Cellular and extracellular involvement in the regeneration of the rat lower vibrissa follicle

Development ◽  
1992 ◽  
Vol 114 (4) ◽  
pp. 887-897 ◽  
Author(s):  
C.A. Jahoda ◽  
K.A. Horne ◽  
A. Mauger ◽  
S. Bard ◽  
P. Sengel
Keyword(s):  
Basement Membrane ◽  
Hair Follicle ◽  
Wound Repair ◽  
Type Iv Collagen ◽  
Initial Response ◽  
Type Iv ◽  
Sequence Of Events ◽  
Papilla Formation ◽  
Wound Reaction ◽  
Dermal Cells

The sequence of events leading to the reconstruction of a fibre-producing hair follicle, after microsurgical amputation of the lower follicle bulb, has been detailed by immunohistology and electron microscopy. The initial response was essentially found to be a wound reaction, in that hyperproliferative follicle epidermis quickly spread to below the level of amputation—associated with downward movement of mesenchymal (or dermal) sheath cells. Fibronectin was prominent in both dermis and epidermis at this stage and, as in wound repair, preceded laminin and type IV collagen in covering the lower dermal-epidermal junction. Once a new basal line of epidermis and a complete basement membrane were established, laminin and type IV collagen were detected below this junction and within the prospective papilla-forming mesenchyme. This coincided with ultrastructural observations of profuse sub-basement membrane extracellular material in the region of new papilla formation. The glassy membrane displayed extensive ultrastructural modifications at its lower level, and these corresponded with localized variations in staining intensities for all three antibodies over time. The membrane hung below the level of the epidermis, and was crossed by migrating cells from the mesenchymal dermal sheath of the follicle - it acted to segregate the inner group of follicular dermal cells from wound fibroblasts. Extracellular matrix may be a mediator of the dermal-epidermal interactions associated with this hair follicle regeneration phenomenon.

Induction of follicle formation and hair growth by vibrissa dermal papillae implanted into rat ear wounds: vibrissa-type fibres are specified

Development ◽  
1992 ◽  
Vol 115 (4) ◽  
pp. 1103-1109 ◽  
Author(s):  
C.A. Jahoda
Keyword(s):  
Basement Membrane ◽  
Hair Follicle ◽  
Fibre Type ◽  
Immunohistochemical Staining ◽  
Hair Growth ◽  
Type Iv Collagen ◽  
Adult Rat ◽  
Type Iv ◽  
Wound Epidermis ◽  
Dermal Papillae

Adult vibrissa follicle dermal papillae have the capacity to induce hair growth and follicle formation when associated with epidermis from various sources. However, the range of conditions under which hair follicle induction will take place has not been established. The question of whether or not the adult papilla carries information to impose fibre-type specificity has also not been fully answered. This study describes how the implantation of isolated papillae into small incisional cuts on the rat ear pinna resulted in the subsequent emergence of abnormally large hair fibres from the wound sites. Many of these hairs were found to display vibrissa-type characteristics. Histological observations indicated that the papillae had interacted with the edges of the wound epidermis to produce new, and particularly large follicles, while immunohistochemical staining revealed that early follicle construction was accompanied by a profusion of the basement membrane constituents laminin and type IV collagen in the subjacent dermis. These findings show that adult rat papillae retain the capacity, as displayed by embryonic dermis, to determine vibrissa specificity in induced follicles.

scholarly journals Dynamically remodeled hepatic extracellular matrix predicts prognosis of early-stage cirrhosis

2021 ◽  
Vol 12 (2) ◽  
Author(s):  
Yuexin Wu ◽  
Yuyan Cao ◽  
Keren Xu ◽  
Yue Zhu ◽  
Yuemei Qiao ◽  
...  
Keyword(s):  
Liver Cirrhosis ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Patient Survival ◽  
Early Stage ◽  
Ecm Remodeling ◽  
Type Iv ◽  
Ecm Proteins ◽  
Stage Disease ◽  
Cirrhotic Patients

