Isolation and native characterization of cysteine-rich collagens from bovine placental tissues and uterus and their relationship to types IV and V collagens

1982 ◽  
Vol 2 (7) ◽  
pp. 493-502 ◽  
Author(s):  
M. Z. Abedin ◽  
Shirley Ayad ◽  
Jacqueline B. Weiss
Keyword(s):  
Type Iv Collagen ◽  
Deae Cellulose ◽  
Collagen Types ◽  
Type V Collagen ◽  
Type Iv ◽  
Probable Relationship ◽  
Simplified Procedure ◽  
Type V

A simplified procedure for the fractionation and purification of different collagen types from various tissues is described which is particularly efficient in separating type-V from type-IV collagen, and highmol.-wt. (HMW) aggregates from 7 S collagen. Uterus and maternal villi contain 2 forms of type-V collagen −{α1(V)}2α2(V) and {α1(V)2α2(V)α3(V)}–which have been separated on DEAE-cellulose. Uterus however appears to be the richest source of both HMW aggregates and the {α1(V)2α2(V)α3(V)} collagen, and a probable relationship between these collagens is discussed.

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.

scholarly journals Monoclonal antibodies against chicken type IV and V collagens: electron microscopic mapping of the epitopes after rotary shadowing.

1984 ◽  
Vol 98 (5) ◽  
pp. 1637-1644 ◽  
Author(s):  
R Mayne ◽  
H Wiedemann ◽  
M H Irwin ◽  
R D Sanderson ◽  
J M Fitch ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Monoclonal Antibodies ◽  
Cleavage Site ◽  
Type Iv Collagen ◽  
Collagen Molecule ◽  
Electron Microscopic ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V ◽  
Rotary Shadowing

The location of the epitopes for monoclonal antibodies against chicken type IV and type V collagens were directly determined in the electron microscope after rotary shadowing of antibody/collagen mixtures. Three monoclonal antibodies against type IV collagen were examined, each one of which was previously demonstrated to be specific for only one of the three pepsin-resistant fragments of the molecule. The three native fragments were designated (F1)2F2, F3, and 7S, and the antibodies that specifically recognize each fragment were called, respectively, IA8 , IIB12 , and ID2 . By electron microscopy, monoclonal antibody IA8 recognized an epitope located in the center of fragment (F1)2F2 and in tetramers of type IV collagen at a distance of 288 nm from the 7S domain, the region of overlap of four type IV molecules. Monoclonal antibody IIB12 , in contrast, recognized an epitope located only 73 nm from the 7S domain. This result therefore provides direct visual evidence that the F3 fragment is located closest to the 7S domain and the order of the fragments must be 7S-F3-(F1)2F2. The epitope for antibody ID2 was located in the overlap region of the 7S domain, and often several antibody molecules were observed to binding to a single 7S domain. The high frequency with which antibody molecules were observed to bind to fragments of type IV collagen suggests that there is a single population of type IV molecules of chain organization [alpha 1(IV)]2 alpha 2(IV), and that four identical molecules must form a tetramer that is joined in an antiparallel manner at the 7S domain. The monoclonal antibodies against type V collagen, called AB12 and DH2 , were both found to recognize epitopes close to one another, the epitopes being located 45-48 nm from one end of the type V collagen molecule. The significance of this result still remains uncertain, but suggests that this site is probably highly immunoreactive. It may also be related to the specific cleavage site of type V collagen by selected metalloproteinases and by alpha-thrombin. This cleavage site is also known to be located close to one end of the type V molecule.

scholarly journals Characterization of muscle epimysium, perimysium and endomysium collagens

1984 ◽  
Vol 219 (3) ◽  
pp. 1017-1026 ◽  
Author(s):  
N Light ◽  
A E Champion
Keyword(s):  
Connective Tissue ◽  
Sodium Dodecyl Sulphate ◽  
Type Iv Collagen ◽  
Sodium Dodecyl ◽  
Basement Membranes ◽  
Type Iii Collagen ◽  
Type I ◽  
Type V Collagen ◽  
Type Iv ◽  
Type V

