital and Skin Pathogens Also Interact With Ln And Collmentioning

confidence: 99%

See 1 more Smart Citation

Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

et al. 2012

View full text Add to dashboard Cite

Laminin (Ln) and collagen are multifunctional glycoproteins that play an important role in cellular morphogenesis, cell signalling, tissue repair and cell migration. These proteins are ubiquitously present in tissues as a part of the basement membrane (BM), constitute a protective layer around blood capillaries and are included in the extracellular matrix (ECM). As a component of BMs, both Lns and collagen(s), thus function as major mechanical containment molecules that protect tissues from pathogens. Invasive pathogens breach the basal lamina and degrade ECM proteins of interstitial spaces and connective tissues using various ECM-degrading proteases or surface-bound plasminogen and matrix metalloproteinases recruited from the host. Most pathogens associated with the respiratory, gastrointestinal, or urogenital tracts, as well as with the central nervous system or the skin, have the capacity to bind and degrade Lns and collagen(s) in order to adhere to and invade host tissues. In this review, we focus on the adaptability of various pathogens to utilize these ECM proteins as enhancers for adhesion to host tissues or as a targets for degradation in order to breach the cellular barriers. The major pathogens discussed are Streptococcus, Staphylococcus, Pseudomonas, Salmonella, Yersinia, Treponema, Mycobacterium, Clostridium, Listeria, Porphyromonas and Haemophilus; Candida, Aspergillus, Pneumocystis, Cryptococcus and Coccidioides; Acanthamoeba, Trypanosoma and Trichomonas; retrovirus and papilloma virus.

show abstract

Section: Structure Function and Distribution Of Collagenmentioning

confidence: 99%

Section: Urogenital and Skin Pathogens Also Interact With Ln And Collmentioning

confidence: 99%

Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

et al. 2012

View full text Add to dashboard Cite

show abstract

“…Type I, II, III, V and XI collagens are mostly found in connective tissues, skins, cartilages and bones (Rama and Chandrakasan ; van der Rest and Garrone ; Xu and Shen ; Wei et al . ) whereas type IV, VI, VIII, X and dogfish egg case collagens belong to the network‐forming family (Knupp and Squire ).…”

Section: Introductionmentioning

confidence: 99%

Thermal Stability of Chicken Keel Bone Collagen

Losso

Ogawa

2013

Journal of Food Biochemistry

View full text Add to dashboard Cite

Acid‐soluble and pepsin‐solubilized collagen were isolated from chicken keel bone and analyzed by electrophoresis and circular dichroism. The denaturation temperature of chicken keel bone was determined by circular dichroism and compared to denaturation temperature of black drum or alligator bone. Our results show that collagen from chicken keel bone is a mixture of type II and type I, has predominantly the amino acids glycine, proline and hydroxyproline, and its secondary structure is predominantly triple‐helix. The onset of the denaturation temperature is 37C; at 44C, 50% of the collagen is denatured and the denaturation is complete at 48.8C making it the highest of vertebrate collagen denaturation temperatures reported in the literature. The high heat stability of chicken keel bone collagen may be in part ascribed to its imino acid content. Because of the high heat stability and low methionine content, chicken keel bone collagen is a high value‐added product with several biochemical and biomedical applications. Practical Applications The denaturation temperature of chicken keel bone collagen is above body temperature and allows applications in cosmetics where other types of collagen may be denatured because of their low denaturation temperature. Chicken type II collagen is well tolerated by patients with rheumatoid arthritis and is effective in the treatment of rheumatoid arthritis. Methionine‐restricted diet inhibits the growth of solid tumor such as gastric cancer, glioblastoma, medulloblastoma and neuroblastoma. Chicken type collagen may be a medical food for patients with solid tumors mentioned above.

show abstract

“…Ref. 40) knitted together by intra-and intermolecular covalent cross-link sites involving IDT. Furthermore, the related extensin RSH, required for cell plate orientation during cytokinesis (4), also contains numerous putative IDT motifs and a repetitive symmetry that, although not palindromic, should also favor similar close packing.…”

Section: Fig 4 Gel Permeation Assay Of Tyr Idt and The Unknown (Dmentioning

confidence: 99%

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

Held

Li²,

Kamyab³

et al. 2004

Journal of Biological Chemistry

108

129

View full text Add to dashboard Cite

Extensins are cell wall hydroxyproline-rich glycoproteins that form covalent networks putatively involving tyrosyl and lysyl residues in cross-links catalyzed by one or more extensin peroxidases. The precise cross-links remain to be chemically identified both as network components in muro and as enzymic products generated in vitro with native extensin monomers as substrates. However, some extensin monomers contain variations within their putative cross-linking motifs that complicate cross-link identification. Other simpler extensins are recalcitrant to isolation including the ubiquitous P3-type extensin whose major repetitive motif, Ser-(Hyp) 4 -Ser-Hyp-Ser-(Hyp) 4 -Tyr-Tyr-Tyr-Lys, is of particular interest, not least because its Tyr-Tyr-Tyr intramolecular isodityrosine cross-link motifs are also putative candidates for further intermolecular cross-linking to form di-isodityrosine. Therefore, we designed a set of extensin analogs encoding tandem repeats of the P3 motif, including Tyr 3 Phe and Lys 3 Leu variations. Expression of these P3 analogs in Nicotiana tabacum cells yielded glycoproteins with virtually all Pro residues hydroxylated and subsequently arabinosylated and with likely galactosylated Ser residues. This was consistent with earlier analyses of P3 glycopeptides isolated from cell wall digests and the predictions of the Hyp contiguity hypothesis. The tyrosine-rich P3 analogs also contained isodityrosine, formed in vivo. Significantly, these isodityrosine-containing analogs were further crosslinked in vitro by an extensin peroxidase to form the tetra-tyrosine intermolecular cross-link amino acid diisodityrosine. This is the first identification of an intermolecular cross-link amino acid in an extensin module and corroborates earlier suggestions that di-isodityrosine represents one mechanism for cross-linking extensins in muro.Hydroxyproline-rich glycoproteins (HRGPs), 1 which include the extensins, proline-rich proteins, and arabinogalactan proteins (AGPs), contribute to extracellular matrix architecture throughout the plant kingdom and the chlorophycean green algae (1-3). HRGPs are involved in all aspects of plant growth and development, including wall assembly during embryogenesis (4), and responses to biotic and abiotic stress that include mechanical stress (5), physical wounding (6), pathogenesis (7), and symbiosis (8 -10).HRGPs are extended macromolecules consisting of small repetitive peptide and glycopeptide motifs that form peptide modules and glycomodules of functional significance, as in "mix-and-match" mode they define the molecular properties of the overall macromolecule. The glycomodules result from a combination of post-translational modifications unique to plants, namely proline hydroxylation (11) and its subsequent glycosylation (12) that leads either to short arabino-oligosaccharide or larger arabinogalactan polysaccharide addition to the Hyp residues. A sequence-dependent O-Hyp glycosylation code directs the addition of oligosaccharide and polysaccharides (13), and it is likely that...

show abstract

Molecular Packing in Network-Forming Collagens

Cited by 20 publications

References 67 publications

Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host

Thermal Stability of Chicken Keel Bone Collagen

Di-isodityrosine Is the Intermolecular Cross-link of Isodityrosine-rich Extensin Analogs Cross-linked in Vitro

Contact Info

Product

Resources

About