AbstractLiver cirrhosis remains major health problem. Despite the progress in diagnosis of asymptomatic early-stage cirrhosis, prognostic biomarkers are needed to identify cirrhotic patients at high risk developing advanced stage disease. Liver cirrhosis is the result of deregulated wound healing and is featured by aberrant extracellular matrix (ECM) remodeling. However, it is not comprehensively understood how ECM is dynamically remodeled in the progressive development of liver cirrhosis. It is yet unknown whether ECM signature is of predictive value in determining prognosis of early-stage liver cirrhosis. In this study, we systematically analyzed proteomics of decellularized hepatic matrix and identified four unique clusters of ECM proteins at tissue damage/inflammation, transitional ECM remodeling or fibrogenesis stage in carbon tetrachloride-induced liver fibrosis. In particular, basement membrane (BM) was heavily deposited at the fibrogenesis stage. BM component minor type IV collagen α5 chain expression was increased in activated hepatic stellate cells. Knockout of minor type IV collagen α5 chain ameliorated liver fibrosis by hampering hepatic stellate cell activation and promoting hepatocyte proliferation. ECM signatures were differentially enriched in the biopsies of good and poor prognosis early-stage liver cirrhosis patients. Clusters of ECM proteins responsible for homeostatic remodeling and tissue fibrogenesis, as well as basement membrane signature were significantly associated with disease progression and patient survival. In particular, a 14-gene signature consisting of basement membrane proteins is potent in predicting disease progression and patient survival. Thus, the ECM signatures are potential prognostic biomarkers to identify cirrhotic patients at high risk developing advanced stage disease.

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

Basement Membrane Laminin and Type IV Collagen in Endometrial Adenocarcinoma: Relation to Differentiation and Treatment

Oncology ◽  
1985 ◽  
Vol 42 (6) ◽  
pp. 370-376 ◽  
Author(s):  
Frej Stenbäck ◽  
Juha Risteli ◽  
Leila Risteli ◽  
Veli-Matti Wasenius
Keyword(s):  
Basement Membrane ◽  
Type Iv Collagen ◽  
Endometrial Adenocarcinoma ◽  
Type Iv

Co-operation between metastatic tumor cells and macrophages in the degradation of basement membrane (type IV) collagen

FEBS Letters ◽  
1983 ◽  
Vol 161 (2) ◽  
pp. 243-246 ◽  
Author(s):  
Nicole Henry ◽  
Yves Eeckhout ◽  
Anne-Louise van Lamsweerde ◽  
Gilbert Vaes
Keyword(s):  
Basement Membrane ◽  
Tumor Cells ◽  
Type Iv Collagen ◽  
Metastatic Tumor ◽  
Type Iv ◽  
Membrane Type

scholarly journals Identification of a multifunctional, cell-binding peptide sequence from the a1(NC1) of type IV collagen.

1990 ◽  
Vol 111 (4) ◽  
pp. 1583-1591 ◽  
Author(s):  
E C Tsilibary ◽  
L A Reger ◽  
A M Vogel ◽  
G G Koliakos ◽  
S S Anderson ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Basement Membrane ◽  
Type Iv Collagen ◽  
Solid Phase ◽  
Peptide Sequence ◽  
Cell Binding ◽  
Type Iv ◽  
Specific Manner ◽  
Dose Dependent ◽  
Nc1 Domain

We have previously identified three distinctive amino acid sequences from type IV collagen which specifically bound to heparin and also inhibited the binding of heparin to intact type IV collagen. One of these chemically synthesized domains, peptide Hep-I, has the sequence TAGSCLRKFSTM and originates from the a1(noncollagenous [NC1]) chain of type IV collagen (Koliakos, G. G., K. K. Koliakos, L. T. Furcht, L. A. Reger, and E. C. Tsilibary. 1989. J. Biol. Chem. 264:2313-2323). We describe in this report that this same peptide also bound to intact type IV collagen in solid-phase assays, in a dose-dependent and specific manner. Interactions between peptide Hep-I and type IV collagen in solution resulted in inhibition of the assembly process of this basement membrane glycoprotein. Therefore, peptide Hep-I should represent a major recognition site in type IV collagen when this protein polymerizes to form a network. In addition, solid phase-immobilized peptide Hep-I was able to promote the adhesion and spreading of bovine aortic endothelial cells. When present in solution, peptide Hep-I competed for the binding of these cells to type IV collagen- and NC1 domain-coated substrata in a dose-dependent manner. Furthermore, radiolabeled peptide Hep-I in solution also bound to endothelial cells in a dose-dependent and specific manner. The binding of radiolabeled Hep-I to endothelial cells could be inhibited by an excess of unlabeled peptide. Finally, in the presence of heparin or chondroitin/dermatan sulfate glycosaminoglycan side chains, the binding of endothelial cells to peptide Hep-I and NC1 domain-coated substrates was also inhibited. We conclude that peptide Hep-I should have a number of functions. The role of this type IV collagen-derived sequence in such diverse phenomena as self-association, heparin binding and cell binding and adhesion makes Hep-I a crucial domain involved in the determination of basement membrane ultrastructure and cellular interactions with type IV collagen-containing matrices.

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