In vitro migration ofHydra nematocytes: The influence of the natural extracellular matrix (the mesoglea), of collagen type IV and type I, laminin, and fibronectin on cell attachment, migration parameters, and on patterns of cytoskeletal proteins

1991 ◽  
Vol 20 (3) ◽  
pp. 215-227 ◽  
Author(s):  
Charo Gonz�lez Agosti ◽  
Robert P. Stidwill
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Cell Attachment ◽  
Cytoskeletal Proteins ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv

scholarly journals Morphometric analysis of the human endoneurial extracellular matrix components during aging

2021 ◽  
Vol 73 (1) ◽  
pp. 103-110
Author(s):  
Braca Kundalic ◽  
Sladjana Ugrenovic ◽  
Ivan Jovanovic ◽  
Vladimir Petrovic ◽  
Aleksandar Petrovic ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Linear Regression Analysis ◽  
Collagen Type I ◽  
Nerve Fibers ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
Ecm Proteins ◽  
Extracellular Matrix Components

The aim of this study was to analyze the expression of extracellular matrix (ECM) proteins in human endoneurium during aging. We harvested 15 cadaveric sural nerves, distributed in 3 age groups (I: 25-44, II: 45-64, III: 65-86 years old). Histological sections were stained immunohistochemically for the presence of collagen type I, type IV and laminin, and the ImageJ processing program was used in morphometrical analysis to determine the percentages of these endoneurial proteins. In two younger groups, the endoneurial matrix of the sural nerve was composed from about equal proportions of these proteins, which may be considered a favorable microenvironment for the regeneration of nerve fibers. Linear regression analysis showed a significant increase in endoneurial collagen type IV with age, while collagen type I and laminin significantly decreased during the aging process. In cases older than 65 years, remodeling of the endoneurial matrix was observed to be significantly higher for the presence of collagen type IV, and lower for the expression of collagen type I and laminin. This age-related imbalance of ECM proteins could represent a disadvantageous microenvironment for nerve fiber regeneration in older adults. Our findings contribute to the development of therapeutic approaches for peripheral nerve regeneration.

scholarly journals Migration through the Extracellular Matrix by the Parasitic Protozoan Leishmania Is Enhanced by Surface Metalloprotease gp63

2003 ◽  
Vol 71 (2) ◽  
pp. 1008-1010 ◽  
Author(s):  
Bradford S. McGwire ◽  
Kwang-Poo Chang ◽  
David M. Engman
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Parasitic Protozoan ◽  
Type Iv ◽  
Extracellular Matrix Components ◽  
Matrix Components

ABSTRACT Leishmania species engineered to express high levels of the surface metalloprotease gp63 have enhanced capacity of migration through extracellular matrix in vitro. This correlates with gp63 degradation of extracellular matrix components, such as collagen type IV and fibronectin, and suggests an important role for gp63 in the pathogenesis of leishmaniasis.

scholarly journals Enterococcus faecalis Adhesin, Ace, Mediates Attachment to Extracellular Matrix Proteins Collagen Type IV and Laminin as well as Collagen Type I

2000 ◽  
Vol 68 (9) ◽  
pp. 5218-5224 ◽  
Author(s):  
Sreedhar R. Nallapareddy ◽  
Xiang Qin ◽  
George M. Weinstock ◽  
Magnus Höök ◽  
Barbara E. Murray
Keyword(s):  
Extracellular Matrix ◽  
Enterococcus Faecalis ◽  
Collagen Type ◽  
Collagen Type I ◽  
Immune Serum ◽  
Collagen Type Iv ◽  
Type I ◽  
Collagen Types ◽  
Type Iv ◽  
Ecm Proteins

ABSTRACT Adhesin-mediated binding to extracellular matrix (ECM) proteins is thought to be a crucial step in the pathogenic process of many bacterial infections. We have previously reported conditional adherence of most Enterococcus faecalis isolates, after growth at 46°C, to ECM proteins collagen types I and IV and laminin; identified an E. faecalis-specific gene, ace, whose encoded protein has characteristics of a bacterial adhesin; and implicated Ace in binding to collagen type I. In this study, we constructed an ace disruption mutant from E. faecalis strain OG1RF that showed marked reduction in adherence to collagen types I and IV and laminin when compared to the parental OG1RF strain after growth at 46°C. Polyclonal immune serum raised against the OG1RF-derived recombinant Ace A domain reacted with a single ∼105-kDa band of mutanolysin extracts from OG1RF grown at 46°C, while no band was detected in extracts from OG1RF grown at 37°C, nor from the OG1RF ace mutant grown at 37 or 46°C. IgGs purified from the anti-Ace A immune serum inhibited adherence of 46°C-grown E. faecalis OG1RF to immobilized collagen type IV and laminin as well as collagen type I, at a concentration as low as 1 μg/ml, and also inhibited the 46°C-evoked adherence of two clinical isolates tested. We also showed in vitro interaction of collagen type IV with Ace from OG1RF mutanolysin extracts on a far-Western blot. Binding of recombinant Ace A to immobilized collagen types I and IV and laminin was demonstrated in an enzyme-linked immunosorbent assay and was shown to be concentration dependent. These results indicate that Ace A mediates the conditional binding of E. faecalis OG1RF to collagen type IV and laminin in addition to collagen type I.

