Glycoproteins on the surface of smooth muscle cells involved in their interaction with type V collagen

1985 ◽  
Vol 63 (11) ◽  
pp. 1176-1182 ◽  
Author(s):  
James R. A. Leushner ◽  
M. Daria Haust
Keyword(s):  
Protein Synthesis ◽  
Cyanogen Bromide ◽  
Attachment Site ◽  
Membrane Glycoproteins ◽  
Type V Collagen ◽  
Attachment Region ◽  
A Cell ◽  
Type V ◽  
In Vitro Interaction

Type V collagen is a major component of the pericellular coat of smooth cells (SMC). The purpose of the present study was to assess biochemically the nature of an in vitro interaction between bovine aortic SMC and type V collagen from the same source. This interaction was originally shown to be mediated by a cell-surface glycoconjugate. Data obtained in the present study suggests that the binding system consists of integral membrane glycoproteins which act alone or in combination with a surface glycolipid in type V attachment. The nature of this system was indicated by the finding of 80 000 and 50 000 components in the plasma membrane fractions which were specifically retained by type V collagen – Sepharose columns and incorporated both methionine and mannose label. Moreover, inhibition of protein synthesis lowered SMC attachment by 25%. The mannose label associated with these components was probably in the form of a simple oligosaccharide at the attachment site since it bound to concanavalinA (ConA) and was sensitive to endoglycosidase H. Iodinated ConA labelling indicated elevated levels of these components were associated with SMC – type V collagen interaction. The attachment region on the type V molecule was localized within the cyanogen bromide peptide 6 of the α2 (V) chain.

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.

scholarly journals Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11, and enhancement of F11-mediated neurite outgrowth by tenascin-R.

1995 ◽  
Vol 130 (2) ◽  
pp. 473-484 ◽  
Author(s):  
U Nörenberg ◽  
M Hubert ◽  
T Brümmendorf ◽  
A Tárnok ◽  
F G Rathjen
Keyword(s):  
Neurite Outgrowth ◽  
Cell Attachment ◽  
Attachment Site ◽  
Direct Interaction ◽  
Bacterial Cells ◽  
Fibronectin Type Iii ◽  
Attachment Region ◽  
A Cell ◽  
Function Relationship

The extracellular matrix glycoprotein tenascin-R (TN-R) is a multidomain protein implicated in neural cell adhesion. To analyze the structure-function relationship of the different domains of TN-R, several recombinant TN-R fragments were expressed in bacterial cells. Two distinct binding regions were localized on the TN-R polypeptide: a region binding the axon-associated immunoglobulin (Ig)-like F11 protein and a cell attachment site. The binding region of the glycosylphosphatidylinositol (GPI)-anchored F11 was allocated to the second and third fibronectin type III (FNIII)-like domain within TN-R. By using a mutant polypeptide of F11 containing only Ig-like domains, a direct interaction between the Ig-like domains of F11 and FNIII-like domains 2-3 of TN-R was demonstrated. The interaction of TN-R with F11 in in vitro cultures enhanced F11-mediated neurite outgrowth, suggesting that the combined action of F11 and TN-R might be of regulatory influence on axon extension. A cell attachment region was identified in the FNIII-like domain eight of TN-R by domain-specific antibodies and fusion constructs. This site is distinct from the F11 binding site within TN-R.

Use of an in Vitro Protein Synthesizing System to Test the Mode of Action of Chloracetamides

Weed Science ◽  
1980 ◽  
Vol 28 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Luanne M. Deal ◽  
J. T. Reeves ◽  
B. A. Larkins ◽  
F. D. Hess
Keyword(s):  
Protein Synthesis ◽  
Sand Culture ◽  
Leucine Incorporation ◽  
Insoluble Protein ◽  
In Vitro System ◽  
A Cell ◽  
Protein Incorporation ◽  
Vitro Protein

