Immunolocalization of type III collagen and procollagen in cirrhotic human liver using monoclonal antibodies

1986 ◽  
Vol 409 (1) ◽  
pp. 37-46 ◽  
Author(s):  
Kooko Sakakibara ◽  
Akira Ooshima ◽  
Shogo Igarashi ◽  
Jo Sakakibara
Keyword(s):  
Monoclonal Antibodies ◽  
Human Liver ◽  
Type Iii Collagen ◽  
Type Iii

scholarly journals Multiple antigenic determinants on type III collagen

1991 ◽  
Vol 274 (3) ◽  
pp. 895-898 ◽  
Author(s):  
J A Werkmeister ◽  
J A M Ramshaw
Keyword(s):  
Monoclonal Antibodies ◽  
Connective Tissue ◽  
Tryptic Digestion ◽  
Antigenic Determinants ◽  
Type Iii Collagen ◽  
Collagen Types ◽  
Type Iii ◽  
Wide Range

Eight monoclonal antibodies have been produced against human pepsin-soluble type III collagen. All antibodies were shown to be highly specific for type III collagen and did not cross-react with a range of other collagen types or connective-tissue proteins. Examination of type III collagen from other species showed that these antibodies had a wide range of species specificities, indicating that several distinct epitopes were being recognized. The location of the epitopes was investigated by using reactivity of the antibodies to CNBr fragments and to sequential fragments formed by tryptic digestion of renaturing type III collagen. These data also indicated that several distinct epitopes were recognized and that they were located over the length of the type III collagen.

Repeated helical epitopes of defined amino acid sequence in human type III collagen identified by monoclonal antibodies

1992 ◽  
Vol 29 (6) ◽  
pp. 759-770 ◽  
Author(s):  
Hori Hisae ◽  
Douglas R. Keene ◽  
Lynn Y. Sakai ◽  
Mary K. Wirtz ◽  
Hans Peter Bächinger ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Human Type

Covalent structure of collagen: amino acid sequence of .alpha.1(III)-CB5 from type III collagen of human liver

Biochemistry ◽  
1980 ◽  
Vol 19 (8) ◽  
pp. 1583-1589 ◽  
Author(s):  
Jerome M. Seyer ◽  
Carlo Mainardi ◽  
Andrew H. Kang
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Liver ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Covalent Structure

Methionine-Specific Staining of Collagen

1982 ◽  
Vol 40 ◽  
pp. 294-295
Author(s):  
E.M. Kuhn ◽  
K.D. Marenus ◽  
M. Beer
Keyword(s):  
Amino Acids ◽  
Collagen Fibers ◽  
Type Iii Collagen ◽  
Type I ◽  
Electron Microscopic ◽  
Good Correspondence ◽  
Specific Staining ◽  
Type Iii ◽  
Different Types ◽  
Sulfur Containing

Fibers composed of different types of collagen cannot be differentiated by conventional electron microscopic stains. We are developing staining procedures aimed at identifying collagen fibers of different types.Pt(Gly-L-Met)Cl binds specifically to sulfur-containing amino acids. Different collagens have methionine (met) residues at somewhat different positions. A good correspondence has been reported between known met positions and Pt(GLM) bands in rat Type I SLS (collagen aggregates in which molecules lie adjacent to each other in exact register). We have confirmed this relationship in Type III collagen SLS (Fig. 1).

Structural Insights into the Glycine Pair Motifs in Type III Collagen

2017 ◽  
Vol 3 (3) ◽  
pp. 269-278
Author(s):  
Bo An ◽  
Shu-Wei Chang ◽  
Cody Hoop ◽  
Jean Baum ◽  
Markus J. Buehler ◽  
...  
Keyword(s):  
Type Iii Collagen ◽  
Type Iii ◽  
Structural Insights

scholarly journals Type III Collagen is Required for Adipogenesis and Actin Stress Fibre Formation in 3T3-L1 Preadipocytes

Biomolecules ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 156
Author(s):  
Mohammad Al Hasan ◽  
Patricia E. Martin ◽  
Xinhua Shu ◽  
Steven Patterson ◽  
Chris Bartholomew
Keyword(s):  
Quantitative Polymerase Chain Reaction ◽  
Type Iii Collagen ◽  
Type Iii ◽  
Actin Stress Fibre ◽  
Matrix Gene ◽  
Gene Transcripts ◽  
Polymerase Chain ◽  
Oil Red O Staining ◽  
Oil Red O

GPR56 is required for the adipogenesis of preadipocytes, and the role of one of its ligands, type III collagen (ColIII), was investigated here. ColIII expression was examined by reverse transcription quantitative polymerase chain reaction, immunoblotting and immunostaining, and its function investigated by knockdown and genome editing in 3T3-L1 cells. Adipogenesis was assessed by oil red O staining of neutral cell lipids and production of established marker and regulator proteins. siRNA-mediated knockdown significantly reduced Col3a1 transcripts, ColIII protein and lipid accumulation in 3T3-L1 differentiating cells. Col3a1−/− 3T3-L1 genome-edited cell lines abolished adipogenesis, demonstrated by a dramatic reduction in adipogenic moderators: Pparγ2 (88%) and C/ebpα (96%) as well as markers aP2 (93%) and oil red O staining (80%). Col3a1−/− 3T3-L1 cells displayed reduced cell adhesion, sustained active β-catenin and deregulation of fibronectin (Fn) and collagen (Col4a1, Col6a1) extracellular matrix gene transcripts. Col3a1−/− 3T3-L1 cells also had dramatically reduced actin stress fibres. We conclude that ColIII is required for 3T3-L1 preadipocyte adipogenesis as well as the formation of actin stress fibres. The phenotype of Col3a1−/− 3T3-L1 cells is very similar to that of Gpr56−/− 3T3-L1 cells, suggesting a functional relationship between ColIII and Gpr56 in preadipocytes.

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