scholarly journals Schwann cells use a novel collagen-dependent mechanism for fibronectin fibril assembly

1998 ◽  
Vol 111 (18) ◽  
pp. 2763-2777 ◽  
Author(s):  
M.A. Chernousov ◽  
R.C. Stahl ◽  
D.J. Carey
Keyword(s):  
Extracellular Matrix ◽  
Schwann Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
The Matrix ◽  
Fibronectin Fibrils ◽  
Dependent Mechanism

Cultured rat Schwann cells were stimulated to deposit fibrillar extracellular matrix by treatment with ascorbic acid in the absence of nerve cells. Immunofluoresence staining of the matrix showed that it contains collagens types I and IV, fibronectin and perlecan but not laminin. Collagen type IV, fibronectin and perlecan co-distributed completely in the matrix fibrils, whereas collagen type I was present in only a subset of these fibrils. Time course studies indicated that collagen type I fibrils appear at late stages of matrix formation. Digestion of Schwann cell extracellular matrix with collagenase effectively disrupted most of the matrix including fibronectin fibrils. This was in contrast with fibroblasts, where collagenase treatment removed collagen with no visible effect on fibronectin fibrils. alpha5 integrin was expressed on the cell surface of Schwann cells and partially codistributed with fibronectin-containing fibrils. This suggests that the inability of Schwann cells to deposit fibronectin-containing matrix through a conventional, collagen-independent mechanism was not due to the lack of fibronectin-binding integrins on their cell surface. Polyclonal anti-fibronectin antibodies inhibited the deposition of fibronectin into the matrix fibrils, whereas collagen type IV fibrils were generally unaffected. Growth of Schwann cells on collagen type IV-coated substrate in the absence of ascorbate induced deposition of fine fibronectin fibrils. These results suggest that Schwann cells use an apparently novel, collagen type IV-dependent mechanism for the deposition of fibronectin into their extracellular matrix.

scholarly journals Expression and function of cell surface extracellular matrix receptors in mouse blastocyst attachment and outgrowth.

1988 ◽  
Vol 106 (4) ◽  
pp. 1331-1348 ◽  
Author(s):  
A E Sutherland ◽  
P G Calarco ◽  
C H Damsky
Keyword(s):  
Extracellular Matrix ◽  
Culture Medium ◽  
Cytoskeletal Proteins ◽  
Collagen Type Iv ◽  
Trophoblast Cells ◽  
Recognition Sequence ◽  
Type Iv ◽  
Extracellular Matrix Components ◽  
And Function

Mouse-hatched blastocysts cultured in vitro will attach and form outgrowths of trophoblast cells on appropriate substrates, providing a model for implantation. Immediately after hatching, the surfaces of blastocysts are quiescent and are not adhesive. Over the period 24-36 h post-hatching, blastocysts cultured in serum-free medium become adhesive and attach and spread on the extracellular matrix components fibronectin, laminin, and collagen type IV in a ligand specific manner. Attachment and trophoblast outgrowth on these substrates can be inhibited by addition to the culture medium of an antibody, anti-ECMr (anti-extracellular matrix receptor), that recognizes a group of 140-kD glycoproteins similar to those of the 140-kD extracellular matrix receptor complex (integrin) recognized in avian cells by CSAT and JG22 monoclonal antibodies. Addition to the culture medium of a synthetic peptide containing the Arg-Gly-Asp tripeptide cell recognition sequence of fibronectin inhibits trophoblast outgrowth on both laminin and fibronectin. However, the presence of the peptide does not affect attachment of the blastocysts to either ligand. Immunoprecipitation of 125I surface-labeled embryos using anti-ECMr reveals that antigens recognized by this antibody are exposed on the surfaces of embryos at a time when they are spreading on the substrate, but are not detectable immediately after hatching. Immunofluorescence experiments show that both the ECMr antigens and the cytoskeletal proteins vinculin and talin are enriched on the cell processes and ventral surfaces of trophectoderm cells in embryo outgrowths, in patterns similar to those seen in fibroblasts, and consistent with their role in adhesion of the trophoblast cells to the substratum.