The effects of chloracetamides on protein synthesis were studied both in vivo and in vitro. Four chloracetamide herbicides, alachlor [2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide], metolachlor [2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)acetamide], CDAA (N–N-diallyl-2-chloroacetamide), and propachlor (2-chloro-N-isopropylacetanilide) were tested for inhibition of [3H]-leucine incorporation into protein. Incorporation of3H-leucine into trichloroacetic acid (TCA)-insoluble protein was inhibited in oat (Avena sativaL. ‘Victory’) seedlings grown in sand culture and treated 12 h at 1 × 10−4M with these chloracetamides. The herbicides were also tested in a cell-free protein synthesizing system containing polyribosomes purified from oat root cytoplasm. These herbicides had no effect on the rates of polypeptide elongation nor on the synthesis of specific polypeptides when herbicides (1 × 10−4M) were added directly to the system. Polypeptide formation was inhibited 89% when 1 × 10−4M cycloheximide was added during translation. Cytoplasmic polyribosomes were isolated from oat roots treated 12 h with 1 × 10−4M herbicide. Translation rates and products were not altered when these polyribosomes were added to the in vitro system. Protein synthesis is inhibited when tested in an in vivo system; however, the inhibition does not occur during the translation of mRNA into protein.

In Vitro Removal of Ochratoxin A by Wine Lactic Acid Bacteria

2007 ◽  
Vol 70 (9) ◽  
pp. 2155-2160 ◽  
Author(s):  
VINCENZO DEL PRETE ◽  
HECTOR RODRIGUEZ ◽  
ALFONSO V. CARRASCOSA ◽  
BLANCA de las RIVAS ◽  
EMILIA GARCIA-MORUNO ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Ochratoxin A ◽  
High Performance ◽  
Culture Medium ◽  
Degradation Products ◽  
Cell Binding ◽  
A Cell ◽  
In Vitro Interaction

A study was carried out to determine the in vitro interaction between ochratoxin A (OTA) and wine lactic acid bacteria (LAB). Fifteen strains belonging to five relevant oenological LAB species were grown in liquid synthetic culture medium containing OTA. The portion of OTA removed during the bacterial growth was 8 to 28%. The OTA removed from the supernatants was partially recovered (31 to 57%) from the bacterial pellet. Cell-free extracts of three representative strains were produced by disrupting cells in a French pressure cell. The ability of crude cell-free extracts to degrade OTA was studied. OTA was not degraded by cell-free extracts of wine LAB strains, and no degradation products of OTA were detected in the high-performance liquid chromatograms of the methanol extract of the bacterial pellet. On the basis of these results, we conclude that OTA removal by wine LAB is a cell-binding phenomenon. The chemistry and the molecular basis of OTA binding to wine LAB remains unknown.

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

1990 ◽  
Vol 95 (4) ◽  
pp. 649-657 ◽  
Author(s):  
D.E. Birk ◽  
J.M. Fitch ◽  
J.P. Babiarz ◽  
K.J. Doane ◽  
T.F. Linsenmayer
Keyword(s):  
Type I Collagen ◽  
Small Diameter ◽  
Collagen Molecule ◽  
Type I ◽  
Collagen Types ◽  
Type V Collagen ◽  
Amino Terminal ◽  
Type V ◽  
Fibril Diameter

The small-diameter fibrils of the chick corneal stroma are heterotypic, composed of both collagen types I and V. This tissue has a high concentration of type V collagen relative to other type I-containing tissues with larger-diameter fibrils, suggesting that heterotypic interactions may have a regulatory role in the control of fibril diameter. The interactions of collagen types I and V were studied using an in vitro self-assembly system. Collagens were purified from lathyritic chick embryos in the presence of protease inhibitors. The type V collagen preparations contained higher molecular weight forms of the alpha 1(V) and alpha 2(V) chains constituting 60–70% of the total. Rotary-shadow electron micrographs showed a persistence of a small, pepsin-sensitive terminal region in an amount consistent with that seen by electrophoresis. In vitro, this purified type V collagen formed thin fibrils with no apparent periodicity, while type I collagen fibrils had a broad distribution of large diameters. However, when type I collagen was mixed with increasing amounts of type V collagen a progressive and significant decrease in both the mean fibril diameter and the variance was observed for D periodic fibrils. The amino-terminal domain of the type V collagen molecule was required for this regulatory effect and in its absence little diameter reducing activity was observed. Electron microscopy using collagen type-specific monoclonal antibodies demonstrated that the fibrils formed were heterotypic, containing both collagen types I and V. These data indicate that the interaction of type V with type I collagen is one mechanism modulating fibril diameter and is at least partially responsible for the regulation of collagen fibril formation.