In the past it has been proven difficult to separate and characterize collagen from muscle because of its relative paucity in this tissue. The present report presents a comprehensive methodology, combining methods previously described by McCollester [(1962) Biochim. Biophys. Acta 57, 427-437] and Laurent, Cockerill, McAnulty & Hastings [(1981) Anal. Biochem. 113, 301-312], in which the three major tracts of muscle connective tissue, the epimysium, perimysium and endomysium, may be prepared and separated from the bulk of muscle protein. Connective tissue thus prepared may be washed with salt and treated with pepsin to liberate soluble native collagen, or can be washed with sodium dodecyl sulphate to produce a very clean insoluble collagenous product. This latter type of preparation may be used for quantification of the ratio of the major genetic forms of collagen or for measurement of reducible cross-link content to give reproducible results. It was shown that both the epimysium and perimysium contain type I collagen as the major component and type III collagen as a minor component; perimysium also contained traces of type V collagen. The endomysium, the sheaths of individual muscle fibres, was shown to contain both type I and type III collagen as major components. Type V collagen was also present in small amounts, and type IV collagen, the collagenous component of basement membranes, was purified from endomysial preparations. This is the first biochemical demonstration of the presence of type IV collagen in muscle endomysium. The preparation was shown to be very similar to other type IV collagens from other basement membranes on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and was indistinguishable from EHS sarcoma collagen and placenta type IV collagen in the electron microscope after rotary shadowing.

Cell type specific recognition of the reconstituted aggregates from isolated type I collagen, type IV collagen, and type V collagen

1999 ◽  
Vol 111 (1) ◽  
pp. 171-177
Author(s):  
Toshihiko Hayashi ◽  
Kazunori Mizuno ◽  
Motohiro Hirose ◽  
Koichi Nakazato ◽  
Eijiro Adachi ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Type I Collagen ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Type I ◽  
Cell Type ◽  
Type V Collagen ◽  
Type Iv ◽  
Cell Type Specific ◽  
Type V

ChemInform Abstract: Cell Type Specific Recognition of the Reconstituted Aggregates from Isolated Type I Collagen, Type IV Collagen, and Type V Collagen

ChemInform ◽  
2010 ◽  
Vol 30 (30) ◽  
pp. no-no
Author(s):  
Toshihiko Hayashi ◽  
Kazunori Mizuno ◽  
Motohiro Hirose ◽  
Koichi Nakazato ◽  
Eijiro Adachi ◽  
...  
Keyword(s):  
Type Iv Collagen ◽  
Type I Collagen ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Type I ◽  
Cell Type ◽  
Type V Collagen ◽  
Type Iv ◽  
Cell Type Specific ◽  
Type V

Isolation and characterization of pepsin-solubilized human basement membrane (type IV) collagen peptides

Biochemistry ◽  
1983 ◽  
Vol 22 (21) ◽  
pp. 4940-4948 ◽  
Author(s):  
Robert S. MacWright ◽  
Virginia A. Benson ◽  
Katherine T. Lovello ◽  
Michel Van der Rest ◽  
Peter P. Fietzek
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Collagen Peptides ◽  
Type Iv ◽  
Isolation And Characterization ◽  
Membrane Type

viking: identification and characterization of a second type IV collagen in Drosophila

Gene ◽  
1997 ◽  
Vol 198 (1-2) ◽  
pp. 17-25 ◽  
Author(s):  
Sukkid Yasothornsrikul ◽  
Wendy J Davis ◽  
Gabrielle Cramer ◽  
Deborah A Kimbrell ◽  
Charles R Dearolf
Keyword(s):  
Type Iv Collagen ◽  
Type Iv ◽  
Identification And Characterization

scholarly journals Purification and characterization of type IV collagen from mouse kidney.

1986 ◽  
Vol 34 (2) ◽  
pp. 789-797 ◽  
Author(s):  
TSUTOMU OIKAWA ◽  
TAKAO IWAGUCHI ◽  
MIKIO KIMURA ◽  
AKIO MATSUZAWA
Keyword(s):  
Type Iv Collagen ◽  
Mouse Kidney ◽  
Purification And Characterization ◽  
Type Iv

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.

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