scholarly journals Protein Truncating Variants of colA in Clostridium perfringens Type G Strains

2021 ◽  
Vol 11 ◽  
Author(s):  
Lore Van Damme ◽  
Natasja Cox ◽  
Chana Callens ◽  
Michelle Dargatz ◽  
Monika Flügel ◽  
...  
Keyword(s):  
Clostridium Perfringens ◽  
Collagen Type ◽  
Gelatin Zymography ◽  
Relative Activity ◽  
Full Length ◽  
Collagen Type Iv ◽  
Type I ◽  
Necrotic Enteritis ◽  
Variant Type ◽  
Type Iv

Extracellular matrix (ECM) degrading enzymes produced by Clostridium perfringens may play an important role during the initial phases of avian necrotic enteritis by facilitating toxin entry in the intestinal mucosa and destruction of the tissue. C. perfringens is known to produce several ECM-degrading proteases, such as kappa toxin, an extracellular collagenase that is encoded by the colA gene. In this study, the colA gene sequence of a collection of 48 C. perfringens strains, including pathogenic (i.e. toxinotype G) and commensal (i.e. toxinotype A) chicken derived strains and strains originating from other host species, was analyzed. Although the colA gene showed a high level of conservation (>96% nucleotide sequence identity), several gene variants carrying different nonsense mutations in the colA gene were identified, leading to the definition of four truncated collagenase variant types (I-IV). Collagenase variant types I, III and IV have a (nearly) complete collagenase unit but lack parts of the C-terminal recruitment domains, whereas collagenase variant types II misses the N-terminal part of collagenase unit. Gene fragments encoding a truncated collagenase were mainly linked with necrotic enteritis associated C. perfringens type G strains with collagenase variant types I and II being the most prevalent types. Gelatin zymography revealed that both recombinant full-length and variant type I collagenase have active auto-cleavage products. Moreover, both recombinant fragments were capable of degrading type I as well as type IV collagen, although variant type I collagenase showed a higher relative activity against collagen type IV as compared to full-length collagenase. Consequently, these smaller truncated collagenases might be able to break down collagen type IV in the epithelial basement membrane of the intestinal villi and so contribute to the initiation of the pathological process leading to necrotic enteritis.

Selective increase in the binding of the alpha 1 beta 1 integrin for collagen type IV during neurite outgrowth of human neuroblastoma TR 14 cells

1994 ◽  
Vol 107 (12) ◽  
pp. 3379-3392
Author(s):  
G. Carmeliet ◽  
B. Himpens ◽  
J.J. Cassiman
Keyword(s):  
Neurite Outgrowth ◽  
Collagen Type ◽  
Collagen Type I ◽  
Collagen Type Iv ◽  
Type I ◽  
Human Neuroblastoma ◽  
Specific Antibodies ◽  
Type Iv ◽  
Beta 1 Integrin ◽  
In Cells

Regulation of beta 1 integrins in neurite outgrowth following N6,2′-O-dibutyryladenosine 3′:5′-cyclic monophosphate (dBcAMP) treatment was investigated using the human neuroblastoma cell line TR 14. Three beta 1 integrins were identified: the alpha 1 beta 1 receptor bound collagen type I, collagen type IV and probably laminin; the alpha 2 beta 1 integrin bound collagen type I; and the alpha v beta i receptor bound fibronectin. Neurite extension was detectable as early as 30 minutes following dBcAMP treatment, was maximal after 24 hours and remained constant during treatment for 4 days. Adhesion-perturbing beta 1 subunit-specific antibodies, added together with dBcAMP, prevented the outgrowth of new neurites. During the first 24 hours of neurite outgrowth, no change was observed in the amount of beta 1 integrins nor in their topographic distribution. However, dBcAMP treatment increased the binding of alpha 1 beta 1 receptors to collagen type IV-Sepharose by a factor 2.3 +/- 0.6 (P < 0.02), while no alteration in the binding to collagen type I was detected. Moreover, neurites and growth cones were immunoreactive for collagen type IV but not for collagen type I. Consistently dBcAMP-induced neurite outgrowth was inhibited by adhesion-perturbing alpha 1 subunit-specific antibodies. Following maximal neurite outgrowth, the amount of beta 1 integrins determined by immunoprecipitation and by confocal microscopy decreased to 58.3 +/- 11.2% (P < 0.001) and to 55.4 +/- 17.5% (P < 0.001) of untreated levels, respectively, without any change in the level of beta 1 mRNA or de novo synthesized beta 1 precursor. However, pulse-chase experiments showed an increased turnover of the beta 1 subunit: the amount of beta 1 precursor that was degraded after 1 hour chase was 50.5 +/- 8.4% in cells treated for 4 days and 34.2 +/- 3.9% in untreated cells (P < 0.02); the amount of mature beta 1 after 24 hours chase was smaller in cells treated for 4 days compared to untreated cells. In conclusion, during neurite outgrowth, alpha 1 beta 1 integrins are required and acquire an enhanced binding activity for collagen type IV; but following maximal neurite outgrowth, expression of beta 1 integrins is reduced.