scholarly journals Directed Evolution of Proteins throughIn VitroProtein Synthesis in Liposomes

2012 ◽  
Vol 2012 ◽  
pp. 1-11 ◽  
Author(s):  
Takehiro Nishikawa ◽  
Takeshi Sunami ◽  
Tomoaki Matsuura ◽  
Tetsuya Yomo
Keyword(s):  
Protein Synthesis ◽  
Directed Evolution ◽  
Single Copy ◽  
Functional Evaluation ◽  
Future Directions ◽  
Pure System ◽  
Protein Functions ◽  
A Cell ◽  
Evolution Of Proteins

Directed evolution of proteins is a technique used to modify protein functions through “Darwinian selection.”In vitrocompartmentalization (IVC) is anin vitrogene screening system for directed evolution of proteins. IVC establishes the link between genetic information (genotype) and the protein translated from the information (phenotype), which is essential for all directed evolution methods, by encapsulating both in a nonliving microcompartment. Herein, we introduce a new liposome-based IVC system consisting of a liposome, the protein synthesis using recombinant elements (PURE) system and a fluorescence-activated cell sorter (FACS) used as a microcompartment,in vitroprotein synthesis system, and high-throughput screen, respectively. Liposome-based IVC is characterized byin vitroprotein synthesis from a single copy of a gene in a cell-sized unilamellar liposome and quantitative functional evaluation of the synthesized proteins. Examples of liposome-based IVC for screening proteins such as GFP andβ-glucuronidase are described. We discuss the future directions for this method and its applications.

scholarly journals Synthesis of type V collagen by chick corneal fibroblasts in vivo and in vitro

FEBS Letters ◽  
1980 ◽  
Vol 115 (1) ◽  
pp. 101-104 ◽  
Author(s):  
Antonia Pöschl ◽  
Klaus Von Der Mark
Keyword(s):  
Type V Collagen ◽  
Corneal Fibroblasts ◽  
Type V

Effect of trna from 5-azacytidine-treated hamster fibrosarcoma cells on protein synthesis in vitro in a cell-free system

1976 ◽  
Vol 25 (4) ◽  
pp. 389-392 ◽  
Author(s):  
Richard L. Momparler ◽  
Stuart Siegel ◽  
Felicidad Avila ◽  
Thomas Lee ◽  
Myron Karon
Keyword(s):  
Protein Synthesis ◽  
Free System ◽  
Cell Free System ◽  
Fibrosarcoma Cells ◽  
A Cell ◽  
Hamster Fibrosarcoma

scholarly journals Characterization of the Type 3 Fimbrial Adhesins ofKlebsiella Strains

1998 ◽  
Vol 66 (6) ◽  
pp. 2887-2894 ◽  
Author(s):  
Tricia A. Schurtz Sebghati ◽  
Timo K. Korhonen ◽  
Douglas B. Hornick ◽  
Steven Clegg
Keyword(s):  
Basement Membranes ◽  
Collagen Types ◽  
Type V Collagen ◽  
Type Iv ◽  
Fimbrial Adhesins ◽  
Type V ◽  
Type 3 ◽  
Fimbrial Adhesin

ABSTRACT The Klebsiella pneumoniae fimbrial adhesin, MrkD, mediates adherence to the basolateral surfaces of renal and pulmonary epithelia and to the basement membranes of tissues. Although all isolates possessing the MrkD adhesin mediate the agglutination, in vitro, of erythrocytes treated with tannic acid, the mrkDgene is not conserved within species. The ability of a plasmid-bornemrkD gene product to mediate binding to type V collagen is associated frequently with strains of K. oxytoca and rarely with strains of K. pneumoniae. In K. pneumoniae, the MrkD adhesin is located within a chromosomally borne gene cluster and mediates binding to collagen types IV and V. The plasmid-borne determinant, mrkD 1P, and the chromosomally borne gene, mrkD 1C, are not genetically related. Some strains of enterobacteria possess amrkD 1C allele that is associated with hemagglutinating activity but does not bind to either type IV or type V collagen.

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