Serum enhancement of human endothelial cell attachment to and spreading on collagens I and IV does not require serum fibronectin or vitronectin

1990 ◽  
Vol 95 (2) ◽  
pp. 255-262
Author(s):  
W.D. Norris ◽  
J.G. Steele ◽  
G. Johnson ◽  
P.A. Underwood
Keyword(s):  
Endothelial Cell ◽  
Culture Medium ◽  
Type I Collagen ◽  
Cell Attachment ◽  
Cell Spreading ◽  
Human Endothelial Cell ◽  
Collagen Type Iv ◽  
Type I ◽  
Type Iv ◽  
Endothelial Cell Attachment

The initial attachment and spreading of endothelial cells from human umbilical artery onto type I collagen, type IV collagen or gelatin substrata was shown to be enhanced by inclusion of serum in the culture medium. To test whether this serum effect was mediated by adsorption of serum fibronectin or vitronectin onto the collagen, these adhesive glycoproteins were selectively removed from the serum prior to addition to the culture medium. The stimulatory effect of serum on human endothelial cell spreading on collagens I and IV was also observed with serum from which either fibronectin or vitronectin, or both, had been selectively removed. The stimulatory effect for cell spreading on gelatin was diminished by selective removal of serum fibronectin, but unaffected by removal of vitronectin. Human endothelial cell attachment and spreading onto tissue culture plastic was abolished by removal of vitronectin from the serum in the culture medium. These results emphasize that the native structure of collagens is required for serum-enhancement of human endothelial cell attachment and spreading on native collagen types I and IV, and show that on these substrata the stimulated adhesion and spreading are not dependent upon adsorption of serum fibronectin or vitronectin onto the collagen substratum.

scholarly journals Differential expression of parietal epithelial cell and podocyte extracellular matrix proteins in focal segmental glomerulosclerosis and diabetic nephropathy

2019 ◽  
Vol 317 (6) ◽  
pp. F1680-F1694 ◽  
Author(s):  
Gek Cher Chan ◽  
Diana G. Eng ◽  
Jeffrey H. Miner ◽  
Charles E. Alpers ◽  
Kelly Hudkins ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Diabetic Nephropathy ◽  
Epithelial Cell ◽  
Focal Segmental Glomerulosclerosis ◽  
Collagen Type ◽  
Collagen Type Iv ◽  
Type Iv ◽  
Ecm Proteins ◽  
Segmental Glomerulosclerosis ◽  
Parietal Epithelial Cell

In healthy glomeruli, parietal epithelial cell (PEC)-derived extracellular matrix (ECM) proteins include laminin-β1, perlecan, and collagen type IV-α2 and podocyte-specific ECM proteins include laminin-β2, agrin, and collagen type IV-α4. This study aimed to define individual ECM protein isoform expression by PECs in both experimental and human focal segmental glomerulosclerosis (FSGS) and diabetic nephropathy (DN) and to determine if changes were CD44 dependent. In experimental FSGS induced with a cytotoxic podocyte antibody and in the BTBR ob/ob mouse model of DN, PEC-derived protein staining was significantly increased in PECs. Dual staining also showed de novo expression of the podocyte-specific ECM proteins laminin-β2 and agrin in PECs. Similar findings were observed in biopsies from patients with FSGS and DN. Increases in individual ECM proteins colocalized with CD44 in PECs in disease. To determine the role of CD44, FSGS was induced in CD44−/− and CD44+/+ mice. PEC staining for perlecan, collagen type IV-α2, laminin-β2, and agrin were significantly lower in diseased CD44−/− mice compared with diseased CD44+/+ mice. These results show that in experimental and human FSGS and DN, PECs typically in an activated state, produce both PEC-derived and podocyte-specific ECM protein isoforms, and that the majority of these changes were dependent on CD44.

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